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FOOD CHEMISTRY
DONGFENG WANG
HONG LIN
JIANQIAN KAN
LINWEI LIU
XIAOXING ZENG
AND
SHENGRONG SHEN
EDITORS
New York
CONTENTS
Preface
vii
Contributors
ix
xi
Chapter 1
Introduction
Dongfeng Wang
Chapter 2
Water
Jianqian Kan and Guoqing Huang
Chapter 3
Carbohydrates
Dongfeng Wang, Jipeng Sun, Guoqing Huang,
Xiaolin Zhou and Liping Sun
Chapter 4
Lipids
Shengrong Shen, Dongfeng Wang and Undurti N. Das
107
Chapter 5
Proteins
Hong Lin, Lisha Wu and Shuhui Wang
137
Chapter 6
Vitamins
Yibin Zhou, Dongfeng Wang and Ping Dong
191
Chapter 7
Minerals
Dongfeng Wang, Lina Yu, Haiyan Li, Bin Zhang,
Shuhui Wang and Xingguo Liang
223
Chapter 8
Food Flavors
Xiaoxiong Zeng and Guaoqing Huang
247
Chapter 9
Food Additives
Linwei Liu and Shiyuan Dong
273
Chapter 10
Toxicants in Foods
Wang Dongfeng, Guoqing Huang and Shuhui Wang
305
Index
35
353
PREFACE
Foods consist of a large quantity of compounds, of which, some are original from plant or
animal materials, some are new ones generated during processing or preservation, some are
intentionally added by manufacturers, and some are contaminants produced during
processing, preservation or packaging. These compounds undergo various changes during
processing and storage and it is hence necessary to understand the effects of processing or
storage on these compounds so as to enhance the nutrition, palatability and safety of foods.
The purpose of Food Chemistry is to elucidate the structure, physicochemical properties,
nutrition and safety of major food constituents and their changes occurred during processing
and storage. Due to the extreme importance, Food Chemistry has been accepted as a major
fundamental course for food-related majors.
Though food chemistry has a history of more than 200 years, it developed into a
relatively independent system in the late 1960s. Since then, the United States, Japan,
Germany and other countries published several authoritative food chemistry textbooks,
including Latest Food Chemistry edited by Hayashi Junzo and Kitamura Mitsuo (Japan),
Food Chemistry by Sakurai Yoshito (Japan), Food Chemistry by Owen R. Fennema (United
States), Food Chemistry by Belitz HD (Germany), Food Chemistry by Zhang Wang (China),
and Food Chemistry by Dongfeng Wang (China). Of the works, the publications edited by
Fennema and Belitz HD have been widely chosen by university students as textbook.
However, the two books contain too many contents and part of them overlaps with those
stated in Biochemistry and Organic Chemistry. Besides, the two books are too expensive for
readers in developing countries.
Hence, there is an urgent demand to publish a simplified Food Chemistry textbook that
most university students can afford, which is the case of this book. This book presents the
chemistry and properties of the six essential nutrients contained in foods, including water,
carbohydrates, lipids, proteins, vitamins and minerals, and their changes occurred during food
processing and storage. In addition, this book also deals with the chemistry and properties of
flavors, food additives and toxic substances in foods. This book is simplified and cheaper
than previously published books without reducing its academic level, and reflects the latest
advances in food chemistry. This work can be used as a textbook by university students and
especially suitable for students in developing countries and non-English speaking countries
for bilingual delivery.
The authors would like to thank the postgraduates of the Laboratory of Food Chemistry
and Nutrition of Ocean University of China, including Mei Ding, Yan Li, Lu Yu, Xingya Li,
viii
Xiang Gao, Wen Zhou, Zhe Xu, Min Wang, Mengqi Li, and Chunsheng Li, for assistance in
literature collection and typesetting, and Ocean University of China for funding the
publication.
CONTRIBUTORS
Undurti N Das
Jawaharlal Nehru Technological University, Kakinada-533 003, India
Liping Sun
College of Chemistry and Engineering, Kunming University of Science and Technology,
Yunnan Province, China
Jipeng Sun
Third Institute of Oceanography State Oceanic Administration, Xiamen, China
Lina Yu
Shandong Peanut Research Institute, Qingdao, China
Xiaoling Zhou
Medical College of Shantou University, Shantou, Guangdong Province, China
Bin Zhang
School of Food and Pharmacy & Medical School, Zhejiang Ocean University, Zhushang
City, Zhejiang Province, China
Haiyan Li
College of Food Science and Engineering, Ocean University of China, Qingdao, China
Banping Wang
College of Food Science and Engineering, Ocean University of China, Qingdao, China
Xingguo Liang
College of Food Science and Engineering, Ocean University of China, Qingdao, China
xii
degree of food science from Northwest Agriculture & Forest University (ShaanXi, China) in
1995.
Hong Lin received the BS degree in 1984, the MS degree in 1990, and the PhD degree
in 1998 in seafood science from the Ocean University of China. Professor Lin is a famous
expert in the seafood safety field and his research area covers novel marine organism-derived
chemical and biological hazard discovery, quality control during seafood processing, and fast
hazard detection method development. Professor Lin has been granted 4 invention patents,
published more than 100 original articles, and edited 4 academic books, including Seafood
Safety (2010), Aquatic Nutrition and Safety (2007), Effective Use of Aquatic Resources
(2007), and Fish Preservation Technologies (2000).
Xiaoxiong Zeng received the BS degree from Hunan Agricultural University in 1985,
the MS degree from Zhejiang Agricultural University in 1988, and the PhD degree from
Shizuoka University (Shizuoka, Japan) in 2000. Dr. Zeng is now a professor of the College of
Food Science and Technology, Nanjing Agricultural University, China. He is one of the
authors or corresponding author of over 100 original papers related to food chemistry, food
biotechnology and glycobiology.
Shengrong Shen is a professor of the School of Biosystems Engineering and Food
Science of Zhejiang University. Professor Shen was granted the PhD degree by the
Department of Biophysics of Zhejiang University in 1997. His research area includes
structural analysis of such bioactive compounds as lipids, fatty acids, and polyphenols. He
has published more than 100 original papers concerning food chemistry, food safety and
applied nutrition in the latest 10 years. Besides, professor Shen has published 5 academic
books related to food and health, tea biochemistry and food chemistry.
Yibin Zhou is a professor of the Department of Food Science and Engineering at Anhui
Agricultural University, Anhui, China. He had edited Food Chemistry (in Chinese) as an
assistant, and is the author or corresponding author of over 40 original papers on
carbohydrates, food engineering, and biotechnology.
Guoqing Huang is a lecturer of the College of Food Science and Engineering, Qingdao
Agricultural University, Qingdao, China.
Shiyuan Dong is a lecturer of the College of Food Science and Engineering, Ocean
University of China, Qingdao, China.
Shuhui Wang is a PhD candidate in Biosystems Engineering Department College of
Agriculture - Ginn College of Engineering, Aubum University, Auburn, AL 36849-5417,
USA
ISBN: 978-1-61942-125-7
2012 Nova Science Publishers, Inc.
Chapter 1
INTRODUCTION
Dongfeng Wang
College of Food Science and Engineering, Ocean University of China, Qingdao, China
ABSTRACT
Food Chemistry is a fundamental discipline for students, engineers, and
professionals engaged in the food industry. This chapter provides an overview of this
discipline, including its definition, purpose, development, and its role in food science and
engineering.
Dongfeng Wang
food. The purpose of Food Chemistry is to elucidate the structure, physical and chemical
properties, nutritional value as well as safety of these components, their changes undergone
during storage and processing, and the effects of these changes on food nutrition and
palatability. The knowledge is of great importance in improving food quality, developing new
food resources, evolving food processing and storage technologies, upgrading food packaging
materials, and increasing food safety and quality.
Natural
Water
Carbohydrates
Proteins
Lipids
Minerals
Vitamins
Pigments
Hormones
Flavor components
Toxic substances
Food components
Natural additives
Food Addtives
Synthetic additives
Unnatural
From processing
Contaminants
From environmental pollution
Introduction
As the trading of foods between regions and countries increased, both consumers and
manufacturers had urgent needs on the information of water contents and the presence nonfood components in foods. Meanwhile, driven by the rapid development of analysis measures,
the desire to understand the natural characteristic of foods also grew. In 1860, German
scholars Hanneberg W. and Stohman F. invented a method for the simultaneous
determination of water, crude fat, ash, and nitrogen contents. Several years later, diets
containing solely proteins, lipids, and carbohydrates were found insufficient for maintaining
life.
In 1900s, with the advancement of analytical techniques and the biochemistry subject and
the rapid development of the food industry, requirements on new food processing
technologies and prolonged storage life emerged, which drove the quick development of food
chemistry. During this period, a growing number of researches papers were published and the
quantity of related journals increased significantly as well, including Archives of Biochemistry
and Biophysics (initiated in 1942), Journal of Agricultural and Food Chemistry (initiated in
1953) and Food Chemistry (initiated in 1966). Due to the emergency of increasing deep and
systematic publications, Food Chemistry gradually developed into an independent subject.
Chinese scholars Yanbin Xia and Ruijin Yang divide the history of Food Chemistry into
four stages.
Stage one: Many natural components were separated from plants and animals and were
identified, including lactic acid, citric acid, malic acid, and tartaric acid. The knowledge was
not systematic yet and was reported mainly by chemists.
Stage two: In the early 1900s (1820 ~ 1850), food chemistry developed quickly along
with the development of agricultural chemistry and gained much importance in Europe.
Specialized food chemistry laboratories were established and many professional journals
related to food chemistry were issued. Meanwhile, adulteration became a serious issue and
the need for impurity determination propelled the development of food chemistry. In this
stage, Justus von Liebig invented an optimized method for quantitative analysis of organic
substances and published Researches on the Chemistry of Food in 1847.
Stage three: In the middle 1900s century, the British scientist Arthur Hill Hassall reported
the microscopic images of pure and adulterated foods and food chemistry came into the
microanalysis time. In 1871, Jean Baptis M.D.M. proposed that diets containing only
proteins, carbohydrates and lipids were insufficient to sustain humans life. The interests on
the nutritional requirements further accelerated the development of food chemistry. Until the
first half of the 20th century, the majority of components in foods were identified and the
number of literatures related to chemistry food increased markedly. Food chemistry then
turned to be a mature and independent subject in mid-20th century.
Stage four: Food chemistry is now in the fourth stage. With the rapid development of
society, economy, science and technology, and the improvement of living standards,
consumers raise higher requirements on food security, nutrition, palatability, and
convenience. Meanwhile, to realize the transformation from traditional to scaled,
standardized, and modernized processing of foods, more and more new technologies,
materials, and equipment are used, which markedly drive the rapid development of food
chemistry. Besides, the advancement of basic chemistry, biochemistry, instrumental analysis
and other related subjects guarantee the rapid development of food chemistry. Food chemistry
has become a most important subject for food scientists [1, 2].
Dongfeng Wang
Application
Flour improving; starch modification; new edible materials exploitation;
high-fructose syrup; food enzymes; molecular basis of food nutrition; new
sweetener and natural additive development; new oligosaccharide
production; oil modification; vegetable protein isolates; functional peptides
production; microbial polysaccharides and single cell protein development;
development and utilization of wild, marine, an edible drug resources, etc.
Chemical peeling; color protection; texture control; vitamin retention; deastringency and debittering; coating and waxing; chemical preservation;
controlled atmosphere storage; bioactive packaging; enzyme-assisted
juicing, filtration and clarification; chemical preservation, etc.
Introduction
Beverage
industry
Dairy industry
Baking
industry
Edible oils
and fats
industry
Condiments
industry
Fermented
food industry
Food safety
Food
inspection
Application
Post-slaughter processing; juice preservation and tenderization; color
protection and development; enhancement of the emulsifying capacity,
gelling capacity, and viscoelasticity of meat; frozen denaturation of
proteins; fresh meat packaging in supermarket; production and application
of fumigation agent; artificial meat production; comprehensive utilization of
viscera, etc
Instant dissolution; ingredient floating and/or sinking inhibition; protein
beverage stabilization; water treatment; juice stabilization; juice color
protection; flavor enhancement; alcohol degree decrease; beer clarification;
beer foamability and bitterness improvement; chemical nature and
prevention of beer non-biological stability; off-flavor elimination; juice deastringency; soybean odor elimination, etc.
Yoghurt and juice milk stabilization; chymosin substitute development;
whey utilization; nutrition fortification of diary products; etc.
High-efficiency leavening agent development; crispness improvement;
bread color and texture modification; aging and mildewing inhibition; etc.
Lipid refinement; lipid modification; development and utilization of DHA,
EPA, and MCT; food emulsifier and anti-oxidant development; oil
absorption reduction of fried foods; etc.
Meat soup production; nucleotide-type flavor enhancers; organic iodinesupplemented salt; etc.
Post-processing of fermented foods; flavor changes during postfermentation; comprehensive utilization of biomass and residues; etc.
Source identification of exogenous toxicants and their prevention;
identification of endogenous toxicants and their elimination; etc
Formulation of inspection standards; rapid analysis; biosensor development;
fingerprint preparation of products; etc.
Due to the rapid development of food chemistry, some important reactions, including the
Millard reaction, caramelization, lipid auto-oxidation, starch gelatinization and aging,
polysaccharide hydrolysis and modification, protein hydrolysis and denaturation, pigment
discoloration, vitamin degradation, metal-catalyzed reactions, enzyme-catalyzed reactions, fat
hydrolysis and transesterification, lipid thermo-oxidative decomposition and polymerization,
flavor compound changes, action mechanisms of food additives, generation of harmful
ingredients as well as postharvest physiology, are identified in foods. The knowledge on these
reactions greatly enhances the development of the food industry.
1.2.2. Role of Food Chemistry in Human Nutrition and Health
It has been more than two centuries since proteins, carbohydrates and lipids were
identified as the three major nutrients for human. The two most important attributes of foods
are to provide consumers with nutrition and sensory satisfaction. One of the objectives of
food chemistry is to investigate the nutrition and flavor composition in food materials and
processed foods and the interactions of the components occurred during processing and
storage and effects of these interactions on food nutrition and palatability. The modern food
Dongfeng Wang
chemistry should not only ensure the healthcare and enjoyment attributes of food
components, but also guide consumers on rational diet selection. The concept of nutrition has
evolved significantly due to social development and the change of the healthy status of
consumers. How to reduce the incidences of diet-related diseases, such as cardiocerebrovascular diseases, cancers, and diabetes, has turned to be a new major task of food
industry. In addition to the healthcare attribute, foods should also provide desirable flavors so
that consumers enjoy the eating process. The emergence of biotechnologies and new food
processing technologies guarantees the safety of foods.
Contamination of foods by pollutants is currently a worldwide concern due to global
environmental deterioration. The analysis and identification of trace and ultramicro
substances are of vital importance to the nutrition value and the control of toxicants of foods.
The development of food chemistry has been associated with the healthy status and
civilization level of human.
Introduction
Table 1-2. Part reactions occurred during food processing and storage and their
influences on foods [3, 4]
Reaction
Nonenzymic
browning
Oxidation
Hydrolysis
Isomerization
Polymerization
Protein
denaturation
Examples
Color development in
bakery foods
Oxidation of lipids,
vitamins, an phenols
Hydrolysis of lipids,
proteins, and carbohydrates
Influence on foods
Desired or undesired color, smell, taste; loss of
nutrition; harmful ingredients.
Change color; desired flavor or off-odors and
toxicants
Increased soluble solids content; texture
changes; desired color, flavor, taste, and
nutrition; toxicity loss of certain components
cis-trans isomerization of
lipids
Foam and insoluble brown
precipitate forming in
frying
Egg white coagulation;
enzyme inactivation
The research fruits and methods of food chemistry have been widely absorbed by the
food industry and greatly promote the development of the food industry. In the last decades,
some new subjects and research areas, such as structural chemistry, free radical chemistry,
membrane separation, edible package, microencapsulation, extrusion, superfine comminution,
bioactive packaging, supercritical extraction, molecular distillation, membrane catalysis, bioreactor, toxicant chemistry of foods, molecular nutrition, and nutria-genomics, have been
established. These new technologies and subjects will undoubtedly facilitate the rapid
development of the food industry, which in turn benefits the improvement of the food
chemistry subject.
REFERENCES
[1]
[2]
[3]
[4]
Wang, DF. Food Chemistry.1st edition. Beijing: Chemistry Industry Press; 2007
Damodaran, S; Parkin, KL; Fennema, OR. Fennemas Food Chemistry. 4th edition.
New York: CRC Press; 2007.
Kan, JQ. Food Chemistry. 1st edition. Beijing: China Agricultural University Press;
2002.
Wang, Z. Food Chemistry. 1st edition. Beijing: China Light Industry Press; 2005.
ISBN: 978-1-61942-125-7
2012 Nova Science Publishers, Inc.
Chapter 2
WATER
1
ABSTRACT
Water is an important component in many foods. Its content and occurrence status
significantly affect the flavor, texture, and stability of foods. This chapter deals with the
various physical and chemical properties of water and ice and the interactions with other
components in foods. Water occurs in multiple states due to interactions with solutes and
the interactions significantly affect the bioavailability of water to chemical reactions and
microorganisms.
To distinguish the differences between water content and its bioavailability, the term
water activity (aw) is proposed and its application in food stability predication are
detailed. The relationship between water content and aw can be presented by moisture
sorption isotherm (MSI), which is very useful in designing the concentration and
dehydration processes of foods.
In addition to aw, molecular mobility (Mm) has also been proposed to predict food
stability. Its definition and its effect on food stability are also a concern of this chapter.
Water is a predominant constituent in many foods (Table 1). Water in proper amount,
location, and orientation profoundly influences the structure, appearance, and taste of
foods and their susceptibility to spoilage.
Because medium water supports chemical reactions and water is a reactant in
hydrolytic processes, the removal of water from foods retards many reactions and inhibits
the growth of microorganisms, thus improving the shelf lives of a number of foods.
Through physical interaction with proteins, polysaccharides, lipids and salts, water
contributes significantly to food texture.
Water is essential to life: as an important governor of body temperature, as a solvent,
as a carrier of nutrients and waste products, as a reactant and reaction medium, as a
lubricant and plasticizer, as a stabilizer of biopolymer conformation, as a likely facilitator
of the dynamic behavior of macromolecules, including their catalytic (enzymatic)
properties, and in other ways yet unknown.
10
Water content
(%)
53~60
50~70
Food
Water content
(%)
10~13
20
65~81
bananas
75
80~85
Cereal flour
Honey
Avocado, bananas, peas
(green)
Beets, broccoli, carrots,
potatoes
Asparagus, beans
(green), cabbage,
cauliflower, lettuce
Bread
85~90
Biscuits
3~8
90~95
Tea
3~7
15
4
Edible oil
74
74~80
80~85
90~95
35~45
Figure 1. Schematic model of a single HOH molecule: (a) sp3 configuration, and (b) van der Waals radii
for a HOH molecule in the vapor state [1].
Water
11
In the vapor state, the bond angle of an isolated water molecule is 104.5. The O-H
internuclear distance is 0.96 and the van der Waals radii for oxygen and hydrogen are 1.40
and 1.2 respectively.
Figure 2 Hydrogen bonding of water molecules in a tetrahedral configuration. Open circles are oxygen
atoms and closed circles are hydrogen atoms. Hydrogen bonds are represented by dashed lines [1].
12
Ice (0C)
Water (1.5C)
Water (83C)
Coordination number
4.0
4.4
4.9
O-HO Distance
0.276 nm
0.290 nm
0.305 nm
Table 3. Comparisons of the melting and boiling points of methanol, dimethyl ether, and
water
Formula
H2O
CH3OH
CH3OCH3
Fp/C
0.0
-98
-138
Kp/C
100.0
64.7
-23
Water
13
Figure 4. Unit cell of ordinary ice at 0C. Circles represent oxygen atoms of water molecules. Nearestneighbor internuclear O-O distance is 2.76 ; is 109 [3].
14
Figure 5. Likely arrangement of water molecules adjacent to sodium chloride. Only water molecules in
plane of paper are shown [3].
Water
15
Figure 8. Hydrogen bonding (dotted lines) of water to two kinds of functional groups occurring in
proteins [3].
Figure 9. Examples of a three-molecule water bridge in papain; 23, 24, and 25 are water molecules [4].
16
Figure 10. Schematic depiction of a globular protein undergoing hydrophobic interaction. Open circles
are hydrophobic groups, L-shaped entities around circles are water molecules oriented in accordance
with a hydrophobic surface, and dots represent water molecules associated with polar groups [2].
Water
17
18
Bound water
Occurs in vicinity of solutes and other
nonaqueous constituents and includes
constitution water, monolayer water,
and multilayer water
Not frozen even at temperatures lower
than -40C
Bulk water
Locates far away
from solutes and
occurs as water-water
hydrogen bonding
Slightly lower than
that of pure water
None
Yes
Changed slightly
Increased
ca. 96%
3. WATER ACTIVITY
Intensive researches have indicated that no relationship can be established between the
water content of a food with its physiochemical properties or stability. It has also been
19
Water
observed that various types of foods with the same water content differ significantly in
perishability. Thus, water content alone is not a reliable indicator of perishability. This
situation is attributable, in part, to differences in the intensity with which water associates
with nonaqueous constituents. The term water activity (aw) was developed to account for
the intensity with which water associates with various nonaqueous constituents. Experience
shows that food stability, safety, and other properties can be predicted far more reliably from
aw than from water content.
P
P0
RVP
ERH
100
(1)
where, RVP is the relative vapor pressure; P is the partial vapor pressure of food moisture at
temperature T; P0 is the saturation vapor pressure of pure water at temperature T, and ERH is
the equilibrium relative humidity at temperature T.
Equation (1) applies only to ideal solutions and thermodynamically equilibrium systems
and the values obtained are only approximate for food systems. The RVP of a food can be
determined by placing it in a closed chamber for a time sufficient to achieve apparent
equilibrium (constant weight) and then measuring either pressure or relative humidity in the
chamber. The vapor pressures of the aqueous solution of solutes are generally lower than that
of pure water and aw hence falls in the range 0~1.
H
R
(3)
where, T is the absolute temperature, R is the gas constant, and H is the isosteric net heat of
sorption at the water content of the sample.
By rearrangement, equation (2-4) can be obtained:
Inaw
H
R
1
T
(4)
where, R and T have the same meaning as those in Equation (2-3), H is the latent heat of
vaporization of pure water (40.5372kJ/mol), and k is calculated from the following formula:
20
k
Plots of Inaw versus 1/T are not always linear over broad temperature ranges, and they
generally exhibit sharp breaks with the onset of ice formation. Figure 11. is a plot of logaw
versus 1/T, illustrating that (a) the relationship is linear at subfreezing temperatures, (b) the
influence of temperature on RVP is typically far greater at subfreezing temperatures than at
above-freezing temperatures, and (c) a sharp break occurs in the plot at the freezing point of
the sample. Below freezing temperatures, the water activity (aw) can be calculated as follow:
aw
p ff
pice
p0 ( SCW )
p0 ( SCW )
(5)
where, pff is the partial pressure of water in partially frozen food, p0(SCW) is the vapor pressure
of pure supercooled water, and pice is the vapor pressure of pure ice.
Two important distinctions should be noted when comparing aw values at above- and
below-freezing temperatures. First, at above-freezing temperatures, aw is a function of sample
composition and temperature, with the former factor predominating. At subfreezing
temperatures, aw becomes independent of sample composition and depends solely on
temperature; that is, in the presence of an ice phase aw values are not influenced by the kind
or ratio of solutes present. Hence, the knowledge of aw at a subfreezing temperature cannot be
used to predict aw at an above-freezing temperature. Second, as the temperature is changed
sufficiently to form or melt ice, the meaning of aw, in terms of food stability, also changes.
For example, in a product at -15C (aw =0.86), microorganisms will not grow and chemical
reactions will occur slowly. However, at 20C and aw 0.86, some chemical reactions will
occur rapidly and some microorganisms will grow at moderate rates.
Figure 11. Relationship between relative vapor pressure and temperature for a complex food above and
below freezing [5].
Water
21
Figure 12. Schematic moisture sorption isotherm encompassing a broad range of moisture contents [3].
22
Figure 13. Generalized moisture sorption isotherm for the low-moisture segment of a food (20C) [3].
Figure 14. Resorption isotherms for various foods and biological substances. Temperature 20C, except
for number 1, which is 40C: (1) confection (main component powdered sucrose), (2) spray-dried
chicory extract, (3) roasted Columbian coffee, (4) pig pancreas extract powder, (5) native rice starch
[6].
The MSI can be prepared in two ways. For high-moisture foods, the desorption isotherm
can be obtained by plotting the water content versus aw during dehydration. For low-moisture
foods, the resorption isotherm can be determined by plotting water content versus aw during
addition of water to the foods. The shape and position of the isotherm are determined by
several factors including sample composition, physical structure of the sample (e.g.,
crystalline or amorphous), sample pretreatments, temperature, and methodology
To deeply understanding the meaning and usefulness of sorption isotherms it is
sometimes appropriate to divide them into three zones as indicated in Figure 13.
Water
23
(1) Water present in Zone I of the isotherm is most strongly absorbed and least mobile.
This water associates with accessible polar sites by water-ion or water-dipole
interactions, is unfreezable at -40C, has no ability to dissolve solutes, and is not
present in sufficient amount to have a plasticizing effect on the solid. It behaves
simply as part of the solid. The high-moisture end of Zone I (boundary of Zones I
and II) corresponds to the Brunauer-Emmett-Teller (BET) monolayer moisture
content of the food. Zone I water constitutes a tiny fraction of the total water in a
high-moisture food material.
(2) Water added in Zone II occupies first-layer sites that are still available. This water
associates with neighboring water molecules and solute molecules primarily by
hydrogen bonding, is slightly less mobile than bulk water, and most of it is
unfreezable at -40C, it exerts a significant plasticizing action on solutes, lowers their
glass transition temperatures, and causes incipient swelling of the solid matrix, leads
to acceleration in the rate of most reactions. Water in Zones I and Zone II usually
constitutes less than 5% of the water in a high-moisture food material.
(3) Further addition of water (Zone III) causes a glass-rubber transition in samples
containing glassy regions, a very large decrease in viscosity, a very large increase in
molecular mobility, and commensurate increases in the rates of many reactions. This
water is freezable, available as a solvent, and readily supports the growth of
microorganism. Zone III water is referred to as bulk-phase water. The bulk-phase
water of Zone III, either entrapped or free, usually constitutes more than 95% of the
total water in a high-moisture food.
24
Range
of aw
Inhibited Microorganisms
1.000.95
Pseudomonas, Escherichia
Proteus, Shigella, Klebsiella,
Bacillus, Clostridium
perfringens, some yeasts
0.950.91
Salmonella, Vibrio
parahaemolyticus, C.
botulinum, Serratia,
Lactobacillus, some molds,
yeasts (Rhodotorula, Pichia)
0.910.87
0.870.80
0.800.75
0.750.65
0.650.60
0.50
No microbial proliferation
0.40
No microbial proliferation
0.30
No microbial proliferation
0.20
No microbial proliferation
Water
25
Figure 16. Relationships among relative water vapor pressure, food stability and sorption isotherms. (A)
Microbial growth versus p/p0. (B) Enzymatic hydrolysis versus p/p0. (C) Oxidation (nonenzymatic)
versus p/p0. (D) Maillard browning versus p/p0. (E) Miscellaneous reaction rates versus p/p0. (F) Water
content versus p/p0. All ordinates are relative rate except for F [3].
26
5.2. Water Activity (aw) and Chemical and Enzymatic Reactions in Foods
The relationship between water activity and the rates of chemical and enzymatic reactions
is very complex. First, water is a reactant of many chemical and enzymatic reactions and its
content significantly influences the balance of the reactions. Second, water can bind to polar
or ionic groups through hydration and significantly affects their contact with other reactants.
Third, many biomolecules swell in the presence of water and more reaction sites are exposed,
leading to accelerated reaction. However, high water contents dilute solutes and retard the
proceeding of reactions.
As shown in Figure 16, all chemical and enzymatic reactions, except oxidation reactions,
have the lowest reaction rates at the boundary of Zone I and Zone II, corresponding aw
0.2~0.3.
27
Water
aw
m(1 - aw )
1
m1c
c 1
m1c
(10)
where, aw is water activity, m is water content (in g H2O/g dry matter), m1 is the BET
monolayer value, and c is a constant.
From this equation, it is apparent that a plot of versus aw, known as a BET plot, should
yield a straight line. An example for native potato starch, with aw replaced by p/p0, is shown
in Figure 17. The linear relationship, as is generally acknowledged, begins to deteriorate at
p/p0 values greater than about 0.35.
The BET monolayer value can be calculated as follows:
1
(y intercept) (slope)
(11)
From Figure 17, the y intercept is 0.6. Calculation of the slope from Figure 17 yields a
value of 10.7. Thus,
m1
1
0.6 10.7
In this particular instance, the BET monolayer value corresponds to a aw, of 0.2.
28
Figure 17. BET plot for native potato starch (resorption data, 20C) [8].
Water
29
components during storage that are related to the stability and processability and includes:
molecular movement or deformation caused by liquid movement or mechanical stretch;
Brownian movements or atomic rotation caused by molecular diffusion; relative movement of
materials in containers or pipelines. Some properties and behavioral characteristics of food
that are dependent on Mm are shown in Table 7. Mm is mainly influenced by hydration and
temperature. The water content and the interaction between water and nonaqueous
components determine the fluidity of the liquid phase. As temperature is increased, the
translational and rotational motion (Mm) becomes easier, while upon cooling to Tg,
translational motion of polymer segments stop.
Frozen foods
Moisture migration (ice crystallization,
formation of in-package ice)
Lactose crystallization (sandiness in frozen
desserts)
Enzymatic activity
Structural collapse of amorphous phase
during sublimation phase of freeze-drying
Shrinkage (partial collapse of foam-like
frozen desserts)
30
Figure 19. State diagram of a binary system. Assumptions: maximal freeze concentration, no solute
crystallization, constant pressure, no time dependence. Tml is the melting point curve, TE is the eutectic
point, Tms is the solubility curve, Tg is the glass transition curve, and Tgis the solute-specific glass
transition temperature of a maximally freeze concentrated solution. Heavy dashed lines represent
conditions of metastable equilibrium. All other lines represent conditions of equilibrium [1].
Most foods are so complex that they cannot be accurately or easily represented on a state
diagram. Differential scanning calorimetry (DSC) can successfully determine the glass
transition temperature (Tg) of simple polymer systems, but is inapplicable to complex food
systems. The Tg of complex food systems is often determined by using dynamic mechanical
analysis (DMA) or dynamic mechanical thermal analysis (DMTA).
Glass transition temperature (Tg) is the temperature at which a supersaturated solution
(amorphous liquid) converts to a glass, and is dependent on solute type and water content. Tg
is a special Tg that applies only to samples containing ice, and only when ice has been formed
so maximum freeze-concentration occurs (very slow cooling). Below Tg or Tg of a complex
sample, all but small molecules lose their translational mobility while retaining limited
rotational and vibrational mobility.
In the glassy state, the food will have greater stability (shelf life). As long as the
temperature remain below Tg, the composition of the system is virtually fixed. This implies
physical stability: crystallization, for instance, will not occur. But some chemical reactions
may still proceed, albeit very slowly because of the high viscosity and the low temperature.
Water
31
approach is of questionable value or is clearly unsuitable. Some examples are (1) chemical
reactions whose rates are not strongly influenced by diffusion, (2) desirable or undesirable
effects achieved through the action of specific chemicals (e.g., alteration of pH or oxygen
tension), (3) situations in which sample Mm is estimated on the basis of a polymeric
component (Tg of polymer) and where Mm of small molecules that can penetrate the polymer
matrix is a primary determinant of the product attribute of interest, and (4) growth of
vegetative cells of microorganisms (p/p0 is a more reliable estimator than Mm). Examples of
diffusion-limited reactions are proton transfer reactions, radical recombination reactions,
acid-base reactions involving transport of H+ and OH-, many enzyme-catalyzed reactions,
protein folding reactions, polymer chain growth, and oxygenation/deoxygenation of
hemoglobin and myoglobin. At constant temperature and pressure, three primary factors
govern the rate at which a chemical reaction will occur: a diffusion factor, D (to sustain a
reaction, reactants must first encounter each other), a frequency-of-collision factor, A
(number of collisions per unit time following an encounter), and a chemical activation-energy
factor, Ea (once a collision occurs between properly oriented reactants the energy available
must be sufficient to cause a reaction, that is, the activation energy for the reaction must be
exceeded). For a reaction to be diffusion-limited, it is clear that factors A and Ea must not be
rate-limiting. Diffusion-limited reactions typically have low activation energies (825
kJ/mol). When a food is cooled and/or reduced in moisture content so that all or part of it is
converted to a glassy state, Mm is greatly reduced and diffusion-limited properties become
stable.
32
It should be noted that the plasticizing effect is valid only when water gets entrapped in
the amorphous region of the components. In the absence of environmental effects, moisture
content is the predominant factor that affects Tg, especially in low-moisture foods.
Table 8. Relationship between the Tg and moisture content of pre-gelatinized starch and
wheat starch
Pre-gelatinized starch
Moisture content
Tg/C
0.153
62
0.166
53
0.181
40
0.222
28
0.247
25
For example, the Tg of the anhydrous mixture of 50% starch and 50% sucrose is about
60C; when the moisture content increases to 2%, the Tg decreases to 20C; when the
moisture content further increases to 6%, Tg falls to as low as 10C. Table 8. lists the
relationships between the Tg and moisture content of native wheat starch and pre-gelatinized
starch. It could be seen that the Tg of both the materials increases along the decrease of
moisture content.
33
Water
Table 9. Tg of maltodextrin with different Des
DE5
Moisture content
0.00
0.02
0.04
0.11
0.18
Tg/C
188
135
102
44
23
DE10
Moisture content
0.00
0.02
0.05
0.10
0.19
Tg/C
160
103
84
30
-6
DE15
Moisture content
0.00
0.02
0.05
0.11
0.20
Tg/C
99
83
65
8
-13
Figure 25. Relationship between average molecular weight and dextrose equivalent (DE) of commercial
starch hydrolysis products with Tg [10].
34
ice-free foods. Because aw can be measured conveniently and quickly, it is still the major
indicator for judging food stability.
REFERENCES
Fennema, OR. Food Chemistry. 3rd edition. New York: Marcel Dekker; 1996.
Damodaran, S; Parkin, KL; Fennema, OR. Fennemas Food Chemistry. 4th edition.
New York: CRC Press; 2007.
[3] Belitz, HD; Gorsch, W. Food Chemistry. 2nd edition. Berlin: Springer-Verlag, 1999.
[4] Berendsen, HJC. Specific interactions of water with biopolymers. In: Franks, F. Water A Comprehensive Treatise. New York: Plenum Press, 1975; 293-349.
[5] Fennema, OR. Enzyme kinetics at low temperature and reduced water activity. In:
Crowe, JH; Clegg, JS. Dry Biological Systems. New York: Academic Press, 1978; 297322.
[6] Ferry, JD. The evaluation of water activity in aqueous solutions from freezing point
depression. International Journal of Food Technology, 1980, 16, 21-30.
[7] Beuchat, LR. Microbial stability as affected by water activity. Cereal Foods World,
1981, 26, 345-349.
[8] Van den Berg, C. Vapour Sorption Equilibria and Other Water-Starch Interactions; A
Physico-Chemical Approach, PhD thesis, Wageningen: Wageningen Agricultural
University, 1981.
[9] Slade, L; Levine, H. Beyond water activity: Recent advances based on an alternate
approach to the assessment of food quality and safety. Critical Reviews in Food Science
and Nutrition. 1991, 30, 115360.
[10] Levine, H., and L. Slade (1986). A polymer physico-chemical approach to the study of
commercial starch hydrolysis products (SHPs). Carbohydrate Polymers, 6, 213244.
[1]
[2]
ISBN: 978-1-61942-125-7
2012 Nova Science Publishers, Inc.
Chapter 3
CARBOHYDRATES
ABSTRACT
Carbohydrates account for 3/4 of the dry weight of terrestrial plants and algae and
can be found in all the plants, animals and microorganisms that human can eat.
Carbohydrates are one of the major components in foods. The compounds not only
provide human beings with energy, but also impart foods with desired textures and tastes.
Carbohydrates undergo various changes during food processing and storage and yield
substantial compounds that affect the flavor, quality and safety of foods. This chapter
deals with the classification of carbohydrates and their most important functional
properties, in which, special attention is paid to the non-enzymatic browning reaction, its
influences on food quality, and its control. The structures, proportions, and applications
of most important polysaccharides and oligosaccharides in foods are then detailed one by
one. Dietary fiber as an important healthy diet component is also introduced at the end of
this chapter.
36
INTRODUCTION
Carbohydrates Classification
Carbohydrates are natural organic compounds converted from carbon dioxide and water
through photosynthesis of plants. According to the number of monosaccharide units,
carbohydrates are divided into monosaccharides, oligosaccharides and polysaccharides.
Monosaccharides are the simplest sugars in structure and can no longer be hydrolyzed. A
monosaccharide often contains three, four, five, or six carbon atoms and its functional group
might be the aldehyde or keto group. An oligosaccharide generally consists of 2 to 20
monosaccharide units and can be hydrolyzed to simple sugars. Oligosaccharides are often
found in glycoproteins or lipopolysaccharides. According to monosaccharide composition,
oligosaccharides are further divided into homo-oligosaccharides and hetero-oligosaccharides.
A homo-oligosaccharide is composed of only one type of monosaccharide, such as maltose
and dextrin with degree of polymerization less than 20. In contrast, a hetero-oligosaccharide
consists of two or more types of monosaccharide units. Polysaccharides, with degree of
polymerization greater than 20, are formed by dehydration of multiple monosaccharide units
and consist of homo-polysaccharides, such as cellulose and starch, and hetero-polysaccharide
such as seaweed and tea polysaccharides. Polysaccharides can also be classified into plant,
animal and microbial polysaccharides according to their origins or storage and functional
polysaccharides according to their biological functions.
Polysaccharides contain multiple hydroxyl groups and can covalently attach to the side
chains of proteins or peptides to form glycoproteins or protein polysaccharides.
Polysaccharides also react with carboxyl-containing molecules to form esters such as
lipopolysaccharide (LPS) and sulfate polysaccharides. Besides, polysaccharides can complex
with transition metals due to the presence of hydroxyl groups. These polysaccharide
derivatives are generally referred to as polysaccharide complexes.
Carbohydrates in Foods
Starch is one of the most abundant carbohydrates in plant-derived foods and is the most
abundant in seeds, roots and tubers. Glycogen is found in animal-derived foods especially in
muscle and liver, and it is structurally similar to amylopectin. Starch is insoluble in aqueous
solutions and does not contribute to the sweetness of foods, unless it was hydrolyzed into
oligosaccharides or glucose.
The majority of plant-derived foods contain only a small amount of free sugars and most
sugars are present as starch. For example, maize contains only 0.2%~0.5% D-glucose,
0.1%~0.4% D-fructose and 1%~2% sucrose. Free sugars not only provide the sweet taste for
foods, but also participate in flavor and color formation during thermal processing. An
increase in free sugar content during processing improves food quality. For example, to
increase the sweetness of sweet corn, sweet corn must be harvested before sugars are
converted to starch.
Many fruits are often harvested before they are fully mature for two reasons. Firstly, the
high rigidity of immature fruits facilitates their transport and storage. Secondly, starch is
Carbohydrates
37
converted to sucrose or other sweet sugars during transport and storage. This change makes
the fruits sweet and soft. The post-harvest ripening is the reverse of the starch synthesis
process in the grain, tuber and root of plants.
The contents of water-soluble sugars in processed foods are generally higher than the
corresponding materials, because sugars are intentionally added by manufacturers to meet the
requirements of consumers on flavor and color.
38
39
Carbohydrates
Sugar alcohols have lower calorific values and are sweeter than their monosaccharide
precursors. Sugar alcohols do not undergo the typical reactions of sugars and are stable
against heating and pH variations. Sugar alcohols share the same chemical properties as
common alcohols and are not involved in the Maillard reaction.
Inositol is a cyclic hexatomic alcohol and has 9 stereoisomers (Table 3-1), of which, 7 are
mesomeric and 2 are optically active. Among the isomers, only the myo isomer is biologically
active. Inositol is often present as free form in the muscle, heart, liver, and lung of animals.
The hydroxyl groups in inositol can react with phosphate acid to produce phosphoinositides.
In higher plants, all the six hydroxyl groups in inositol are phosphated to inositol
hexaphosphate. Phosphoinositides can complex with Ca2+ and Mg2+, forming calcium and
magnesium salts of phytic acid.
Glycosides are the condensation products of monosaccharides and non-saccharide ligand
through the hemiacetal hydroxyl of monosaccharide. The bond between sugar and ligand is
referred to as the glycosidic linkage.
Glycosides contain one furanose or pyranose ring and the new chiral center might be
present in the alpha or beta form. Most glycosides occur in the beta form in nature.
Oligosaccharides
Oligosaccharides are water-soluble and occur widely in nature. Generally, naturally
occurring oligosaccharides contain less than six monosaccharide units, of which, most are
disaccharides and trisaccharides. For example, sucrose and maltose are disaccharides, and
affinose is a trisaccharide.
Some high-molecular weight oligosaccharides, such as cyclodextrins (or schardinger
dextrin), have gained wide applications in the food industry. Cyclodextrins consist of 6~8 Dglucopyranose units, corresponding to -, -, and - cyclodextrins respectively. In addition to
molecular weight, the three cyclodextrins differ in their water solubility and cavity size, as
shown in Table 3-2. X-ray diffraction reveals that -cyclodextrin is a highly symmetric
cylinder. Six C6 hydroxyl groups are located in the bottom of the cylinder and 12 C2 and C3
hydroxyl groups are arranged on the cylinder top. The inner wall of the cylinder is covered
with C-H groups and hence more hydrophobic than the external surface. Cyclodextrins are
used to stabilize hydrophobic substances by entrapping them in the cavity during food
processing.
Table 3-2. Chemical and physical properties of cyclodextrins
Item
Number of glucose residues
Molecular weight
Solubility in water at 25C (g/l)
Optical rotation
Inner diameter of cavity (nm)
Cavity height (nm)
-cyclodextrin
6
972
145
+150.5
0.57
0.67
-cyclodextrin
7
1135
18.5
+162.5
0.78
0.70
-cyclodextrin
8
1297
232
+174.4
0.95
0.70
40
Polysaccharides
Structure
The degrees of polymerization (DP) of polysaccharides range from 21 to several
thousands. Polysaccharides consist of one type of structural unit (homoglycans) or multiple
types of structure units (heteroglycans) and the structural units can be linked in a linear (such
as cellulose and amylose) or branched pattern (such as amylopectin and glycogen). The
monosaccharide units generally occur periodically in polysaccharides and each periodic
repeat contains one or more alternative structural units. An example of the exceptions is the
carbohydrate components in glycoproteins, in which the monosaccharide compositions are
nonperiodic all along the chain.
The DPs of polysaccharides are heterogeneous, that is, polysaccharides have no fixed
molecular weight (MW) and display the Gauss distribution. The heterogeneity of
polysaccharide molecular weight is associated with the metabolic status of organisms. For
example, the MW of glycogen is closely dependent on the blood glucose level of animals.
When the blood glucose level is low, the liver glycogen is hydrolyzed and glycogen is
cleaved to small segments. In contrast, when the blood glucose level increases, glycogen is
synthesized in the liver and the glycogen MW is increased. In addition, many polysaccharides
are present as complexes, such as glycoproteins, glycopeptides and glycolipids. In this case,
the MWs of polysaccharides are determined by much more factors than polysaccharide alone.
Conformation
Polysaccharides are either straight or branched molecules, but they have much more
complex conformations. Some typical conformations are elucidated in the following by taking
glucans and some other polysaccharides as examples.
Extended or stretched ribbon-type conformation
This conformation is typical for 1,4-linked -D-glucopyranosyl residues (Figure 3-1), for
instance that in cellulose fibers. This formula shows that the stretched chain conformation is
due to the zigzag geometry of monomer linkages involving oxygen bridging. The chain may
be shortened or compressed to enable formation of H-bonds between adjacent resides and
thus contribute to conformational stabilization. In this type of conformation, if the number of
monomers in turn is denoted as n and the pitch (advancement) in the axial direction per
monomer unit is denoted as h, n ranges from 2 to 4 and h equals the length of a monomer
unit. Thus, the chain given in Figure 3-2(a) has n value of -2.55 and h value of 5.13 .
A strongly plated ribbon-type conformation might also occur, as shown by a segment of a
pectin chain (1,4-linked -D-galactopyranosyl-uronate units) and an alginate chain (1,4linked -L-gulopyranosyluronate units), as shown in Figure 3-3.
41
Carbohydrates
(a) Peetin
(b) Alginate
Since alginate contains multiple oxygen atoms, it can complex with many transition
metals. As shown in Figure 3-3(b), Ca2+ stabilizes the conformation of alginate. In this case,
two alginate chains are assembled in a conformation which resembles an egg box, which is
referred as the egg box type of conformation (Figure 3-4).
Hollow helix-type conformation
This conformation is typical for 1,3-linked -D-glucopyranose units and occurs in the
polysaccharide lichenin, for example, as shown in Figure 3-5 (a). The formula shows that the
helical conformation of the chain is imposed by a U-form geometry of the monomer linkages.
Amylose (1,4-linked -D-glucopyranosyl residues) also has such a geometry, and hence a
helical conformation (Figure 3-5 (b)).
42
(a) Lichenin.
(b) Amylose
Figure 3-6. Stabilization of helical conformations. a, clathrate compounds; b, coiled double or triple
helices; c, nesting.
The number(n) of monomers per turn and the pitch in the axial direction per residue (h)
might differ significantly in this conformation.
The value of n varies from 2 to 10, while h can be near its limit value of 0. The
conformation of a (1-3)-glucan, with n value of 5.64 and h value of 3.16 , is shown in
Figure 3-2(b).
The helical conformation can be stabilized in various ways. When the helix diameter is
large, inclusion (clathrate) compounds can be formed (Figure 3-6(a)). More extended or
stretched chains, with smaller helix diameter, can form double or triple stranded helices
(Figure 3.6(b)), while strongly-stretched chains, in order to stabilize the conformation, have a
zigzag, plated association and not stranded (Figure 3-6(c)).
Crumpled-type conformation
This conformation occurs with, for example, 1,2-linked -D-glucopyranosyl residues
(Figure 3-2 (c)). This is due to the wrinkled geometry of the monomer O-bridge linkages.
Here, the n value varies from 4 up to 2 and h is 23 . The conformation reproduced in
Figure 3-2 (c), the n = 2.62 and h = 2.79 . The likelihood of such a disorderly form
associating into more orderly conformations is low. Polysaccharides of this conformational
type play only a negligible role in nature.
Loosely-jointed conformation
This is typical for glycans with 1,6-linked -D-glucopyranosyl units, because they exhibit
a particularly great variability in conformation. The great flexibility of this glycan-type
conformation is based on the nature of the connecting bridge between the monomers. The
bridge has three free rotational bonds and, furthermore, the sugar residues are further apart.
Carbohydrates
43
Conformations of heteroglycans
The examples considered so far have demonstrated that a prediction is possible for a
homoglycan conformation based on the geometry of the bonds of the monomer units which
maintain the oxygen bridges. It is more difficult to predict the conformation of a heteroglycan
with a periodic sequence of several monomers, which implies different types of
conformations. Such a case is shown by -carrageenan, in which the -D-galactopyranosy l-4sulfate units have a U-form geometry, while the 3,6-anhydro--Dgalactopyranosyl-2-sulfate
residues have a zigzag geometry (Figure 3-7).
Calculations have shown that conformational possibilities vary from a shortened,
compressed ribbon band type to a stretched helix type. X-ray diffraction analyses have proved
that a stretched helix exists, but as a double stranded helix in order to stabilize the
conformation.
Interchain interactions
As mentioned above, the periodically arranged monosaccharide sequence in a
polysaccharide can be interrupted by nonperiodic segments. Such sequence interferences
result in conformational disorders. This will be explained in more detail with -carrageenan.
44
Carbohydrates
45
Physiochemical Properties
Solubility
Most monosaccharides, such as sugar alcohols, glycosides, and oligosaccharides, are
water soluble. At 20C, up to 195 g of sucrose can dissolve in 100 g of water. The solubility
of sugar alcohols varies significantly with species. For example, sorbitol has a higher
solubility than sucrose and reaches up 220 g per 100g water, while that of mannitol, erythritol
and isomaltitolto is only 17, 50, and 100 g per 100g water, respectively. Sugar alcohols
absorb much more heat than sugars when dissolution and thus produce cooling sensation in
the mouth. Sugar alcohols are added to candies and chewing gums to provide the cooling
sensation.
The solubility of glycosides is closely correlated with their ligands. Generally, glycosides
are more water soluble than corresponding ligands. For example, flavonoids are usually
insoluble, but the corresponding glycosides are soluble. Flavonoids provide foods with
different colors and tastes in the soluble glucoside form.
Each sugar unit in polysaccharides contains an average of three hydroxyl groups and each
hydroxyl group can hydrogen bond with one or more water molecules. In addition, the
oxygen atoms in the sugar ring and glycosidic bond can also form hydrogen bonds with
water. Therefore, monosaccharide units in polysaccharides can be completely solvated and
most polysaccharides have strong water-holding capabilities and are highly hydrophilic.
Polysaccharides in foods affect the movement of water and significantly influence the
functional properties of foods.
The presence of polysaccharides does not increase the penetrability or significantly
reduce the freezing point of water, although polysaccharides can be solvated by water.
Therefore, polysaccharides are good frozen stabilizers. Taking starch solution as an example,
when a starch solution is frozen, a two-phase system is formed, of which, one phase is
composed of crystal water and another phase is in the glass state consisting of 70% starch and
30% unfrozen water. Due to the extremely high polysaccharide concentration in the glassstate phase, the viscosity is high and the movement of unfrozen water in the glass-state phase
is restricted. In addition, polysaccharides are concentrated in low temperatures. In this case,
46
the mobility of water is further restricted and water molecules can no longer adsorb to crystal
nucleus or the active sites for crystal growth. Both high and low molecular weight
polysaccharides can effectively protect food texture and structure from being damaged during
frozen storage.
Some polysaccharides occur in a highly ordered form. In these molecules, the chains are
tightly bound to form crystals. Because the number of exposed hydroxyl groups is
significantly reduced, these polysaccharides are insoluble in water unless the inter-chain
hydrogen bonds are broken. Taking cellulose as an example, the structural unit -Dglucopyranosyl residues are arranged orderly and linearly along the chain and form interchain hydrogen bonds with parallel chains. The crystal regions of cellulose are not water
soluble and are very stable.
The majority of carbohydrates is not present as crystals and readily dissolves or swells in
water. Water-soluble polysaccharides and their derivates used in the food industry are often
termed gums or hydrophilic colloids. The solutions of most macromolecular polysaccharides
are viscous and the viscosity depends on the molecular size, shape, net charge and
conformation in solution. The thickening and gelling properties of polysaccharides
significantly affect the quality of foods.
Hydrolysis
Hydrolysis of Glycosides
Though glycosides occur in low contents in foods, they impart important physiological
effects and functionality to foods. For example, nature saponins are strong foaming agent and
stabilizer, flavonoids produce bitterness and color for foods. In addition to a small amount of
sweet glycosides such as stevioside and osladin, most glycosides taste bitter or astringent,
particularly when the ligand is larger than methyl. When glycosides are hydrolyzed, their
solubility is reduced and the bitterness or astringency is alleviated.
O-glycoside bonds are stable in neutral and weak alkaline solutions, but easily
hydrolyzed in acidic conditions. Most glycosides in foods (except for strong acidic foods) are
stable.
In the enzymatic hydrolysis of glycosides, the sugar component is transformed to highly
active half-chair conformation and the glycosidic bond is weakened. Then, a proton is
transferred from the enzyme to an oxygen atom in glycoside. When the oxygen atom is
separated from the carbon atom, a positively-charged carbon ion is generated. This carbon ion
then reacts with the negatively-charged -COO- group in the enzyme and is temporarily
stabilized until it is completely hydrolyzed by reacting with the -OH- group in solvent.
N-glycosidic bond is not as stable as O-glycosidic bonds and is susceptible to hydrolysis
in water. For example, glycosylamines are unstable in water and can be hydrolyzed to colored
products through a series of reactions. These reactions are the main reason of Maillard
reaction initiation (to be discussed in Section 3.2.4).
Thioglycosides, which contain S-glycosidic bonds, occur naturally in mustard and
horseradish and are very stable and water-soluble. Thioglycosides can be hydrolyzed by thioglucosidase to produce isothiocyanates, as shown in Figure 3-11.
Cyanogenic glycosides are another category of glycosides that significantly affect food
safety. Cyanogenic glycosides are widely present in apricot, cassava, sorghum, bamboo, and
lima beans and can yield toxic hydrocyanic acid upon hydrolysis. Amygdalin and
Carbohydrates
47
mandelonitrile are the most important cyanogenic glycosides. The complete hydrolysis of
amygdalin generates D-glucose, benzaldehyde, and hydrocyanic acid (Figure 3-12).
Table 3-3 lists the main thio-glycosides and their hydrolysates. Excessive intake of
cyanogenic glycosides leads to cyanide poisoning.
In addition to enzyme activity and environmental acidity, the hydrolysis of glycosides is
also affected by glycodic bond conformation, substitution of the sugar ring, and sugar ring
size. Generally, glycosides with glycodic bond are hydrolyzed faster than those with
glycodic bond. Substitution on the sugar ring reduces the hydrolysis rate and furanosides are
hydrolyzed faster than corresponding pyranosides (Table 3-4). The hydrolysis rate of
glycosides increases rapidly with elevated temperature, as shown in Table 3-4.
Hydrolysis of oligosaccharides and polysaccharides
Similar to glycosides, oligosaccharides are hydrolyzed easily by acid and enzymes and
are stable in alkaline solutions. Sucrose can be hydrolyzed by acid to yield equamolar mixture
of glucose and fructose that is called invert sugar.
Occurrence
Almond kernel and dried
alpinia japonica
Lima bean, linseed (flax),
cassava
Tare
Sieve (black bean) and
Chickpea horsebean
Hydrolysates
D-Glucose + hydrocyanic acid + benzaldehyde
D-Glucose + hydrocyanic acid + acetone
Vicianose + hydrocyanic acid + benzaldehyde
D-Glucose + hydrocyanic acid + acetone (to be
confirmed)
48
Occurrence
Arabicus of lotus
Broomcorn and corn
Black mustard
Brassicaceae
Hydrolysates
D-Glucose + hydrocyanic acid + lotoflavin
D-Glucose + hydrocyanic acid + salicylide
D- Glucose + propyl isorhodanide + KHSO4
D-Glucose+ 5-ethenyl-2-oxazolidinethione, or
goitrogen+ KHSO4
80C
13.8
15.4
93C
76.1
141.0
Oxidation
Carbohydrates with reducing free aldehydes or ketoses that can be converted to aldehyde
groups can be oxidized into aldonic acid in the presence of weak oxidants in alkaline
conditions. When strong oxidants are present, both the aldehyde and primary hydroxyl of
aldoses are oxidized to carboxyl and aldaric acids are produced as a result [3, 18].
Some enzymes catalyze the oxidation of aldoses. For example, dehydrogenases oxidize
the primary hydroxyl of some aldoses to produce uronic acids. D-glucuronic acid, Dgalacturonic acid, and D-manuronic acid are the components of many heteropolysaccharides.
D-glucose can be oxidized to D-gluconic acid by glucose oxidase. Figure 3-13 illustrates
the preparation of D-gluconic acid and gluconolactones. D-gluconic acid--lactone can be
transformed to -lactone and both can be hydrolyzed into D-gluconic acid at room
Carbohydrates
49
Reduction
The carbonyl groups of monosaccharides can be reduced to the hydroxyl group.
Reduction of a ketose yields to two sugar alcohols isomers due to the formation of a new
chiral carbon atom. Figure 3-14 shows sugar alcohols produced by the reduction of glucose
and fructose.
Esterification and Etherification
Due to the presence of hydroxyl groups, sugars can be esterified by organic acids or some
inorganic acids, such as D-glucose-6-phosphate and D-fructose-1,6-diphosphate (Figure 315). The ester derivatives of starch, such as starch succinate, have found wide applications in
the food industry. Another typical example is sucrose fatty acid ester, which is a commonly
used an emulsifier.
Figure 3-15. Esterification of glucose and fructose by phosphorus acid (left: D-glucose; right: Dfructose).
Sugars can also be etherified, but naturally occurring sugar ethers are not as diverse as
sugar esters. Etherification of polysaccharides can significantly improve their functional
properties. Carboxymethyl cellulose (CMC) is an important ester of cellulose and is soluble
in water. CMC has been widely used in the food industry as thickening agent or emulsion
stabilizer.
50
Properties of Carbohydrates
Hydroscopicity
Carbohydrates contain abundant hydrophilic hydroxyls and can bind water through
hydrogen bonding. For example, when monosaccharides or oligosaccharides are placed in
environments of different relative humidity (RH), the compounds can absorb moisture from
air (Table 3-5).
Table 3-5. Moisture adsorption of different sugars (%)
Sugar
D-glucose
D-fructose
Sucrose
Anhydrous maltose
Hydrous maltose
Anhydrous lactose
Anhydrous lactose
100%, 25d
14.5
73.4
18.4
18.4
Not measured
1.4
Not measured
Figure 3-16. Hydroscopicity and water holding capacity of tea polysaccharide in different RHs (left:
RH=81%; middle: RH=43%; right: RH=43%).
All sugar alcohols, except mannitol and isomaltulose, exhibit hygroscopicity especially in
high RH environments. The hygroscopicity of sugar alcohols varies with their purity and lowpurity compounds have relatively higher hygroscopicity. Sugar alcohols are used as
moisturizing agent in cream foods and soft pastries. Polysaccharides also absorb moisture
from air and hence have good water holding capacity (Figure 3-16).
The hydroscopicity of carbohydrates, which is often referred to as moisture retention
capacity, is the most important attribute and determines their applications in foods. For
example, to overcome the sticky problem of icing sugar powders after packaging, sugars with
low hydroscopicity, such as lactose and maltose, are preferred in such products.
Carbohydrates
51
52
Figure 3-18. Effective volume of straight-chain and branched-chain polysaccharides with equal
molecular weights in solution.
Branched polysaccharides (amylopectin, glycogen) are more soluble in water than their
perfectly linear counterparts since the chainchain interaction is less pronounced and there is
a greater extent of solvation of the molecules. This is especially the case for highly branched
polysaccharides, because they have much less effective volumes than their linear
counterparts, as shown in Figure 3-18.
In addition to the DP, unfolding degree, and rigidity, the viscosity of polysaccharides is
also affected by the shape and flexibility of polysaccharides after solvaiton.
The charge carried by solvated polysaccharides significantly influences the viscosity of
the solution. For example, straight-chain polysaccharides containing carboxyl, sulfate hemiester or phosphate groups are often negatively charged. The electrostatic repulsion between
the molecules unfolds the molecules and increases their effective volume, leading to
increased viscosity. Hence, pH has significant impact on the viscosity of polysaccharide
solutions, since it is closely related to the charge statues of the molecules.
The viscosity of polysaccharide solutions decreases with the increase of temperature,
except xanthan solution, whose viscosity remains nearly unchanged in the temperature range
0~100C. Besides, the viscosity of xanthan gum solutions decreases with shear rate increase.
Hence, xanthan gum solutions are pseudoplastic. A practical use would be in salad dressing:
xanthan gum makes it thick enough at rest in the bottle to keep the mixture fairly
homogeneous, but the shear forces generated by shaking and pouring thins it, so it can be
easily poured. When it exits the bottle, the shear forces are removed and it thickens back and
clings to the salad.
Gelation
Gelation is another important property of polysaccharides. In food processing,
polysaccharides or proteins and other macromolecules can form a sponge-like threedimensional network gel structure through hydrogen bonding, hydrophobic interaction, Van
der Waals attraction, ionic cross bridges, entanglement or covalent bonding (Figure 3-19).
Liquids containing small-sized solutes and polymers fill the holes of the gel network.
Carbohydrates
53
Gels possess the properties of both solids and liquids. They are not as flowable as
continuous liquids or rigid as orderly organized solids. Instead, gels are viscoelastic semisolids and can retain their shape even in the presence of external stresses. Polysaccharide gels
generally contain only about 1% polymerthat is, they may contain as much as 99% water.
Examples of polysaccharide gels are dessert gels, aspics, structured fruit pieces, structured
onion rings, meat-analog pet foods, and icings.
The firmness of a gel depends on the extent of junction zone formation. If the conjunction
zone area is not long enough, polysaccharide chains cannot bind tightly. In this case, the
chains can be separated by pressure or high temperature due to increased mobility of the
chains. Such gels are easily damaged and are heat-labile. If the conjunction area contains long
chain segments, the interaction between chains is strong enough to withstand applied pressure
or thermal stimulation. Gels of this type are hard and stable. Therefore, gels of different
hardness and strength are available by controlling the length of the conjunction zone.
Branched-chain polysaccharides or heteropolysaccharides cannot bind to each other well
as linear molecules and large enough conjunction areas cannot be formed between these
molecules. Hence, gels cannot be formed by branched-chain or hetero- polysaccharides. This
is also the case for charged molecules, such as those containing carboxyl groups, because the
Coulomb repulsion between chains hinders the formation of conjunction zone.
Figure 3-19. A diagrammatic representation of the type of three-dimensional network structure found in
gels.
Flavor Retention
Aroma release from food matrix and the subsequent delivery of flavor to the olfactory
and gustatory receptors is greatly dependent on the type of food ingredients and on the
physicochemical properties of the aroma compound. It has been shown that macromolecules,
such as polysaccharides, are involved in the retention of volatile compounds. Polysaccharides
influence the volatility of aroma compounds and their partitioning between different phases
[1].
54
The use of carbohydrates may induce a significant decrease in flavor perception and/or
release. Some factors affecting the retention and release of volatile flavor compounds by
carbohydrates are depending on physicochemical properties of flavor compounds, type of
carbohydrates and their concentrations. Firstly, high molecular weight flavor compounds tend
to retain in carbohydrate than low molecular weight flavor compounds. Additionally, long
linear chain length molecules will be retained in polysaccharide matrix higher than short
chain molecules or aromatic one. Among the volatile flavor compounds such as alcohol,
aldehyde, ester and ketone, alcohol are usually the best retained in carbohydrates. The
retention of polar (hydrophilic) volatiles flavor compounds is expected to be very low in
carbohydrates complex. The second factor is depending on type of carbohydrates. Each type
of carbohydrate resents different structure that influence on the interaction between flavor
compounds and its structure and also the retention and release. Thirdly, the concentration of
carbohydrates generally shows that an increase in the concentration of sugar is proportional of
the release of flavor compounds due to the salting out effect. On the other hand, an increase in
polysaccharide concentration leads to a decrease the release of flavor compounds due to
complexation and viscosity effect of that polysaccharide themselves. This knowledge can be
used to optimize product quality in term of flavour retention during preparation or processing
and its release during eating [2].
Relative sweetness
100
Sugar/sugar alcohol
D-Mannitol
Relative sweetness
69
Galactitol
D-Fructose
D-Galactose
D-Glucose
Invert sugar
Lactose
Maltose
41
114
63
69
95
39
46
D-Mannose
Raffinose
D-Rhamnose
D-Sorbitol
Xylitol
D-Xylose
59
22
33
51
102
67
Carbohydrates
55
Sweetness
Sweetness is a value relative to that of sucrose under the same conditions, which is often
referred to as 100. All sugars, sugar alcohols and oligosaccharides are sweet (Table 3-6) with
varying intensity of sweetness and some glycosides and polysaccharide complexes are
excellent sweeteners. For example, the sweetness of honey and most fruits is contributed by
sucrose, D-fructose or D-glucose. The sweetness perceived by consumers varies with the
composition, conformation, and physical aspects of sugars.
The intensities of sweetness of sugar alcohols differ markedly from those of
corresponding sugars. For example, sorbitol is sweeter than glucose and that of xylitol is
greater than xylose. Generally, all sugar alcohols, except xylitol, are less sweet than sucrose.
Sugar alcohols are usually incompletely absorbed into the blood stream from the small
intestines which generally results in a smaller change in blood glucose than sucrose. This
property makes them popular sweeteners among diabetics and people on low-carbohydrate
diets. As an exception, erythritol is actually absorbed in the small intestine and excreted
unchanged through urine, so it has no side effects at typical levels of consumption.
56
Amadori products are degraded via various pathways in the intermediate stage, leading to
the formation of furfurals, reductones and fragmentation products (carbonyl and
hydroxycarbonyl compounds). Furfural or hydromethylfurfural (HMF) formation (Figure 322) is favored under acidic conditions, while alkaline media favor the production of
reductones (Figure 3-23).
The products of 1-amino-1-deoxy-2-ketose fragmentation in alkaline media, such acetol,
diacetyl, pyruvaldehyde, etc, are able to react with amino acids via the Strecker degradation
(named after the German chemist Adolph Strecker, Figure 3-24) to give Strecker aldehydes of
the amino acids and aminoketones; the latter subsequently condense to form pyrazines.
Strecker aldehydes and pyrazines contribute to aroma formation in heated foods.
Carbohydrates
57
58
The majority of the compounds displaying color are formed in the final stage of the
Maillard reaction. Furfurals, reductones, aldehydes either undergo aldol condensation without
the intervention of amino compounds or react with amino compounds as other intermediates,
leading to the ultimate reaction products known as melanoidins. Hodge defined melanoidins
as brown, nitrogenous polymers and copolymers. The structures of melanoidins remain
unknown till now. The pigment generated in the Maillard reaction is soluble in the early stage
of polymerization and exhibits no characteristic absorption pick in the visible range. Infrared
spectrum and chemical composition analysis indicate that melanoidins contain unsaturated
bonds, heterocycles, and complete amino acid residues.
The reaction mechanism of the Maillard reaction proposed by John Hodge is largely
unchanged after 60 years and is still widely cited. However, the hypothesis has some flaws.
Firstly, the mechanism presents only the general process of the Maillard reaction and the
details on the reaction are not described. Secondly, some new reactions have been identified
by other researchers. For example, the work of Japanese scientists Namiki and co-workers
found that the carbonyl fission products can also be formed directly from N-substituted
glycosylamine through a free radical-mediated pathway, which is known as the Namiki
pathway [4].
Mechanism of Caramelization
Heating of carbohydrates without the presence of nitrogen-containing compounds causes
a complex group of reactions termed caramelization. Unlike the Maillard reaction,
caramelization of carbohydrates is thermolysis as compared to the reaction with amino acids.
Mild heating or thermolysis in the early stage leads to anomeric shifts, ring size change,
glycosidic bond breakdown, and new glycosidic bond formation. Mostly, thermolysis causes
dehydration of the sugar molecule with introduction of double bonds or formation of anhydro
rings. Caramelization yields hundreds of flavor compounds and these compounds impart
foods with pleasant color and flavor. The caramels derived from different sugars have similar
compositions. Generally, the products of caramelization include caramel, which is the
polymerization product of sugar dehydration, and aldehydes, ketones, phenols, etc.
The caramelization process is divided into two stages.
Caramel formation
Figure 3-26 illustrates the formation of caramel by taking sucrose as the example. It can
be seen that caramelization is the removal of water from a sugar, proceeding to isomerization
and polymerization of the sugars into various high-molecular weight compounds.
Carbohydrates
59
The aqueous solutions of caramels are colloidal and the isoelectric points range from
3.0~9.0, with some exceptions with pI lower than 3. The presence of acids or certain salts
facilitates the reaction. The caramel prepared by heating sucrose solution in the presence of
acid or acidic ammonium salts has been widely used in food coloration.
The caramelization of sucrose consists of three steps:
Step 1: Caramelization of sucrose starts with the melting of the sugar at high
temperatures followed by foaming (boiling). At this stage sucrose decomposes into glucose
and fructose. This is followed by a condensation step, in which the individual sugars lose
water and react with each other to form the isosaccharosan (Figure 3-27). Isosaccharosan
loses the sweetness of sugar and tastes bitter instead.
Step 2: This step involves further dehydration reactions. Isosaccharosan dehydrates and
condensates to caramelan. Caramelan is one of the three main products of sucrose
caramelization. Caramelan are lightly brown and tastes bitter with formula of C24H36O18.
Caramelan melts at 138C and is soluble in water and ethanol.
Step 3: This step includes both fragmentation reactions (flavor production) and
polymerization reactions (color production). With respect to color production, caramelan is
further dehydrated to form caramelen. If the mixture is further heated, polymerization
reaction occurs and the insoluble caramelin is generated. The caramelan melts at 154C,
tastes bitter, and is soluble in water with formula of C36H50O25. Caramelin appears dark
brown and are not soluble in water with formula of C125H188O80.
60
The presence of iron enhances the color of caramels. Phosphates, inorganic salts,
alkalines, citric acid, ammonia, and ammonium sulfate catalyze sugar caramelization.
Ammonia and ammonium sulfate increase the yield of caramel. However, the addition of
ammonia and ammonium sulfate cause the generation of 4-methylimidazole at high
temperatures, which is an anticonvulsants and can cause nervous system damage after longterm consumption. Ammonia and ammonium sulfate have been prohibited in the production
of caramels.
Caramel flavors from thermal fragmentation
a. Formation of aldehydes in acid media.
In acid media, aldoses or ketones undergo enolization to yield hexose-1,2-enediol when
heated, followed by a series of dehydration reactions, as shown in Figure 3-28.
b. Formation of aldehydes in alkaline media.
In alkaline conditions, the intermediate 1,2-enol hexose, such as fructose, is produced via
the tautomery of reducing sugars and is then fragmented when heated, as shown in Figure 329.
Figure 3-28. Formation of aldehydes from sugars in acid media and thermal condition.
Carbohydrates
61
62
Structure of catechin
Catechin possesses two benzene rings (called the A- and B-rings) and a dihydropyran
heterocycle (the C-ring) with a hydroxyl group on carbon 3, as shown below:
Catechin contains multiple phenolic hydroxyl groups and is very susceptible to oxidation,
polymerization, and condensation. Catechin is white crystal and is oxidized to yellowishbrown compounds in the air. Catechin is soluble in water, ethanol, methanol, acetone, and
acetic anhydride, partially soluble in ethyl acetate and acetic acid, and insoluble in chloroform
and anhydrous ether.
Carbohydrates
63
Mechanism of oxidation
The hydroxyl groups in catechin have different activities with respect to auto-oxidation.
Hydroxyl groups in adjacent and vicinal positions are oxidized easily, while the OH in
carbon 3 on ring C cannot be oxidized.
The mechanism of the nonenzymatic auto-oxidation of catechin is very complex and not
well understood to the present. It is generally accepted that the process involves two
reactions. The first is the formation of quinine. Quinine is unstable and rapidly undergoes
condensation. The condensation product in the early stage is soluble, light yellow and tastes
bitter. As the reaction proceeds, the intermediates are further condensed to brown nitrogenous
polymer in the presence of amino compounds. The general process is illustrated in Figure 331.
Effects on Color
The composition of nonenzymatic browning reaction products is very complex. Many
components affect the color of foods and their molecular weights range from several
hundreds to up to more than 100000 Dolton. Several coloring compounds have been isolated
from different model systems.
64
A yellow compound is isolated from the Maillard reaction product of the xylose Lys
model system and MS and NMR reveals that its possible structure is one of the following two
[5]:
(1)
Furan-2-carboxaldehyde L-alanine model system
Two red products are isolated and identified from the Maillard reaction product and their
structures are shown below [6]:
(2)
Xylose L-alanie model system
A white compound is isolated:
(3)
Glucose propylamine model system in ethanol solution.
A yellow product is identified:
(4)
Xylose alanie model system in the presence of carbonyl compounds.
Two yellow compounds are isolated:
65
Carbohydrates
(5)
One red compound is isolated:
(6)
Starting materials, as well as reaction conditions, markedly affect the elemental
composition and structure of melanoidins. Thus far, the structures of the melanoidins have not
been elucidated, although some structural insights have been gained from model reactions. In
a glucose/amino acid Maillard reaction system, the carbonyl compound reacts mainly via the
Amadori product to form several deoxyosones which are able to react with each other in an
aldol-type condensation to form a basic melanoidin skeleton of amino-branched sugar
degradation products. Figure 3-32 shows the possible structure of a melanoidin formed from
3-deoxyhexosuloses in this way.
Figure 3-32. Part of possible melanoidin structure formed from 3-deoxyhexosulose involving amino
compounds [7].
66
Figure 3-34. pH changes of various sugar-amino acids solutions heated at 100C. From up to down:
glucose, lactose, lactose + alanine, glucose +alanine, lactose + glycine, glucose + glycine, glucose +
lysine, lactose+ lysine.
Carbohydrates
67
Elizalde et al. found that the volatile compounds of the MRP of the glucose-glycine
system showed a significant antioxidant activity and prolonged the induction period of
soybean oil thermoxidation by up to 3 times in relation to the control [9]. Bedinghaus and
Ockerman compared the lipid oxidation inhibitor activities of fifteen MRPs prepared by
heating one of three sugars (glucose, xylose, and dihydroxyacetone) with one of five amino
acids (arginine, histidine, leucine, lysine, and tryptophan) by using cooked ground pork
patties as the model food. It was found that the most effective MRPs were xylose-lysine,
xylose-tryptophan, dihydroxyacetone-histidine, and dihydroxy-acetone-tryptophan when
compared to controls [10]. Yamaguchi et al. obtained a fraction from the MRP of the xylose
glycine system through multiple chromatographic steps and found that it is more effective in
preventing linoleic acid oxidation than BHA and propyl gallate [11]. Yoshimura et al.
investigated the MRP of the glucose-glycine system on the inhibition toward active oxygen
and fount that it inhibited more than ca. 90% of active oxygen species existing in the form of
hydroxyl radicals (OH) [12].
Morales and Jimnez-Prez investigated the DPPH scavenging activities of MRPs
produced by heating glucose or lactose with lysine, alanine or glycine. It was found that all
the MRPs were effective DPPH scavenging agents. Browning was not directly related to the
free radical scavenging properties of MRPs formed at prolonged heating conditions and
fluorescence measurement is more effective than browning to follow the formation of MRPs
with free radical scavenging activities, as shown in Figure 3-35.
Although the antioxidant effects of MRPs have been well recognized, their application as
effective antioxidants in foods is still limited due to insufficient knowledge on the structure
and antioxidant mechanism of MRPs. Early researches indicated that antioxidant capability of
MRPs is contributed by the intermediate reductones of the Maillard reaction and the metal
chelating ability of MRPs. Latest researches indicate that MRPs also have strong active
oxygen scavenging capabilities and can reduce peroxides.
68
Effects on Nutrition
One of the most obvious negative consequences of the Maillard reaction in food is the
loss of nutritive value of proteins due to decreased digestibility, destruction and/or biological
inactivation of amino acids, including essential amino acids like lysine and tryptophan,
inhibition of proteolytic and glycolitic enzymes, and interaction with metal ions.
Lysine is the most liable to loss in non-enzymatic browning, followed by alkaline amino
acids, including L-Arg and L-His. In addition to sugar-amino acid reactions, Strecker
degradation is also involved in amino acid loss. The formation of complex macromolecules
reduces the solubility of proteins and reduces their nutritional value. The effect of the
Maillard reaction on amino acid availability has been investigated by using rainbow trout
(Salmo gairdneri) as the model. It was found that arginine and lysine exhibited the greatest
losses in the mixture of fish protein isolate and glucose stored for 40 d at 37C and the
apparent digestibility and absorption of individual amino acids, particularly lysine, was lower
in trout fed browned protein than in those fed the control protein [14].
Vitamin C is also involved in browning and therefore suffers loss during the process.
The products of non-enzymatic browning reduce the bioavailability of minerals.
Whitelaw et al. employed the dialysis procedure to determine the effect of the Maillard
reaction on apparent 65Zn availability. In the presence of 65ZnCl2, the amino acids glycine, Dleucine, L-proline, L-lysine and L-glutamic acid were combined with D-glucose and
autoclaved (110-120C, 15 atm, 10 min) to produce high molecular weight 65Zn binding
compounds that were not dialyzable (6-8KD). Experiments in stimulated gastrointestinal
digestive conditions revealed that the Maillard reactions significantly reduced the
bioavailability of Zn [15].
Harmful Compounds
The safety of MRPs has attracted wide attentions in recent years. With the development
of new instrumental analysis measures, more and more harmful compounds have been
isolated and identified. For example, mutagenic compounds have been found in instant and
caffeine-free coffee and the compounds consist of dicarbonyl compounds, methylglyoxal,
diacetyl and glyoxal, among which the methylglyoxal presented highest mutagenic activity
[16]. Also in both fried and grilled meat and fish, mutagenic compounds were identified,
mainly stemming from heterocyclic amines [17]. The reaction mechanism seems to have a
major influence on the mutagenicity of the reaction products. For instance, ketose sugars
showed a higher mutagenic activity than the corresponding aldose sugars [18]. However, due
to the complexity of non-enzymatic browning reactions and the poor stability of
intermediates, only very few harmful compounds have been well elucidated, of which,
acrylamide is the most intensively studied.
Acrylamide is a well-known cancerogen and can cause neurologic damage. Acrylamide
has been detected in nearly all the foods, but fried and roasted foods that are processed at high
temperatures have much higher acrylamide contents, as presented in Table 3-7.
69
Carbohydrates
Table 3-7. Content of acrylamide in some foods
Foods
Potato chips
French fries
Biscuit
Fried bread
American breakfast
Cornflakes
Bread
Number of
samples
14
9
14
21
15
3
20
70
acrylamide formation is detected within 10 min and the content remains unchanged thereafter.
While in the glucose/methionine system, the formation of acrylamide keeps increasing in the
first 30 min and then remains unchanged in remaining time.
pH
Medium pH affects multiple reactions of non-enzymatic browning. Aqueous solutions of
sugar (xylose or glucose) and amino acid (glycine or lysine monohydrochloride), are heated
without pH control for up to 120 min and the total reaction products are analyzed by HPLC
and compared with those of the corresponding model systems maintained at pH 5 throughout
heating.
For xylose-lysine, seven of these peaks are common to the systems heated both with and
without pH control for 15 min, while no peak is common to both glucose-lysine systems
heated for 120min, indicating different products are formed under the conditions [19].
Generally, the browning rate between sugars and amino acids increases with pH when the
medium pH is greater than 3.5 and is reversely proportional to pH values in the range 2.0~3.5.
Hence, browning can be suppressed by reducing pH. This is why browning does not occur
readily in acidic foods such as pickled vegetables. Sulfites inhibit nonenzymatic browning by
reacting with carbonyl intermediates, thereby preventing their further reaction to form brown
pigments [20].
Figure 3-36. The time course of the browning develop in heated sugars -amines solutions at 100CUp
to down: glucose+lysine, lactose +lysine, glucose+glycine, lactose+ glycine, glucose+alanine, lactose
+alanine, lactose, and glucose.
Carbohydrates
71
High Pressure
High pressure (100-1000 MPa), which is gaining increasing importance as a foodprocessing technology particularly in combination with moderate temperatures (30-60 C),
may influence the Maillard reaction and thereby affects the flavor, color, and nutritional value
of foods. It has been proposed that high pressure exerts its influence on non-enzymatic
browning by changing the medium pH. The effect of high pressure on Maillard reaction has
been investigated by using the glucose-lysine model system over a range of pH values (5-10)
at 60 C either under atmospheric pressure or at 400 MPa. The results obtained showed that
high pressure affected in different ways the different stages of the Maillard reaction and that
such effects were strongly influenced by pressure-induced changes in the pH of the systems.
In unbuffered media, at an initial pH 8.0, the formation of Amadori rearrangement products
(ARP) was not considerably affected by pressure, whereas the intermediate and advanced
stages of the Maillard reaction were suppressed, suggesting a retardation of the degradation of
the ARP. In buffered media, at pH values 8.0, pressure slowed the Maillard reaction from the
initial stages. These effects are attributed to the pH drop caused by the pressure-induced
dissociation of the acid groups [22].
Control of Non-Enzymatic Browning
The non-enzymatic browning has both beneficial and adverse impacts on food qualities.
Researchers have developed rational approaches to minimize adverse consequences of
browning reactions and optimize beneficial ones.
Non-enzymatic browning can be prevented by chemical or biochemical methods [23]:
Sulfhydryl compounds
Sulfur-containing amino acids such as cysteine, N-acetylcysteine, and the tripeptide
glutathione play key roles in the biotransformation of toxic compounds by actively
participating in their detoxification. These antioxidant and antitoxic effects are due to a
multiplicity of mechanisms including their ability to act as (a) reducing agents, (b) scavengers
of reactive oxygen (free radical species), (c) destroyers of fatty acid hydroperoxides, (d)
strong nucleophiles that can trap electrophilic compounds and intermediates, (e) precursors
for intracellular reduced glutathione, and (f) inducers of cellular detoxification. Under certain
conditions, SH-containing compounds may be as effective as sodium sulfite in preventing
nonenzymatic browning of both apples and potatoes.
Acetylation of amino groups
Modifications of amino groups prevent them from participating in browning reactions.
For example, treatment of foods with the enzyme transglutaminase will transform lysine
amino groups to amide groups. The former initiate browning, whereas the latter do not.
Antioxidants
Oxygen seems to be required for some nonenzymatic browning reactions. Hence,
antioxidants could suppress browning in some foods. Besides, antioxidants can trap or
72
prevent the formation of intermediates in the Maillard and related reactions, thus prevent the
formation of undesirable compounds during food processing.
Deglycation
An extract from soil microorganisms catalyzed the deglycation of - and fructosyllysines to lysine. This finding suggests that these purified enzymes could be used to
prevent or reverse Maillard reactions in foods and in vivo provided they are safe in other
regards.
Non-enzymatic browning can also be prevented by controlling processing conditions:
Low temperature
Non-enzymatic browning occurs slowly in low temperatures. Storage at low temperatures
can delay non-enzymatic browning in foods.
Sulfurous acid
The condensation product of carbonyl group and sulfurous acid can react with R-NH2
and the resultant product cannot be transformed to Schiffs base. Hence, SO2 and sulfites
suppress non-enzymatic browning.
pH
Non-enzymatic browning does not occur readily in acidic conditions as in alkaline
conditions.
Product concentration
Products with lower concentrations suffer lighter browning. For example, because lemon
juice is more susceptible to browning than orange juice, the concentration factor of lemon
juice is 4:1, which is lower than 6:1 of orange juice.
Insensitive sugar
The presence of free carbonyl groups is essential for non-enzymatic browning.
Replacement of reducing sugar with sucrose can prevent browning.
Removal of sugar
Some foods contain only trace amount of sugars and these sugars can be removed to
prevent non-enzymatic browning. For example, glucose oxidase and catalase have been used
to remove the trace glucose in dried egg yolk and dehydrated meat.
Calcium salts
Calcium can complex with amino acids to form precipitates.
Carbohydrates
73
Oligosaccharides
Oligosaccharides occur naturally in a variety of foods, especially plant-derived foods,
such as vegetables, grains, legumes, and algae. Oligosaccharides have also been identified in
animal-derived foods, including milk, honey and insects. Sucrose, maltose, lactose and
cyclodextrin are the most important oligosaccharides for the food industry. Some
oligosaccharides, such as fructo-oligosaccharides, xylo-oligosaccharides, and Konjac
oligosaccharides, have obviouse physiological functions and can be used as the effective
ingredients of functional foods.
Cellobiose, maltose, isomaltose, gentiobiose and trehalose are common disaccharides. All
these disaccharides, except trehalose, contain a free semi-acetal group and hence are reducing
sugars.
Sucrose, lactose, lactulose, and melibiose are hybrid-oligosaccharides and each contains a
reducing group except sucrose. Of the sugars, lactose deserves special attention. Lactose is
found notably in milk and non-fermented dairy products and accounts for 2~8% of milk by
weight. In small intestine, lactose is hydrolyzed by lactase to D-glucose and D-galactose,
which are then absorbed by the human body. However, some consumers lack the lactase and
cannot digest or metabolize lactose. These consumers might suffer abdominal pain, bloating,
flatulence, diarrhea, nausea, and acid reflux and this is called lactose intolerance or lactase
deficiency.
Some natural foods contain functional oligosaccharides. These compounds cannot be
absorbed by human body and provide very few energy, but can enhance the proliferation of
intestinal bifidobacteria and prevent dental caries and colon. Some important functional
oligosaccharides are described below.
Soybean oligosaccharide
Soybean oligosaccharide has once been regarded as an antinutritional factor and has been
reported to increase the incidence of diarrhea in rats. However, recent researches reveal that
soybean oligosaccharide has the potential as new functional ingredients in functional foods.
Soybean oligosaccharide has recently been found to be probiotic material and have been
approved by the Food and Drug Administration as generally recognized as safe material in the
USA. Composition analysis indicates that soybean oligosaccharide was composed of
74
galactose (65.3%), mannose (15.6%), fructose (7.8%) and glucose (8.7%) [24]. Intake of 3~5
g soybean oligosaccharide per day is sufficient to enhance the proliferation of bifidobacteria.
Fructo-oligosaccharide
Fructo-oligosaccharides (FOS) are fructose oligosaccharides containing a single glucose
moiety. FOS are mainly composed of 1-kestose (GF2), nystose (GF3), and 1--fructofuranosyl
nystose (GF4), in which fructosyl units (F) are bound at the (2 1) position of sucrose
molecule (GF). FOS occur naturally in various fruits and vegetables, such as bananas, onions,
chicory root, garlic, asparagus, barley, wheat, jcama, tomatoes, and leeks, but commercial
FOS are often prepared by transfructosylation from sucrose and chemical or enzymatic
hydrolysis of inulin.
FOS are about 0.4 and 0.6 times as sweet as sucrose and have been used in the
pharmaceutical and food industries as functional sweeteners. FOS with low polymeric grade
have better therapeutic properties than those with a high polymeric degree. They present
properties such as low caloric values, non-cariogenic properties, decreased levels of
phospholipids, triglycerides and cholesterol, help gut calcium and magnesium absorption, and
are used as prebiotics to stimulate the bifidobacteria growth in the human colon [25]. Figure
3-37 illustrates the structure of several FOS.
Xylo-oligosaccharide
Xylo-oligosaccharides (XOS) consist of 2~7 xylose residues connected through by the
(14) glycosidic bond. XOS are about 40 times as sweet as sucrose. XOS have good thermal
stability and are not decomposed in acidic conditions (pH2.5~7) when heated. XOS can be
used in yogurt, lactobacillus drinks, carbonated drinks and other acidic beverages.
Commercial XOS consists mainly of xylose, xylobiose, and less amount of polymers with
DP greater than 3. Xylobiose is the main constituent of XOS and its content determines the
quality of XOS products. XOS can be prepared by the enzymatic (xylanase) hydrolysis of
xylan-rich materials, such as corncob, bagasse, cottonseed hull, and bran. Many fungi and
bacteria can produce xylanase, of which, the endoxylanase produced by Chaetomiu globosum
has been used in the industrial production of XOS.
XOS cannot be digested but can selectively activate bacterial reproduction within
intestines and hence are prebiological substances. It can obviously improve intestinal
microecological balance, proliferate bifid bacteria and gastric function.
Chito-oligosaccharides
Chito-oligosaccharides (COS) are oligomers of N-acetyl-D-glucosamine and Dglucosamine connected through the -1, 4 glycosidic bond. COS are water soluble in contrast
to chitosan and chitin. COS carry positive charge, which allows COS to bind to negatively
charged cell surface strongly. This property contributes to many physiological functions of
COS, such as antitumor, immunostimulatory, and anti-inflammatory. Besides, COS stimulate
the proliferation of Bifidobacteria bifidium and Lactobacillus sp. [26].
Carbohydrates
75
Other oligosaccharides
Palatinose (6-O--D-glucopyranosyl-D-fructose), also referred as isomaltulose, is a
reducing disaccharide identified during the processing of sugar from sugar cane. It is
completely digested and provides the same caloric value as sucrose, but it is non-cariogenic
and digested much slower, leading not only to a low glycemic response but also to a
prolonged glucose supply, indicating its potential as a parenteral nutrient acceptable to both
diabetics and non-diabetics. Its ingestion selectively promotes the growth of beneficial
bifidobacteria amongst the human intestinal micro flora. It is more stable than sucrose, which
facilitates the maintenance of its sweetness and taste in fermented foods and beverages. It has
been suggested as a non-cariogenic alternative to sucrose, and as such is currently widely
used as a sugar substitute in foods. This disaccharide has a sweet taste and very similar
physical and sensory properties to sucrose [27].
Lactulose (4-O--D-galactopyranosyl-D-fructose) is a synthetic disaccharide and is also
termed isomerized lactose, because it can be prepared from the isomerization of lactose. It is a
Bifidus factor in nutrition and is a very important humanizing factor in infant formula and is
added to commercial infant formula products and various milk products. This sugar has
greater sweetness and solubility than lactose and if produced economically, it could widely be
used in baking and confectionery applications [28].
76
Content
73
70
40
49
19
Variety
Potato
Wheat
Sorghum
Buckwheat noodles
Pea
Content
16
66
60
72
58
Amylose
50~ 85
26
1
Amylopectin
15~50
74
99
Starch
Potato starch
Cassava starch
Wheat starch
Amylose
21
17
28
Amylopectin
79
83
72
Carbohydrates
77
Type B amylose shows the left-hand double helices structure, which are packed in a
parallel arrangement. Hydroxyl groups are located outside of the chains and the double helix
is stabilized by the hydrogen bridges between amylose molecules. The internal channel of the
helix is hydrophobic and hence can enclose only hydrophobic compounds, such as lipids. The
A-type is very similar to the B-type, except that the central channel is occupied by another
double helix, as shown in Figure 3-38.
Amylopectin is the highly branched polymer of glucose. The backbone chain is
composed of glucose units linked in a linear way with (14) glycosidic bonds and
branching takes place through (16) bonds. In amylopectin, (16) bonds account for
4%~5% of total glycosidic bonds.
Figure 3-38. Unit cells and arrangement of double helices (cross section) in type-A amylose (left) and
type-B amylose (right) [29].
Due to the presence of multiple linear branches, amylopectin has multiple reducing ends
and are hydrolyzed by enzymes faster than amylose. The branches of amylopectin are
arranged in parallel or double helix, as shown in Figure 3-39.
Amylopectin contributes to the crystalline structure of starch granules. The molecular
weight of amylopectin ranges from 5107~5108. The ratio of amylopectin in starches
generally exceeds 75% and the value can reach up to 99% in some species, such as waxy corn
starch, as shown in Table 3-9. Starches derived from potato also contains a high phosphorus
content (0.06~0.1%). Hence, potato starches are slightly negatively charged and swell more
rapidly in warm water due to coulombic repulsion.
Gelatinization
Starch granule: Starches are present as granules in plant cells. Starch granules can be
round, oval, and polygonal and their sizes range from 0.001~0.15 mm, depending on the plant
78
species, of which, potato starch granules have the largest size and cereal starch granules have
the smallest size, as shown in Figure 3-40. Polarization microscopy observation and X-ray
diffraction find double refraction and X-ray diffraction in starch granules, indicating the
presence of crystalline structure alternate layers of crystal region and amorphous region
(Figure 3-41 I). About 70% of the mass of a starch granule is regarded as amorphous and
about 30% as crystalline.
The amorphous regions contain mainly amylose and the crystalline regions consist
primarily of amylopectin. Amylose can enclose fatty acids and hydrocarbons due to the
presence of the hydrophobic internal channel and the complexes are termed inclusion
complexes. Amylose occur as double helices as in starch granules. Amylose and amylopectin
are arranged radially in starch granules, as shown in Figure 3-41 II.
Figure 3-39. Structural models (I, II) for amylopectin with parallel double helices. III is an enlarged
segment of I or II.
Carbohydrates
79
Figure 3-40. Shapes of starch grains in electron microscope (1200).A, Green bean starch (mean grain
size: 0.016nm); B, Potato starch (mean grain size: 0.049nm; C, Common corn starch (mean grain size:
0.013nm); D, Sweet potato starch (mean grain size: 0.017nm).
Figure 3-41. Sketch of crystallization section and amorphous section of starches (I), and radial shape of
amylose and amylopectin in starches (I, II).
Gelatinization: Due to the inter-molecular hydrogen bonding, starch is not soluble in cold
water in spite of the abundance of hydroxyl groups. When the suspension is heated, the
vibration of starch molecules increases and the hydrogen bonding between molecules is
disrupted. As a result, more hydroxyl groups are exposed and starch-water hydrogen bonding
is formed instead. With the diffusion of water into starch granules, many long chains are
separated and the confusion degree increases markedly. Meanwhile, the number and size of
80
6ISCOSITY "RABENDER UNITS X
crystal regions reduce significantly. When the suspension is further heated, the swelling
becomes reversible. In this case, random coils are observed in amylopectin due to hydration
and the ordered structure of starch is destroyed. This process is termed gelatinization and the
temperature at which irreversible changes occur is called the gelatinization temperature.
Starch gelatinization can be divided into three phases. In phase I, water diffuses into
granules and absorbs to the polar groups in amorphous regions below the gelatinization
temperature. The starch can restore to their original form if dehydrated. In phase II, when the
gelatinization temperature is reached, bulk water enters starch granules and the granules swell
significantly. Due to the increase of volume, the fraction between swollen starch increases
and the suspension becomes viscous, which can be followed by Brabender amylograph. In
this phase, water molecules enter the microcrystalline areas and the original arrangement is
disrupted. When the temperature further increases, the viscosity of the suspension increases
accordingly. In phase III, the swollen starch granules are disintegrated and the suspension
viscosity drops sharply, as shown in Figure 3-42. It could be seen that the shape of the curve
varies greatly for different starches.
The gelatinization of starch is affected by the following factors:
Water activity: Gelatinization occurs readily in medium with high water activity. The
presence of high concentration of sugars significantly suppresses gelatinization, because the
molecules can compete for water with starch.
4IME MIN
Carbohydrates
81
Helix amylose
Fatty acid
Figure 3-43. Scheme of the lipid-starch inclusion complex.
82
Medium pH: Starch undergoes retrogradation readily in the pH range 5~7 and the process
is inhibited in alkaline or acidic solutions due to charge repulsion.
Temperature: The optimum temperature for starch retrogradation is 2C~4C and
retrogradation does not occur in temperatures above 60C or below -20C.
Cooling speed: When starch paste is cooled slowly, starch molecules have sufficient time
to align and retrogradation occurs readily. If the paste is cooled rapidly, the water in the paste
crystallizes quickly, which prevents the approaching of starch molecules. Hence,
retrogradation occurs slowly in rapid cooling.
Presence of other ingredients: Lipids and emulsifying agents prevent retrogradation.
Compounds such as glyceryl monopalmitate (GMP), other monoglycerides and their
derivatives, and sodium stearoyl 2-lactylate (SSL) are often added into doughs of bread and
other baked goods to prevent starch retrogradation and increase shelf life.
Hydrolysis of starch
Starches can be randomly hydrolyzed by acids and enzymes. Under mild conditions,
starch is only partially hydrolyzed by acids. This process is called thinning and the products
are termed acid-modified or thin-boiling starch. Acid-modified starch has increased gel
transparency and strength and is less susceptible to retrogradation. Acid-modified starch has
wide applications and can be used as film forming agent and adhesive agent in products such
as pan-coated roasted nuts and candy. Besides, they are also used as encapsulating agents and
flavor carriers.
Enzymatic hydrolysis has been used in the production of commercially important syrups.
In the production of high-fructose corn syrup, corn is firstly hydrolyzed by -amylase and
glucoamylase to obtain high purity D-glucose. D-glucose isomerase is then added and Dglucose is converted to D-fructose. The final product is the mixture of 58% D-glucose and
42% D-fructose. High-fructose corn syrup is commonly used as sweetener in soft drinks.
The degree of hydrolysis of starch is measured by dextrose equivalency (DE), which is
defined as the percentage of reducing sugar in the syrup. DE is related to the degree of
polymerization and is calculated in the following equation:
(1)
Glucose polymers with DE less than 20 are defined as maltodextrins and those with DE
in the range 20~60 are termed corn syrup. Table 3-14 lists the functional properties of some
hydrolysis products of starch.
Modified starch
Physical, chemical and biochemical modifications have been implemented to enhance the
functional properties of starches and modified starches have gained wide applications in the
food, pharmaceuticals, and chemical industry. Important modified starches that are widely
used in the food industry are described below.
Low viscosity starch: Starch of this type is also termed acid-modified starch. When starch
is exposed to acid below the gelatinization temperature, hydrolysis occurs only in the
Carbohydrates
83
amorphous region and the crystal region nearly remains intact. The modified starch produced
under such conditions is not soluble in cold water but is readily soluble in boiling water.
Compared with native starch, low viscosity starch has decreased viscosity and gel strength of
hot paste and elevated gelatinization temperature. Low viscosity starch can be used as
thickening and film forming agents.
Pre-gelatinized starch: This product is obtained by heating starch suspension above the
gelatinization temperature and then dried with drum drying, spray drying or extrusion. Pregelatinized starch can dissolve and form gel in cold water. Pre-gelatinized starch can be used
in elder and infant foods, surimi products, ham, sausage, and bakery foods. Besides, pregelatinized starch has gained applications in cooking-free instant foods due to its solubility in
cold water.
Table 3-14. The functional properties of hydrolysis products from starch
Properties enhanced by greater
Properties enhanced in products of less
hydrolysis A
conversion B
Sweetness
Viscosity production
Hygroscopicity and humectancy
Body formation
Freezing point depression
Foam stabilization
Flavor enhancement
Sugar crystallization prevention
Fermentability
Ice crystal growth prevention
Browning reaction
Note: A high DE syrups; B low DE syrups and maltodextrins.
Etherified starch: All the three free hydroxyl groups in each D-glucopyranose unit can be
etherified. Hydroxyethyl starches of low degree of substitution (DS) have reduced
gelatinization temperature, increased swelling rate, and lowered tendency of pastes and gels
to retrogradation. Hydroxyalkyl starches, such as hydroxypropyl starch, can be used in salad
dressings, pie fillings, and other foods as thickening agent.
Esterified Starch: Starch can be esterified by acidic orthophosphates, acid
pyrophosphates, and tripolyphosphates to produce various starch esters. Compared with
native starch, monostarch phosphates gelatinize in lower temperatures and those with DS
greater than 0.07 can swell in cold water and have increased paste viscosity and transparency,
and decreased retrogradation. These properties are quite similar to those of potato starch,
which has high phosphorus content.
Because monostarch phosphates have good freezing-thawing stability, they are preferred
in frozen foods, such as frozen broth and frozen cream pie, as thickening agent to unmodified
starch.
Starch can also be esterified by various organic acids, such as acetic acid, long-chain fatty
acids (C6~C26), succinic acid, adipic acid, and citric acid. These esters are superior in
thickening and paste transparency and stability to native starch and can be used in bakery
products, soup powder, sauce, pudding and frozen foods as thickening agent and stabilizer, as
well as in dehydrated fruit as protective agent and in flavor processing as encapsulating
material.
Crosslinked starch: Starch can react with sodium trimetaphosphate, phosphorus
oxychloride, epichlorohydrin, and acid anhydride to yield crosslinked derivates. Crosslinking
84
prevents starch granule swelling and increases the stability against heating. Crosslinking by
phosphorus increases the stability of swollen starch granules, but the paste of distarch
phosphates is opaque in contrast to that of monostarch phosphate.
Table 3-15. Comparisons of the properties of native and modified starches
Starch
Amylose/Amylopectin
ratio
1:3
Gelatinization
temperature range (C)
62~72
Properties
0:1
63~70
High-amylose
starch
Acidmodified
starch
Hydroxyethyl
starch
Monostarch
phosphate
Crosslinked
starch
3:2-4:1
66~92
Variable
69~79
Variable
58~68 (DS0.04)
Variable
56~66
Variable
Acetylated
starch
Variable
Common
starch
Waxy starch
Starches with high degree of crosslinking are very stable against high temperature, low
pH and mechanical vibration and their gelatinization temperature is proportional to the degree
of crosslinking. Some starches with high degree of crosslinking do not swell even in boiling
water.
Crosslinked starches are mainly used in infant foods, salad dressing, fruit pie filling and
cream-style corn as thickeners and stabilizers. They also provide resistance to gelling and
retrogradation, show good freeze-thaw stability, and do not undergo syneresis or weep on
standing.
Oxidized starch: Starch is hydrolyzed and oxidized when its aqueous suspension is
incubated with sodium hypochlorite below the gelatinization temperature and the carboxyl
group occurs once every 25 to 50 glucose residues in the resulting oxidation products.
Oxidized starch has relative low viscosity even in high concentrations and is used as
thickening agent in salad dressing and mayonnaise. Compared with low viscosity starch,
oxidized starch is less susceptible to retrogradation or forming opaque gel.
Table 3-15 lists the nature of a variety of starch before and after modification.
Glycogen
Glycogen is also called animal starch and is the major storage carbohydrate in muscle and
liver tissue of animals. Because glycogen accounts for only 0.02%~0.1% of fresh animal
Carbohydrates
85
tissues, it is less important for the food industry than starch. Glycogen is much branched than
starch and is similar to amylopectin in structure.
86
widely used in ice creams and other foods to prevent ice crystal formation. CMC also
increases the volume and elongate shelf life of cakes and other bakery foods, improves the
mouthfeel of sucrose and prevent CO2 escape from low-calorie carbonated beverage.
Methylcellulose (MC) and hydroxypropyl methylcellulose (HPMC)
MC is the etherified derivative of cellulose and is prepared by treating alkaline CMC with
chloroform. The DS of commercially important MC lies in the range 1.1~2.2.
MC is characterized by its gelling properties. When a MC solution is heated, the initial
viscosity drops with rising temperature and then increases sharply. This can be explained by
the breakdown of hydration layer around MC molecules upon heating, which increases the
hydrophobic interactions between MC molecules. Electrolytes such as NaCl and
nonelectrolytes such as sucrose and sorbierite reduce the gelling temperature of MC by
competing for water molecules. MC cannot be digested by human body and is a calorie-free
polysaccharide.
HPMC is prepared by incubating cellulose with methyl chloride and cyclopropane in
alkaline solutions. The DS of commercial HPMC ranges from 0.002 to 0.3.
The initial viscosity of HPMC solution decreases with temperature elevation and the
formation of gel is reversible at specific temperature, which is similar to that of MC. The
gelling temperature and gel strength are related to the type of substation groups, DS and
concentration of the soluble gel. The hydroxypropyl group stabilizes the hydration layer of
HPMC and thereby increases the gelling temperature. Changing the proportion of methyl to
hydroxypropyl substituents can vary the jelling temperature within a wide range.
MC and HPMC increase the water retention and absorption capabilities of foods and
prevent excessive oil absorption in fried foods. MC can be added to functional foods as
fillings and dehydration and shrinkage inhibitors. The two derivatives are added to salad
dressings as thickening and stabilizing agents and to various foods as edible coatings and fat
substitutes.
Hemicellulose
Hemicelluloses occur along with cellulose in the cell walls of plant cells and consist of
multiple monomers in contrast to cellulose, such as xylose, mannose, galactose, rhamnose,
and arabinose in addition to glucose. The compositions of hemicelluloses vary with the plant
origin and tissue. For example, wheat and rye contain mainly arabinoxylans, while -glucans
predominate in barley and oats.
In the food industry, hemicellulose is mainly added to bakery foods to increase the water
binding capability of flour, improve the kneading quality of dough by reducing the energy
required by kneading, and increase bread volume. Breads containing hemicellulose have
delayed hardening time compared with those without hemicellulose. Hemicellulose is an
important source of dietary fiber.
Carbohydrates
87
Pectin
Pectins are polymers consisting of D-galactopyranosyluronic acids connected through the
-1,4-glycodic linkage. In addition to galacturonic acid, pectins might also contain rhamnose,
galatose, arabinose, and other sugars. Pectins are present in the cells and intercellular layers
of plants. Pectins originated from various sources differ mainly in their contents of methoxyl
groups or degrees of esterification (DE). The DE of pectins is defined as the percentage of the
number of esterified D-galacturonic acid residues among all D-galacturonic acid residues.
Pectins with DE greater than 50% are termed high-methoxyl pectin (HM) and those with
DE less than 50% are called low-methoxyl pectin (LM). Protopectins are the highly methyl
esterified and insoluble form of pectins and are found in immature fruits and vegetables.
Pectins with low DS are called pectinic acids and can be converted from protopectins by
the hydrolysis of protopectinase and pectin methyl esterase. Pectinic acids are either colloidal
or soluble in water depending on the degree of polymerization and degree of methyl
esterification, of which, water soluble pectinic acids are also referred as low-methoxyl pectin.
Pectinic acids can be completely hydrolyzed by pectin methyl esterase to pectic acids.
Various pectinases participate in the post-harvesting ripening of plants. During this
process, protopectinase converts protopectins to colloidal or soluble pectinic acids.
Pectinesterase removes methoxyl groups from pectins to produce poly-D-galacturonic acid or
pectic acid, which is then hydrolyzed by polygalacturonase to yield D-galacturonic acid units.
These enzymes work together in the ripening of fruits and are important for the texture
formation of fruits and vegetables.
Pectin is an important polysaccharide with applications in foods, pharmaceuticals, and a
number of other industries. Its importance in the food sector lies in its ability to form gel in
the presence of divalent ions such as Ca2+ or a solute at low pH. In the case of HM, gels are
formed only in low pH and high sugar concentrations. Generally, HM concentration 1%, pH
2.8~3.3 and sucrose concentration 58%~75% facilitate the gelation of HM. In HM, the crosslinking of pectin molecules involves a combination of hydrogen bonds and hydrophobic
interactions between the molecules. Low pH suppresses the dissociation of carboxylic groups
and the loss of charges minimizes the electrostatic impulsion between HM molecules.
Meanwhile, sugars compete for water molecules and reduce the solvation of HM chains,
facilitating the hydrogen bonding between HM molecules and consequently their gelation.
HM gels can maintain their original properties even when heated at 100 C.
The strength of pectin gels is positively proportional to the molecule weights and intermolecular association of pectins. Generally, the gelation time increases as the degree of
methyl esterification increases from 30%~50%, because the raise of carbomethoxy groups
increases the steric hindrance for hydrogen bonding between pectin molecules. Pectins with
degree of methyl esterification in the range 50%~70% have enhanced hydrophobic
interactions and therefore gel in shorter time. The gelling characteristics of pectins are the
function of degree of methyl esterification, as shown in Table 3-16.
In the case of LM, the presence of divalent ions, such as Ca2+, is a prerequisite for their
gelation and the ions function as the bridge between LM molecules. Increasing the
concentration of Ca2+, which is the only divalent cation allowed in the food industry,
increases the gelling temperature and gel strength of LM, which is similar to the role of Ca2+
in the formation of the egg-box structure in alginate gels. LM is not as sensitive to pH as HM
and can gel in a wider pH range 2.5~6.5. Though sucrose is not a prerequisite for LM
88
gelation, the addition of 10%~20% sucrose markedly improves the texture of gels. LM gels
are less rigid or elastic than common pectin gels, but sugars or plasticizing agents improve the
properties. LM pectin, since it does not require sugar for gelation, is used to make dietetic
jams, jellies, and marmalades.
Agar
Agar is a gelatinous polysaccharide extracted from some species of Rhodophyceae by a
hot water extraction process.
Gelling conditions
pH
Sugar concentration
(%)
2.8~3.4 65%
2.8~3.4 65%
2.5~2.6 None
Presence of
divalent ions
No
No
Yes
Rate of
gelation
High
Low
High
The hydroxyl groups on the chains are more or less esterified by methyl, sulfuric acid,
and pyruvic acid. Commercial agar is colorless or light yellow strips or powder. Agar is
insoluble in cold water, but dissolves slowly in hot water. The -1,4-glycodic bonds can be
specifically hydrolyzed by the agarlytic enzymes derived from soil and marine organisms to
yield agar oligosaccharide. Figure 3-44 illustrates the structure of agarose.
Carbohydrates
89
90
Application
Agar is a most potent gelling agent in the food industry and is widely used in candies,
puddings, ice cream, gelly, and many other foods as gelling agent. Besides, agar is
indigestible and is a good source of dietary fiber. In the fermentation industry, agar has been
widely used to encapsulate enzymes and microbes.
Carrageenan
Carrageenans are mixtures of several related galactans having sulfate half-ester groups
attached to the sugar units and are extracted from the red seaweeds (Rhodophyceae).
Carrageenans are important commercial hydrophilic gels.
Carrageenans are linear chains of D-galactopyranosyl units joined with alternating (1,3)D- and (1,4)-D-glycosidic linkages, with most sugar units having one or two sulfate groups
esterified to a hydroxyl group at carbon atoms C-2 or C-6. The molecular weights (MWs) of
carrageenan range from (1~5)105 and the average MW of food-grade carrageenans is 2105.
According to the positions of sulfate half-ester groups, carrageenans are divided into -, -, -,
-, -, -, and - classes. Figure 3-45 presents the structures of the 7 carrageenan classes.
Table 3-17. Properties of -, -, and - carrageenans
Item
Solubility
Condition
Hot water
-carrageenan
Soluble above 70C
Cold water
Hot milk
Cold milk
Gelling
properties
Miscibility
-carrageenan
Soluble above
70C
Ca2+ salt gives
thixotropic
dispersions
-carrageenan
Soluble
Soluble
Insoluble
Cold milk
(Tetrasodium
pyrophosphate)
Concentrated sugar
solutions
Concentrated salt
solutions
Organic solvents
Cations
Thickens or gels
Thickens or gels
Soluble hot
Difficulty soluble
soluble
Disperses with
thickening
Increased
thickening or
gelling
Soluble hot
Soluble hot
Soluble hot
Insoluble
Hard gel with K+
Insoluble
Non-gelatinous
Gel type
Insoluble
Strong gel with
Ca2+
Elastic without
syneresis
Non-synergetic
Non-gelatinous
91
Carbohydrates
Function
Ice cream formation and
syneresis inhibition
Coca suspension
Smoothing and texture
modifier
Syneresis inhibition,
shape retention, and curd
formation reduction
Fat and protein
stabilization
Gelling agent and texture
modification
Ingredients suspending
and texture modification
Texture modifier and
Food
Dessert gels
Function
Gelling
Fruit drinks
Bread
Pie
Seasonings
Canned foods
Meats
Beer
Alginate
Alginate, also termed algin or alginic acid, is an anionic polysaccharide obtained from
brown seaweeds. Commercial alginate is often available as sodium salt.
92
Property utilized
Thickening, hydratability,
reaction with Ca2+
Gelling, thickening, and
emulsifying
Gelling, thickening, acid
resistance
Gelling
Foam stabilizing,
coagulating, clarifying
Thickening, bonding
Stabilizing, bonding
Alginate type
Sodium alginate, calcium
alginate, PGA1
Sodium alginate, calcium
alginate, PGA
PGA, sodium alginate
PGA, sodium alginate
PGA, sodium alginate
Sodium alginate, calcium
alginate, PGA
Sodium alginate, PGA
Carbohydrates
93
94
from the hemoproteins of meat during heat processing or storage. This would in turn inhibit
the catalytic activity of iron ions [30].
Functional ingredients
After chitosan is absorbed, it can form indigestible complexes with triglycerides, fatty
acids, bile acid, and cholesterol. To complement for the bile acid that is associated with
chitosan, the liver increases the secretion of bile acid. Since bile acid is converted from
cholesterol in the liver, the content of cholesterol in liver and blood is deceased. Hence,
chitosan is an effective ingredient of functional foods.
Juice clarificant
Fruit juices become turbid after long-time storage due to the presence of negatively
charged pectin, cellulose, tannin, and pentosan. The positively charged chitosan can coagulate
these components by electrostatic attraction and hence is widely used in fruit juice
clarification. Chitosan has high affinity to polyphenolic compounds, such as catechin and
cinnamic acid. Chitosan has been added to grape wines to remove these components.
Chitosan-treated grape wines are dark golden yellow compared to the light yellow of
untreated products and hence have improved quality.
Water clarificant
Chitosan is more effective in removing polychlorobiphenyl (PCB) than active carbon.
Chitosan in combination with bentonite can effectively remove particles, color, and odor of
drinking water and that in combination with polysilicate, polyaluminosilicate, and ferric
chloride markedly reduces the COD and turbidity of water.
Carbohydrates
95
Antibacterial agent
The antibacterial activity of COS is related to its molecular weight and medium pH. It is
generally recognized that COS of molecular weight 1500 has the highest antibacterial
activity. Medium pH affects the dissociation of amino groups and therefore influences the
antibacterial activity. COS is more effective in inhibiting microbial growth in acidic medium
than in neutral or alkaline medium. Short-chain COS, such as those with seven or more
monomers, can enter inside microbial cells and inhibit the biosynthesis of mRNA and
proteins by binding to DNA, thus killing the microbes.
COS is more effective in inhibiting the growth of molds in soy sauce than benzoic acid
and sodium benzoate without affecting the taste and color of soy sauce.
Preservative
COS has abundant free amino and hydroxyl groups and therefore has strong water
retention capability. The mixture of COS and high-molecular weight chitosan with strong
film forming ability has been used as fruit and vegetable coatings to prevent water
evaporation and Vc loss and elongate the shelf life. COS also significantly reduces the
spoilage rate of fruits and vegetables as chitosan.
Calcium absorption enhancer
COS of DP 3~7 reduces the excretion of fecal calcium and increases the fracture force of
rat thighbone in contrast to chitosan, which hinders the absorption of calcium.
96
reduces the viscosity and delays the arrival of the peak viscosity. Wheat starch synergistically
improves the viscosity of guar gum solutions.
Guar gum prevents ice crystal growth and produces desired consistency, chewiness, and
heat stimulation resistance in ice cream. In cheese, guar gum is added to avoid syneresis. In
bakery foods, guar gum elongates the shelf life and reduces the water absorption of sucrose in
the glace of pastries.
Locust bean gum, also called carob gum, occurs in the seeds of carob tree (Ceratonia
siliqua). It structure is similar to that of guar gum, except that the galactose residues are
distributed randomly along the -1,4-linked mannose backbone.
The ratio of mannose/galactose residues of locust bean gum ranges from 3:1 to 6:1 and its
molecular weight is about 31000. Due to the irregular distribution of galactose residues, some
mannose residues are exposed or naked without attached galactose residues. Due to this
difference, locust bean gum has different properties compared to guar gum. For example, the
viscosity of locust bean gum solutions is lower than that of guar gum solutions.
Locust bean gum is used as a thickener, binder and stabilizer in canned meats, salad
dressings, sausages, soft cheeses, and ice creams. It also improves the water binding capacity
of dough especially in the case of low-gluten flour. Locust bean gum can improve the
viscosity of other gelatinous polysaccharides. For example, the viscosity of the solution
containing 0.5% agar and 0.1% locust bean gum is 5 times higher than that of agar alone.
Gum Tragacanth
Gum tragacanth is a plant exudate collected from the plants of the Astragalus genus. The
gum has been used for over 2000 years as Arabic gum and is mainly produced in Iran, Syria,
and Turkey.
Gum tragacanth has a very complex structure and composition. When gum tragacanth is
suspended in water, one fraction is dissolved and this part is called tragacanthic acid.
Tragacanthic acid accounts for 60%~70% of gum tragacanth and consists of 43% Dgalacturonic acid, 10% fucose, 4% D-galactose, and 40% D-xylose and L-arabinose, of
which, the galacturonic acid residues form the backbone and the other residues are attached as
side chains. The molecular weight of tragacanthic acid is about 800000. The insoluble
fraction is termed bassorin, which contains 75% L-arabinose, 12% D-galactose, and 3% Dgalacturonase and L-rhamnose with molecular weight of 84000.
Carbohydrates
97
Gum tragacanth produces high viscosity and hence is used as thickening agents. Gum
tragacanth is used as a thickening agent and a stabilizer in salad dressings (0.41.2%) and in
fillings and icings in bakery goods. As an additive in ice creams (0.5%), it provides a soft
texture.
Microbial Polysaccharides
Microorganisms can produce multiple polysaccharides, of which, dextran and xanthan are
the most important for the food industry.
Dextran is an extracelluar polysaccharide produced by Leuconostoc mesenteroides,
Streptobacterium dextranicum, Streptococcus mutans and other species. Dextran is composed
of glucose units, of which, the monomers in the straight chain are connected through -1,6
linkages, while branches begin mainly from -1,3 linkages (Figure 3-47), with part 1,4- and
1,2- linkages. The type and number of the glycosidic linkages vary with the source. The
dextran produced by Leuconostoc mesenteroides NRRL B512 contains 95% 1,6- linkages and
the remaining 5% are 1,3- and 1,4- linkages.
Dextran is used in confections to improve viscosity and water retention and inhibit sugar
crystallization. In chewing gum and soft sweets, dextran is added as gelling agent. Dextran
inhibits ice crystal formation in ice creams and provides desired consistency and mouthfeel
for puddings.
98
Xanthan is secreted by multiple species of the Flavobacterium genus and the commercial
xanthan is produced by Xanthomonas campestris. Xanthan can be considered as derivative of
cellulose.
On an average, every second glucose residue bears in the 3-position a trisaccharide of the
structure -D-Manp- (14)--D-GlcpA(12)--D-Manp as the side chain. The mannose
bound to the main chain is acetylated in position 6 and ca. 50% of the terminal mannose
residues occur ketalized with pyruvate as 4,6-O-(1-carboxyethylidene)-D-mannopyranose
(Figure 3-48). The molecular weight of xanthan is greater than 2106 Dal.
Xanthan is readily soluble in both cold and hot water and provides high viscosity even in
low concentrations, but the jellification is weakened in high xanthan concentrations. Xanthan
solutions are pseudoplasitc fluids and exhibit obvious shear thinning. Xanthan is compatible
with most edible salts and edible acids and can coexist with them in foods. Xanthan interacts
with guar gum to give rise to a synergistic increase in solution viscosity and with locust bean
gum to produce a heatreversible gel.
Xanthan is widely used to stabilize aqueous dispersions, suspensions, and emulsions.
Xanthan is added to juices and canned foods as suspending and stabilizing agents. In starch
gels, the addition of xanthan gum substantially improves their freeze-thaw stability and
reduces syneresis. Due to the high stability of xanthan gels, xanthan can be used in seasonings
with high salt contents or acidity.
Glucomannan
Glucomannan is slightly branched polymer consisting of -(14)-linked D-mannose and
D-glucose in a ratio of 1.6:1. Short side chains of 11-16 monosaccharides occur at intervals of
50-60 units of the main chain attached by 13 linkages. Some native glucomannan are
partially acetylated at C-2 and C-3 of certain of mannose residues [31]. The weight-average
molecular weights range from 105~106 and depend on source.
Glucomannan is soluble in water to produce highly viscous pseudoplastic fluids. In
alkaline conditions, glucomannan is deaceylated and aggregates to form the threedimensional network and strong thermo-irreversible gel [32]. However, glucomannan can
interact with xanthan to yield thermo-reversible gel.
Glucomannan has strong hydrophilicity, gelation capacity, and film-forming ability.
Glucomannan is added to jellies, jams, confections, dietary products, ice creams, meat
products, and breads as thickening and stabilizing agents.
Gum Arabic
Gum Arabic is extracted from the exudate of various Acacia species, primarily Acacia
senegal. Gum Arabic is a proteoglycan and its molecular weight lies in the range
260000~1160000. The glycan fraction accounts for 70% of the total gum and consists of Larabinose, D-galactose and D-glucuronic acid in the molar ratio of 3.5:1.1:2.9:1.6. The
backbone of gum Arabic consists of -D-galactopyranosyl residues linked by 13 bonds and
side chains are attached at position 6 (Figure 3-49). Gum Arabic is present as acidic or neutral
salts and the counter ions are Ca2+, Mg2+, and K+. The protein fraction accounts for 2% of the
Carbohydrates
99
total gum, but the value can reach up to 25% in some species. The glycan fraction is
covalently connected to the hydroxyproline and serine residues of the protein fraction.
Gum Arabic is readily soluble in water and provides low viscosity, but the viscosity
increases dramatically in high gum Arabic concentrations. This property is different from
other polysaccharides, which can provide high viscosity even in low concentrations. The
solubility of gum Arabic reaches up to 50% by weight. Arabic gum solutions with
concentration less than 40% are Newtonian fluids, but those with higher concentrations
exhibits the pseudoplastic behavior.
In the presence of ions, the viscosity of gum Arabic solutions varies with pH and the
highest viscosity is obtained at pH 6~8. The viscosity reduces proportionally when the
valence and concentration of ions increases. Gum Arabic is compatible with most gums,
except gelatin and sodium alginate.
100
Gum Arabic is used as emulsifier and stabilizer. It retards sugar crystallization and fat
separation in confectioneries and large ice crystal formation in ice creams, and can be used as
a foam stabilizer in beverages. Gum Arabic is also applied as a flavor fixative in the
production of encapsulated, powdered aroma concentrates. For example, essential oils are
emulsified with gum Arabic solution and then spray-dried. In this process, the polysaccharide
forms a film surrounding the oil droplet, which protects the oil against oxidation and other
changes.
DIETARY FIBER
Dietary fibers (DF) were once considered as nonnutritive crude fibers and unimportant
for human diets. However, with the rapid improvement of social economy and people's living
standards, people dietary structure changes greatly. The proportion of plant-derived foods in
diets decreases obviously and that of animal-derived foods containing high calorie, high
protein content and high fat contents increases significantly instead, which impairs the
nutrition balance of the diets. Due to the imbalance, the incidences of adiposity, hypertension,
diabetes, cancer, and cardiovascular diseases keep rising. The emergency of these diseases
has been contributed to the decreased intake of DF and DF has been widely accepted as the
seventh essential nutrient.
Carbohydrates
101
SDF and IDF have different physiological and health functions. IDF cannot be
metabolized by human body, but can absorb water as it moves through the digestive system,
thus easing defecation. SDF can be partially fermented by the microorganisms inhabited in
the colon and produce active byproducts. SDF protects against cholesterol gallstone [33],
increase heavy metal evacuation, reduce cholesterol levels in serum and liver, inhibit
postprandial blood glucose increase, and prevent hypertension and heart disease. IDF
increases defecation and prevents obesity, laxation, and intestinal cancers. The ratio of IDF to
SDF markedly affects the physiological functions of DF.
By Source
DF can be obtained by extraction from plants (including algae) and animals or by
synthesis, of which, plants are the major source at present. Chitin and chitosan are typical
representatives of animal-derived DF. Dextran is a water soluble DF. In addition to
microorganism, it is also synthesized from dextrin by transglucosylation of dextrin dextranase
(EC 2.4.1.2) [34].
Physichemical Properties
Solubility and viscosity
DF molecules with ordered and less branched structures have strong inter-molecular
bonding capacities and thereby poor solubility. For example, the linear cellulose is insoluble,
but pectins with irregular structure are readily water soluble. Insoluble DF can be converted
to soluble DF by high temperature, high pressure, or shearing force. Conversion of IDF to
SDF is an important measure to improve DF quality. SDF are viscous upon ingestion and can
complex with heavy metals, fats, and cholesterol.
Water retention
Most DFs contain abundant hydrophilic groups and can absorb much water. The water
retention capacity of DFs varies with the source, composition, structure, preparation method,
and particle size. Generally, cellulose-based DFs have lower water retention capacity
compared with other DFs. Too low particle sizes reduce the index. Besides, high temperature
treatment, cooking, and enzymatic hydrolysis could change the physical properties of DFs
and thereby influence the water retention capacity.
Organic compounds absorption
The abundant active groups on the surface of DF can absorb bile acid, cholesterol, and
mutagens in the intestines of human body and therefore affects their metabolism and
adsorption.
Cation binding and ion exchange
102
Some DFs contains carboxyl groups, hydroxyl groups, amino acids, and some other
active groups. Various cations, such as Ca2+, Fe2+, Zn2+, Cu2+, and Pb2+, can bind to these
groups or exchange with the ions attached to these groups. The binding or exchange is
reversible and changes the pH, osmotic pressure, and redox potential of the intestine and
provides a buffering environment that is beneficial for digestion and absorption. Cations with
high polarizability, such as Pb2+, are preferred in absorption by DF. Hence, DF has the
function of removing toxic metals. The ions bound to DF can exchange with Na+ and K+. The
exchange reduces the Na+/K+ ratio in the blood and consequently lowers the blood pressure. It
should be noted that DF also reduces the adsorption of some beneficial elements. Hence, it is
necessary to supplement some minerals in DF-containing foods to avoid mineral imbalance.
Prebiotics
DFs are only partially fermented in the colon. DFs are the nutrition source of the
microbes in the colon and support the growth of multiple bacteria, of which, most are
beneficial for human body. Besides, DFs can induce the substantial propagation of aerobes
and thereby reduces the incidence of some cancers.
Bulking effect
DFs have markedly increased volume after swelling and can cause satiety. Besides, the
presence of DF affects the digestion and absorption of other food components and delays the
feeling of hunger. Hence, DFs are effective in preventing adiposity.
Metabolism
As mentioned in the definition, DFs cannot be digested in the mouth, stomach, or small
intestine and only partially fermented by the microbes in the large intestine. The degree and
rate of decomposition are associated with the solubility, chemical structure, particle size, and
ingestion mode of DF. Soluble DFs, such as pectin and seaweed gums, are readily digested in
the large intestine, but insoluble cellulose cannot be easily utilized by intestinal
microorganisms. Some of the metabolites, such as fatty acids, can be absorbed by human
body as energy source and some metabolites have important physiological functions.
Safety Aspects
Although DFs have multiple beneficial effects on human body, excessive intake of DFs
can cause discomfort and affect the absorption of fats, proteins, and essential elements. It
should be mentioned that these effects vary with DF composition and individuals.
Some IDFs, such as guar gum, can be fermented by intestinal microorganisms to produce
volatile fatty acids, carbon dioxide, and methane, which can cause abdominal distension. The
filling effect of DFs reduces the adsorption of proteins, fatty acids, and carbohydrates and the
increased viscosity of gastrointestinal fluids prevents the contact between these substrates
Carbohydrates
103
with digestive enzymes. Hence, DFs reduce their bioavailability. DFs can bind metal ions and
can reduce their absorption.
Some DFs interfere with the absorption of vitamins. It is reported that konjac mannan
reduces fat-soluble vitamin absorption by removing bile acids, but does not reduce fatinsoluble vitamin absorption in the intestine [35].
No uniform standards have been formulated for the daily intake of DFs due to the
complexity of DFs and individual differences. The daily intake recommended by FDA is
20~35g for adults and that in Japanese is 20 g or more. The Chinese Nutrition Association
enacted the Chinese dietary intake references in 2000 and suggests that the daily dietary fiber
intake of adults is 30.2 g.
REFERENCES
[1]
104
[13] Morales, FJ; Jimnez-Prez, S. Free radical scavenging capacity of Maillard reaction
products as related to colour and fluorescence. Food Chemistry, 2001, 72, 119-125.
[14] Plakas, SM; et al., Effect of Maillard Browning Reaction on Protein Utilization and
Plasma Amino Acid Response by Rainbow Trout (Salmo gairdneri). The Journal of
Nutrition, 1985, 115, 1589-1599.
[15] Whitelaw, ML; Weaver, CM. Maillard Browning Effects on In Vitro Availability of
Zinc. Journal of Food Science, 1988, 53, 1508-1510.
[16] Nagao, M., et al., Mutagens in coffee and tea. Mutat Res, 1979, 68, 101-106.
[17] Martins, SIFS; Jongen, WMF; van Boekel, MAJS. A review of Maillard reaction in
food and implications to kinetic modelling. Trends in Food Science and Technology,
2000, 11, 364-373.
[18] Alink, GM; van Boekel, MAJS; Jongen, WMF. Mutagenicity of Heated Sugar-Casein
Systems: Effect of the Maillard Reaction. Journal of Agricultural and Food Chemistry,
2000. 48, 2271-2275.
[19] Monti, SM; Bailey, RG; Ames, JM. The influence of pH on the non-volatile reaction
products of aqueous Maillard model systems by HPLC with diode array detection.
Food Chemistry, 1998, 62, 369-375.
[20] Wedzicha, BL; Adamu, DJM. Reactivity of vegetables towards sulphur dioxide. Food
Chemistry, 1987, 26, 159-173.
[21] Kanner, J; Shapira, N. Oxygen- and Metal-Ion-Dependent Nonenzymatic Browning of
Grapefruit Juice, in Quality Factors of Fruits and Vegetables. American Chemical
Society, 1989, 55-64.
[22] Moreno, F.J., et al., High-Pressure Effects on Maillard Reaction between Glucose and
Lysine. Journal of Agricultural and Food Chemistry, 2002, 51, 394-400.
[23] Friedman, M., Food Browning and Its Prevention: An Overview. AU - Friedman,
Mendel. Journal of Agricultural and Food Chemistry, 1996, 44, 631-653.
[24] Chen, H., et al., Chemical composition analysis of soybean oligosaccharides and its
effect on ATPase activities in hyperlipidemic rats. International Journal of Biological
Macromolecules, 2010, 46, 229-231.
[25] Caicedo, L; Silva, E; Snchez, O. Semibatch and continuous fructooligosaccharides
production by Aspergillus sp. N74 in a mechanically agitated airlift reactor. Journal of
Chemical Technology and Biotechnology, 2009, 84, 650-656.
[26] Lee, HW, et al., Chitosan oligosaccharides, dp 2-8, have prebiotic effect on the
Bifidobacterium bifidium and Lactobacillus sp. Anaerobe, 2002, 8, 319-324.
[27] Krastanov, A; Yoshida, T. Production of palatinose using Serratia plymuthica cells
immobilized in chitosan. Journal of Industrial Microbiology and Biotechnology, 2003,
30, 593-598.
[28] T., M., et al., Lactulose as a sugar with physiological significance. Bulletin 212,
International Dairy Federation, Brussels, 1987, 69-76.
[29] Galliard, T., Starch: Properties and Potential. 1st edition. Chichester: John Wiley and
Sons; 1987.
[30] Kamil, JYVA; Jeon, YJ; Shahidi,F. Antioxidative activity of chitosans of different
viscosity in cooked comminuted flesh of herring (Clupea harengus). Food Chemistry,
2002, 79, 69-77.
[31] Teleman, A., et al., Isolation and characterization of O-acetylated glucomannans from
aspen and birch wood. Carbohydrate Research, 2003, 338, 525-534.
Carbohydrates
105
[32] Huang, L., et al., Gelation Behavior of Native and Acetylated Konjac Glucomannan.
Biomacromolecules, 2002, 3, 1296-1303.
[33] Schwesinger, W.H., et al., Soluble dietary fiber protects against cholesterol gallstone
formation. The American Journal of Surgery, 1999, 177, 307-310.
[34] Yamamoto, K.;Yasuda, J; Too, K. Arrhythmias in newborn Thoroughbred foals.
Equine Veterinary Journal, 1992, 24, 169-173.
[35] Doi, K., et al., Influence of dietary fiber (konjac mannan) on absorption of vitamin B12
and vitamin E. Tohoku J Exp Med, 1983, 141, S677-S681.
ISBN: 978-1-61942-125-7
2012 Nova Science Publishers, Inc.
Chapter 4
LIPIDS
1
ABSTRACT
Lipids are a broad group of naturally-occurring molecules that are soluble in organic
solvents but insoluble or only sparingly soluble in water. Triacylglycerols account for
95% of total lipids in foods. Lipids are major energy source for human body and protect
human body from mechanical damage and heat loss. Lipids are also the carriers of fatsoluble vitamins and the precursors of many bioactive molecules such as prostaglandin,
sex hormone, and epinephrine. This chapter deals with the nomenclature, classification,
and fatty acid distribution theories of lipids and their functional properties, including
polymorphism, plasticity, and emulsification. Lipids undergo multiple chemical reactions
during processing and storage, such as hydrolysis, oxidation, and thermal decomposition.
The effects of these reactions, especially oxidation, on food flavor and safety are
elucidated in detail. Lipid processing techniques, including refinement, hydrogenation
and interesterification, are also concerned in this chapter.
1. INTRODUCTION
It should be understood that though the term lipid is used majority of the times as a
synonym for fats, in fact, fats are a subgroup of lipids called triglycerides. Lipids encompass
molecules such as fatty acids and their derivatives including tri-, di-, and monoglycerides and
phospholipids, as well as other sterol-containing metabolites such as cholesterol. Humans and
other mammals have a variety of pathways to synthesize and metabolize lipids. Some lipids
cannot be synthesized by mammals and therefore must be ingested from the diet. Such lipids
are termed essential fatty acids (EFAs).
108
All plants and animals eaten by humans contain lipids. Various vegetables and most fruits
contain very little amounts of lipids, generally about 0.3%, except avocado, whose edible
portion contains about 20% lipids. The lipid content in the muscle tissue of lean beef, fish,
white poultry, and shell fish is about 2%, about 3.7% in cows milk, about 2-4% in grains,
about 30% in fatty pork, 32% in an egg yolk, and about 35% in fillets of fatty fish. Oilbearing nuts and seeds contain from 20% fat in soybeans to 65% fat in walnuts.
1.1. Nomenclature
1.1.1. Fatty Acids
Fatty acids refer to any aliphatic monocarboxylic acids that are released by the hydrolysis
of naturally occurring lipids. More than 800 natural fatty acids have been identified, of which,
most contain a linear chain and even number of carbon atoms. Based on the presence or
absence of double bonds, lipids are divided into saturated and unsaturated fatty acids.
Palmitic acid and stearic acid are examples of saturated fatty acids. Unsaturated fatty acids
contain two or more double bonds. For instance, oleic acid has only one double bond, linoleic
acid has two double bonds, linolenic acid contains three double bonds, and arachidonic acid
contains up to four double bonds.
Fatty acids can be named by using one of the following four nomenclature systems.
Trivial nomenclature
Lipids are named according to their sources, such as palmitic acid, lauric acid, butyric
acid, stearic acid, and oleic acid.
Systematic nomenclature
Carbon atoms are counted from the carboxylic acid end.
Symbol nomenclature
Fatty acids can be represented by a simple numerical expression consisting of two terms
separated by a colon, with the first term depicting the number of carbon atoms and the second
the number of double bonds. For example, hexadecanoic acid,
CH3CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2COOH
can be named as 16:0 and linoleic acid (9, 12-octadecadienoic acid) can be presented as 18:2.
This notation can be ambiguous, because some different fatty acids might have the same
numbers.
Omega-x or n-x nomenclature
109
Lipids
Unsaturated fatty acids can be named in the n-x or -x system. In this system, the
terminal methyl carbon is designated as or n and x represents the location of the first double
bond. Carbon atoms are counted from the terminal methyl carbon (namely or n) to the
carbonyl carbon. Because all adjacent double bonds in all natural polyenoic acids (containing
2 to 6 double bonds) are spaced by a methylene, the locations of all other bonds can be
determined if the first double bond is specified. For example, linoleic acid is presented as
18:2(-9). Because the first double locates in the 9th carbon, the second double occurs
between C12 and C13.
The geometric configuration of double bonds is usually designated by the use of cis and
trans, indicating whether the alkyl groups are on the same or opposite sides of the molecule.
Unsaturated fatty acids occur naturally in the cis form, but the trans form is more
thermodynamically stable.
If the four groups attached to the two carbon atoms of a double bond are different, the
configuration can be designated according to the Cahn-Ingold-Prelog rules. In this system,
each group is assigned a priority. If the two groups with higher priority (greater atom number)
locate in the same side of the double bond, the letter Z is used to designate the configuration.
If the two groups are on the opposite sides, the letter E is used.
Table 4-1 lists the systematic and common names of some fatty acids in naturallyoccurring lipids.
Table 4-1. Nomenclature of some common fatty acids
Abbreviation
4:0
6:0
8:0
10:0
12:0
14:0
16:0
16:1(n-7)
18:0
18:1(n-9)
18:2(n-6)
18:3(n-3)
20:0
20:4(n-6)
20:5(n-3)
22:1(n-9)
22:5(n-3)
22:6 (n-6)
Systematic name
Butanoic
Hexanoic
Octanoic
Decanoic
Dodecanoic
Tetradecanoic
Hexadecanoic
9-Hexadecanoic
Octadecanoic
9-Octadecanoic
9,12-Octadecanoic
9,12,15- Octadecanoic
Arachidic
5,8,11,14-Eicosatetraenoic
5,8,11,14,17-Eicosatetraenoic
13-Docosenoic
7,10,13,16,19-Docosapentaenoic
4,7,10,13,16,19-Docosahexaenoic
Common name
Butyric
Caproic
Caprylic
Capric
Lauric
Myristic
Palmitic
Palmitoleic
Stearic
Oleic
Linoleic
Linolenic
Eicosanoic
Arachidonic
EPA
Erucic
Symbol
B
H
Oc
D
La
M
P
Po
Sta
O
L
Ln
Ad
An
E
DHA
Note: aSome authors use S for stearic, but this can be confusing, since S is also used for saturated
whenever triaclycerol composition is expressed in terms of saturated (S) and unsaturated (U) fatty
acids. For example, S3 or SSS=all three fatty acids saturated, SU2 or SUU = diunsaturated
monosaturated, and so on.
110
Figure 4-1. Structure of acylglycerols. R denotes fatty acid; there may be fatty acid, two fatty acids or
three fatty acids in the acylglycerols, which is mono-acyglycerol, di-acyglycerol or triacylglycerol
respectively; R1=R2=R3, the triacylglycerol is defined as simple triacylglycerol, otherwise mixed
triacylglycerol.
1.1.2. Acylglycerols
Lipids are the mixtures of mono-, di-, and triesters of glycerol with fatty acids, which are
termed monoacylglycerols, diacylglycerols, and triacylglycerols, respectively. Natural fats are
mainly present as triacylglycerols.
In order to designate the configuration of glycerol derivatives, the stereospecific
numbering (Sn) system is used in acylglycerol nomenclature. In this system, the carbon atom
that appears on top in that Fischer projection that shows a vertical carbon chain with the
hydroxyl group at carbon-2 to the left is designated as C-1 and the prefix 'sn' (for
stereospecifically numbered) is printed immediately preceding the glycerol term. An example
is shown in Figure 4-1. If R1 denotes stearic acid (St), R2 oleic acid (O), and R3 linoleic acid
(L) in the structure, this triacylglycerol is named Sn-glycerol-1-stearic acid-2-oleic acid-3linoleic acid, Sn-18:0-8:1-18:2, or Sn-StOL.
If the product is the racemic mixture of two antipodes, the prefix 'rac-' (for racemo) can
be used preceding the full name, such as in rac-StOM. In this case, the middle acid (O,
standing for the oleic acid) is in position 2 and the remaining two fatty acids (St and M,
standing for stearic and myristic acids respectively) are equally distributed in positions 1 and
3.
If the prefix is used before the name, such as -StOM, it indicates that the middle acid
is in position 2, but the distribution of the other two acids is unknown.
In the case of simple triacylglycerols or those with unknown fatty acids distribution, the
prefix can be omitted. For example, StOM can be used to express any mixture of Sn-StOM,
Sn-MOSt, Sn-OStM, Sn-MStO, Sn-StMO, and Sn-OMSt.
1.1.3. Phospholipids
Phospholipids refer to any lipids that contain phosphoric acid in the structures as monoor diester. According to the type of hydroxyl donors, phospholipids are divided into
phosphoglycerides and sphingolipids (sphingophospholipids), in the former structure the
alcohol is glycerol and the later sphingosine.
Lipids
111
1.2. Classification
Based on chemical structure and composition, lipids can be divided into simple lipids,
compound lipids, and derived lipids.
Simple lipids are compounds consisting of fatty acids and alcohols and include fats, oils,
and waxes.
Compound lipids contain many other groups in addition to fatty acids and alcohols.
Glycerophosphonolipids, sphingomyelins, cerebroside, and ganglioside are the examples of
compound lipids.
Derived lipids are the derivatives of simple and compound lipids and have the common
properties of lipids. Steroids, hydrocarbons, carotenoid, and fat-soluble vitamins are examples
of this group.
Most lipids in foods are acylglycerols. According to composition, lipids in animal and
plant-derived foods are divided into the following:
Milkfat
Milkfat exists in the latex of mammals. Milkfat consists mainly of palmitic acid, oleic
acid, and stearic acid. Compared with other animal-derived lipids, milkfat contain abundant
C4~C12 short-chain fatty acids, small amounts of odd- and branch-chain fatty acids, and
trans double bonds.
Laurates
Laurates are mainly found in palme plants such as coconut palm and babassu. Laurates
are featured by their high lauric acid contents, which reach up to 40%~50%. Laurates have
medium contents of C6, C8, and C10 fatty acids, low unsaturated fatty acid contents, and low
melting points.
Plant butter
Plant butter originates from the seeds of tropical plants and is characterized by narrow
melting point range. Although plant butter has a higher content of saturated fatty acids than
112
unsaturated fatty acids, trisaturated glycerides have not been identified in plant butter. Plant
butter is widely used in candies and cocoa butter is the most important plant butter.
Oleate-linoleate
Lipids of this category are the most abundant in nature and are found only in plants. The
lipids have high contents of oleic acid and linoleic acid and the contents of saturated fatty
acids are less than 20%. Peanut oil, corn oil, olive oil, palm oil, sesame oil, cottonseed oil,
and sunflower oil are important members of this category.
Linolenates
Linolenates contain large amount of linolenic acid and soybean oil, wheat germ oil, and
perilla oil belong to this category.
Animal fats
Lipids of this group, such as lard and tallow, are the storage fat of domestic animals.
Animal fats contain large amount of C16 and C18 fatty acids and medium contents of
unsaturated fatty acids, mostly oleic and linoleic acids, and small amount of odd-numbered
fatty acids. Animal fats contain appreciable amount of fully saturated triacylglycerols and
thus exhibit high melting points.
Marine oils
Marine oils contain abundant long-chain unsaturated fatty acids and are rich in vitamins
A and D. Eicose pentaenois acid (EPA) and docosahexenoic acid (DHA) are typical examples
of this category. Due to high unsaturation degree, marine oils are susceptible to oxidation.
Lipids
113
molecule; that is, only SXX and SSX should be present. If a fatty acid forms more than twothirds of the total acids, it should occur at least twice in every molecule; that is, only SSX and
SSS should be present.
However, analysis of many natural fats, especially those of animal origin, reveals marked
deviation from this theory. Trisaturated acylglycerols have been found in fats containing less
than 67% saturated fatty acids. This theory is applicable only to triacyglycerols that consist of
two components and does not take positional isomers into consideration. This theory is no
longer considered valid.
Random (1, 2, 3-Random) distribution theory
According to this theory, fatty acids are distributed randomly both within each
triacylglycerol molecule and among all the triacylglycerols. Thus, the fatty acid composition
of all the three positions of glycerol should be the same and also equivalent to the fatty acid
composition of the total fat. The proportion of any given fatty acid species can be calculated
according to the following equation:
%sn-XYZ = (mol% X in total fat) mol% Y in total fat) mol% Z in total fat) 10-4.
For example, if a fat contains four fatty acids, including 8% palmitic acid (P), 2% stearic
acid (St), 30% oleic acid (O), and 60% linoleic acid (L), 64 possible triacylglycerol species
would exist. The percentages of any species can be calculated by taking the following
equations as example:
Sn-OOO(%) = 30%30% 30% 10-4 = 2.7.
Sn-PLSt(%) = 860210-4 = 0.096.
Sn-LOL (%) = 60306010-4 = 10.8.
The fatty acid distribution of most lipids does not conform to the random distribution
theory. In natural lipids, the fatty acids in the Sn-2 position are different from those in
positions Sn-1 and Sn-3. Hence, great deviation exists between the predicted and actual
distribution of fatty acids in natural lipids. However, this theory can be used to predict the
fatty acid distribution in randomly interesterified fats.
Restricted random distribution theory
This theory was initiated by Kartha in 1953 [2]. According to this theory, saturated and
unsaturated fatty acids in animal fats are distributed randomly. Fully saturated triacylglycerols
(SSS) can be present, but only to the extent that the fat can remain fluid in vivo. Excess SSS,
according to this theory, can exchange with UUS and UUU to generate SSU and SUU.
Kartha's calculations do not account for positional isomers or positioning of individual acids.
1, 3-Random-2-Random distribution
114
This theory was proposed by Vander al, Coleman, and Fulton between 1960 and 1961
based on their researches of directed hydrolysis of Sn-1 and Sn-3 fatty acids by steapsin.
According to this theory, the fatty acid composition at position 2 is different and independent
from that of positions 1 and 3 and fatty acids are distributed randomly in Sn-2 and Sn-1,3.
Thus, the composition at positions 1 and 3 will, presumably, be identical. According to this
theory, the content of any given triacylglycerol can be calculated with the following equation:
Sn-XYZ(%) = (mol%X in positions 1 and 3)(mol%Y in position 2)(mol%Z in
positions 1 and 3)10-4.
This theory is very useful in the exact predication of plant-derived lipids.
1-Random-2-Random-3-Random distribution theory
This theory was proposed by Tsuda in 1962. According to this theory, fatty acids are
separately but randomly distributed at each of the three positions of the triacylglycerol
molecules of a natural fat. Thus, the possibility of a given fatty acid appearing in each Sn
position would likely be different. The content of a given triacylglycerol species can be
calculated as:
%sn-XYZ = (mol% X at sn-1)(mol% Y at sn-2)(mol% Z at sn-3)10-4.
This theory is applicable to the predication of common animal fat, milkfat, and seed fats.
Peanut
Soybean
Position
1
2
3
1
2
3
1
2
3
14:0
16:0
34
2
37
14
2
11
14
1
13
18:0
50
2
53
5
5
6
22
6
18:1
12
87
9
59
59
57
23
70
28
18:2
1
9
19
39
10
48
7
45
18:3
9
8
20:0
20:1
1
4
1
3
20:2
20:0
1
0.5
3
115
Lipids
Table 4-2. (Continued)
Source
Beef
Pig
Position
1
2
3
1
2
3
14:0
4
9
1
1
4
-
16:0
41
17
22
10
72
-
18:0
17
9
24
30
2
7
18:1
20
41
37
51
13
73
18:2
4
5
5
6
3
18
18:3
1
1
1
20:0
20:1
20:2
20:0
Lard has different fatty acid distribution patterns compared with other animal-derived
fats. For example, palmitic acid is mainly found in position Sn-2, stearic acid is distributed in
Sn-1, linoleic in Sn-3, and oleic acid in Sn-3 and Sn-1.
In milkfat, short-chain fatty acids attach specifically to position Sn-3, while the longchain polyunsaturated fatty acids are preferably esterified at position Sn-2 of marine oils.
The fatty acid distributions of some natural fats are listed in Table 4-2.
116
Lipids
117
For example, the smoking point of refined edible oil is generally higher than 240 C, but
the presence of free fatty acids dramatically decreases the index. The flash point of plantderived edible oil is generally over 225-240 C and the fire point is usually 20-60 C higher
than the flash point.
118
heated to above 55 C until completely melts and is then allowed to cool slowly until 29 C.
The crystals are reheated to 32 C to melt other crystal forms than the form. The later
process is repeated until cocoa butter is completely transformed to the form.
2.3. Plasticity
Lard and butter that are solids in room temperature are actually the mixtures of liquid oils
and solid fats. The lipids are completely solidified only in very low temperatures. Such
homogeneous mixtures of liquid oils and solid fats are defined as the plastic fat. Plastic fat
can maintain their shape even in exposure to external forces. The plasticity of fats is affected
by the following factors:
Fat crystal form
Fat crystals in the ' form have the best plasticity, because substantial amount of small
bubbles are trapped in the ' crystals. In contrast, only a small amount of air bubbles are
trapped in crystals and the air bubbles are large in volume. Hence, fats in the form have
less plasticity.
Melting point range
Fats with wider melting point ranges exhibit better plasticity.
Solid to liquid ratio
The fat/oil ratio significantly affects lipid plasticity. If the percentage of the solid phase is
too high, rigid crosslinking occurs and the fat exhibits high hardness and poor plasticity. If the
percentage of liquid phase is too high, the fat is flowable, soft, and susceptible to
deformation.
Figure 4-4. Heat content (H) or dilatometric (D) melting curve of a glyceride mixture [3].
Lipids
119
The solid phase to liquid phase ratio is also termed as the solid fat index (SFI). SFI is the
most important index that determines the plasticity of lipids and can be determined by
measuring the expansion of the fat, i.e. the volume increase of the fat during its transition
from solid to liquid.
The volumes of solid fat and liquid oil increase when heated. The expansion without
phase transformation is defined as thermal expansion. When solid fat is transformed to the
liquid state in high temperatures, the volume increase is called melting dilation. The meltexpansion curve of plastic fats can be followed by measuring the specific volume change of
liquid oil and solid fat in different temperatures. As shown in Figure 4-4, solid fat starts to
melt at point X and is gradually melted until to point Y, at which the fat is completely
liquefied. The fat in point b is a mixture of solid and liquid. In this point, the percentage of
solid fat is ab/ac and that of liquid oil is bc/ac. Hence, the SFI in point b is ab/bc.
If a lipid melts in a very narrow temperature range, the slope between points X and Y is
high. Otherwise, the lipid exhibits a wide plastic range. Hence, the plastic range of lipids can
be modified by adding lipids with different melting points.
SFI can be measured exactly by using a dilatometer. However, measurement with
dilatometer is time consuming and is applicable only to fats with SFI less than 50%. Pulsed
nuclear magnetic resonance is the most common method for SFI determination. Because
ultrasonic travels faster in solid fat than in liquid oil, ultrasonic methods have been developed
for SFI measurement.
120
When the amount of static charge on the surface of dispersed droplets turns insufficient,
the repulsion between droplets is reduced. As a result, the droplets attach to each other and
flocculation occurs. The membranes of droplets remain intact after flocculation.
Coalescence
The membranes of dispersed droplets are disrupted and the drops move to each other,
leading to coalescence. Coalescence reduces the interface area of the dispersed phase and
planar interface might occur when coalescence is serious.
Coalescence can be prevented by adding emulsifiers. Emulsifiers are surfactants
containing both hydrophilic and lipophilic groups and are located in the oil/water interface.
Emulsifiers decrease the interfacial tension and thus reduce the energy required for emulsion
formation. Although surfactants reduce the interfacial tension, the interfacial free energy is
still positive and emulsions are still thermodynamically unstable.
2.4.2. Emulsifier
Emulsifiers are divided into anionic, cationic and nonionic types according to structure
and property. Based on origin, emulsifiers can be divided into natural and synthetic ones.
Based on functions, emulsifiers are divided into surfactants, viscosity reinforcing agents and
solid absorption agents. According to polarity, emulsifiers are divided into hydrophilic and
lipophilic ones.
Fatty monoglycerides and their derivatives (including glycerol monostearate and stearic
acid glyceride), sucrose fatty acid ester, sorbitan fatty acid ester and their derivatives (such as
sorbitan monooleate (Span 80) and polyoxyethylene sorbitan monostearate (Span 60)), and
phospholipids (such as modified soybean phospholipid), are widely used in the food industry
as emulsifiers.
Lipids
121
When foods are fried, water might migrate into hot lipids, leading to lipid hydrolysis and
fatty acid release. Frying decreases the smoke point of lipids and deteriorate the quality of
foods.
Lipid hydrolysis is not preferred in most cases. However, moderate lipid hydrolysis can
create special flavors for some foods. For example, in cheese production, microbes and milk
lipases are added to produce desired flavor. In breads and yogurts, lipid hydrolysis also
contributes to flavor formation.
3.2. Oxidation
Lipid oxidation is a major cause of quality deterioration of lipid-containing foods. Lipid
oxidation generates various off-flavors and leads to rancid (oxidative rancidity), which render
these foods less acceptable. In addition, oxidation decreases the nutritional quality of foods
and produces potential toxicants. The prevention of lipid oxidation has been recognized as an
important issue of lipid chemistry.
3.2.1. Autoxidation
The autoxidation of lipids is a typical free radical chain reaction and the autoxidation rate
is markedly inhibited by chemicals which can interfere with free radical reactions. Light and
free radical-producing substances catalyze the reaction and the quantum yields exceed unity
when the oxidation reaction is initiated by light. Lipid autoxidation yields high levels of
hydroperoxides (ROOH) and the induction periods of pure substrates are longer than mixture
substrates.
The lipid autoxidation process is comprised of three steps: initiation, propagation, and
termination.
Initiation:
Propagation:
Termination:
RHR +H
R + O2 ROO
ROO + RH ROOH + R
R + R R-R
R + ROO R-O-O-R
ROO + ROO R-O-O-R + O2
In initiation, the hydrogen atom on the -carbon atom of the double bonds of unsaturated
fatty acids or their triacylglycerols (designated as RH) is detached by metal catalysis or
exposure to light or heat and a fatty acid radical known as the alkyl radical (R) is produced.
R then reacts with oxygen to produce peroxy radicals ROO, which grabbles the hydrogen
atom from -carbon atom of another molecules (RH) to yield hydroperoxides (ROOH) and
new free radicals R. The reactions are repeated and lead to the propagation of lipid
autoxidation. Once these free radicals are combined to produce stable non-free radical
products, the chain reaction is terminated.
Initiation needs high activation energy and is therefore the limiting step of lipid
autoxidation.
122
123
Lipids
OOH
R
H2
C
C
H
C
H
CHO
C
H
C
H
C
H
CH2
CHO
CHO
C5H11
3C5H11CHO
O
C5H11
RCHO
124
Each of the four hydroperoxides has multiple geometric isomers with the conjugated
diene system in the cis, trans or the trans, trans configuration, but the unconjugated double
bond is always cis. Linolenate autoxidation results in more 9- and 16-hydroperoxides than the
12- and 13-isomers, because oxygen prefers C9 and C16 and the 12- and 13-hydroperoxides
are decomposed rapidly. The 12- and 13-hydroperoxides can form six-membered peroxide
hydroperoxide via 1,4-cyclization or prostaglandin-like endoperoxides via 1,3-cyclization.
Lipids
125
Oxygen concentration
The autoxidation of lipids is not affected by oxygen level in the case of sufficient partial
pressure of oxygen. However, when the partial pressure of oxygen is low, the lipid
autoxidation rate is proportional to the partial pressure of oxygen.
Surface area
The lipid autoxidation rate is positively correlated with the area of the interface in contact
with air. In the case of a large surface area to volume ratio, the decrease of oxygen partial
pressure exerts no significant effect on oxidation rate. In O/W emulsions, the autoxidation
rate is determined by the diffusion of oxygen to the oil phase.
126
Lipids are oxidized very rapidly in dried foods with aw less than 0.1. When aw is
increased, lipid autoxidation rate decreases dramatically. When the aw reaches 0.3, lipids are
oxidized in the minimum rate. This is because water reduces the catalytic activity of metals,
quenches free radicals, enhances non-enzymatic browning (producing antioxidant
compounds), and prevents the contact between foods and oxygen. When aw increases in the
range 0.3~0.7, the water solubility of oxygen and the fluidity of catalysts increase and more
reaction sites on substrates are exposed, leading to accelerated oxidation. When the aw further
increases, the lipid oxidation rate is reduced again due to diluted oxygen and catalyst
concentrations.
Auxiliary oxidants
Some divalent or polyvalent transit metals with appropriate redox potentials, such as Co,
Cu, Fe, Mn, and Ni, are effective auxiliary oxidants. These metals can shorten the initiation
period and accelerate lipid oxidation in concentrations as low as 0.1 mg/kg.
Light and radiation
Visible light, UV light and high-energy radiation can initiate the formation of free
radicals and decompose hydroperoxides, thus stimulating lipid oxidation. Hence, lipids or
lipid-containing foods should be stored in dark place or packed with opaque materials.
Special attention should be paid to this issue in the radiation sterilization of foods.
Antioxidants
Antioxidants can delay and retard the autoxidation of lipids. The effects of antioxidants
on lipid oxidation are detailed in Section 3.2.7.
127
Lipids
Singlet oxygen does not show obvious specificity to substrate structure and can react with
any double bonds in unsaturated fatty acids. The rate of photosensitized oxidation is
proportional to the number of double bonds and is not affected by their locations. This
property is evidenced by the rate constants of the reactions of singlet oxygen with oleic acid,
linoleic acid, linolenic acid, and arachidonic acid, which are 0.74 105 mol-1 S-1 L, 1.3
105 mol-1 S-1 L, 1.9 105 mol-1 S-1 L, and 2.4 105 mol-1 S-1 L respectively. In the
case of triplet oxygen, it is much less active and the rate constant of the reaction with linoleic
acid is only 89 mol-1 S-1 L, which is 1450 times lower than that of singlet oxygen. Hence,
the oxidation initiated by singlet oxygen predominates in the oxidation of unsaturated fatty
acids.
HOO
13
12
OOH
HOO
10
OOH
128
Lipids
129
130
R1
R3
R3
R4
R4
R2
R2
Thermal polymerization occurs either between different molecules (Figure 4-15) or inside
the same molecule (Figure 4-16).
In oxidative thermal polymerization, homolysis occurs in the -carbon of a double bond
and the resultant free radicals react with each other to produce non-cyclic dimmers or add to a
double bond to yield cyclic or non-cyclic compounds.
The thermal polymerization of lipids deteriorates the quality of foods and adversely
affects food nutrition and safety. However, these reactions are desired in some cases. For
example, thermal polymerization contributes to the formation of special flavors in fried foods.
131
Lipids
oil. In degumming, oils are added with 2%-3% water or vapor and then agitated. The water
phase is then separated by settling or centrifugation. Carbohydrates and proteins are also
removed in this step.
Neutralization
To remove free fatty acids and part phospholipids and pigments, NaOH solutions of
appropriate concentrations are added to heated oils. The resultant foots or soapstock is
separated and used for making soap.
Gossypol and aflatoxin are also removed or destroyed in neutralization.
Bleaching
Chlorophyll, lutein, carotene, and other pigments affect the appearance of oil and
decrease the stability against oxidation. These coloring materials can be removed by
absorbents, such as floridin, emathlite, and active carbon. Other impurities, such as
phospholipids, soaps, and some oxidation products are also absorbed by the absorbents. The
absorbents are then separated by filtration.
Deodorization
The off-flavors of lipids are caused by the volatile compounds generated in lipid
oxidation. These compounds can be removed by distillation in reduced pressure. Some
nonvolatile off-flavor compounds are also destroyed by water steam and are then distilled
away.
Table 4-3. Content changes of harmful substances in rapeseed oil during refining(g/kg)
Compounds
Anthracene
Phenanthrene
1,2-benzanthracene
3,4-benzopyrene
Crude oil
10.1
100
14
2.5
Neutralization
5.8
68
7.8
1.8
Bleaching
4.0
42
5.0
1.0
Deodorization
0.4
15
3.1
0.9
The quality of oils is obviously improved after refining. Table 4-3 lists the removal of
various harmful substances in rapeseed oil during refining. It should be noted that some
useful components, such as fat-soluble vitamins and natural antioxidants are lost during
refining. Hence, additional antioxidants are often added to refined oils to improve the
antioxidant capacity.
3.4.2. Hydrogenation
Hydrogenation is the addition of hydrogen to the double bonds of unsaturated fatty acids.
Due to the insufficient supply of natural solid fat, liquid oils are hydrogenated to produce
semisolid fats. Hydrogenated fats have gained wide applications in the production of
margarine and shortening oil.
132
SR
High
Low
High
High
Rate
High
High
High
High
133
Lipids
Reaction rate constants can be calculated from the starting and ending fatty acid
compositions and the hydrogenation time. Selective hydrogenation reduces the formation of
fully saturated glycerides, avoids excessive hardening of fats, and increases fat stability by
decreasing the content of linoleic acid. However, selective hydrogenation yields undesired
amount of trans isomers that cannot be absorbed by human body.
As shown in Table 4-4, both catalyst species and operating conditions affect the
hydrogenation selectivity.
3.4.3. Interesterification
The distribution pattern of fatty acids in lipids markedly affects the properties of lipids.
Because these properties affect the application of lipids in industries, interesterification has
been performed to improve lipid performance. Interesterification changes the distribution
pattern of fatty acid in triacylglycerols and is thus of industrial importance. Both intra(Figure 4-18) and inter-molecular interesterification (Figure 4-19) can occur, depending on
the composition and structure of triglycerides.
Interesterification can be accomplished by heating lipids in high temperatures for a long
period. In the presence of catalyst, interesterification occurs at lower temperatures in a short
period (50C, 30min). Alkali metals and alkylated alkali metal are effective low-temperature
catalysts and sodium methoxide is the most common one. The dosage of catalyst is generally
about 0.1% of lipids.
R1
R2
R1
R1
R2
R3
R2
R3
R3
Figure 4-18. Intra-molecular interesterification.
R1
R1
R1
R2
R2
R2
R1
R2
R2
R1
R1
R2
R1
R2
R1
R2
R2
R1
Excessive catalyst leads to more lipid loss due to the formation of soap and methyl esters.
Impurities, such as free fatty acids and peroxides, can react with sodium methoxide and
these impurities must be present in low levels in interesterification. Besides, sodium
methoxide can react with water and lost the catalytic activity. Hence, interesterification
reactions can be terminated by adding water.
134
Lipids
135
REFERENCES
[1]
[2]
[3]
[4]
[5]
[6]
[7]
Hilditch, TP; Williams, PN. The Chemical Constitution of Natural Fats, 4th edition.
London: Chapman and Hall, 1964.
Kartha, ARS. The glyceride structure of natural fats. II. The rule of glyceride type
distribution of natural fats. Journal of the American Oil Chemists' Society, 1953, 30,
326329.
Fennema, OR. Food Chemistry. 3rd edition. New York: Marcel Dekker; 1996.
Chan, HW; Levett, G. Autoxidation of methyl linoleate: Analysis of methyl
hydroxylinoleate isomers by high performance liquid chromatography. Lipids, 1977,
12, 837-840.
Chan, HW; Levett, G. Autoxidation of methyl linoleate: Separation and analysis of
isomeric mixtures of methyl linoleate hydroperoxides and methyl hydroxylinoleates.
Lipids, 1977, 12: 99-104.
Frankel, EN. Autoxidation in Fatty Acids. Journal of the American Oil Chemists'
Society, 1979, 353-390.
Sreenivasan, B. Interesterification of fats. Journal of the American Oil Chemists'
Society, 1978, 796805.
ISBN: 978-1-61942-125-7
2012 Nova Science Publishers, Inc.
Chapter 5
PROTEINS
1
ABSTRACT
Protein is one of the most important components in foods. Most proteins are
constituted with 20 kinds of amino acids that are linked through peptide linkages. The
combination of these amino acids leads to the occurrence of substantial amount of
proteins with different structures and functions. Theoretically, all proteins produced by
organisms can be utilized by human body. However, only proteins that are readily
digestible, non-toxic and nutritious with specific functions are used in diets. This chapter
briefly describes the properties and structures of amino acid components and proteins and
highlights the properties of important dietary protein sources. Denaturation is an
important change in food processing. The mechanism of denaturation, properties of
denatured proteins and factors causing denaturation are also included in this chapter. In
addition to the nutrition attribute, some functional properties, including emulsifying,
foaming, gelling, and viscosity, also contribute to its wide applications in the food
industry. These functional properties are described in detail in this chapter. Proteins
undergo various changes during processing. These changes might greatly affect the
quality of foods. This chapter also emphasize on the changes of proteins occurred in
various processing techniques.
138
Proteins
139
The acylated products are more stable against various reagents and can be removed by
many methods. Hence, carbobenzoxy chloride has been widely used in protein synthesis for
amine group protection.
(2) Alkylation of amine group
Amino acids can react with 1-fluoro-2, 4-dinitrobenzene (FDNB) to yield N-2,4dinitrophenyl amino acids (DNP-amino acids), which are yellow compounds and crystallize
readily. This reaction is very important in N-terminal acid labeling for protein sequencing in
Sangers method.
The azide compound can react with another amino acid ester by condensation to produce
a dipeptide:
140
II
III
IV
V
Amino acids
Glu, Asp, Gln, Asn
Thr, Ser, Ala, Gly, Met,
Cys
Hpr, Pro
Taste
Sour
Sweet
Pyrrole
Alkaline
Proteins
141
(1) Neutral peptides consisting of type I and V amino acids and those containing only
type II amino acids exhibit light tastes.
(2) The sodium salts of oligopeptides consisting of only type I amino acids or type I and
type II amino acids taste fresh, such as Glu-Glu, Glu-Asp, Glu-Ser, and Glu-Thr.
(3) The combination of type III amino acids with type I amino acids remove the bitter
taste, but remain the sour taste.
(4) Peptides composed of type III, IV, or V amino acids only or their combinations are
bitter.
(5) Peptide formation, carboxyl group esterification, or diketopiperazine formation by
coupling of type IV and V amino acids enhances the bitter taste.
(6) Peptides with type IV and V amino acids locating at the C terminal are 3~5 times
bitterer than those with the amino acids locating at the N terminal or the middle of the
peptides.
(7) Type II amino acids (especially Gly) locating at either terminals or cyclized increase
the bitterness.
All peptides contain AH polar groups. However, because peptides differ markedly in
molecular weight and nature of hydrophobic groups, they have different bitterness receptor
binding capabilities. The bitterness intensity of peptides can be predicated by calculating the
average hydrophobicity of side chains, which is related to the total hydrophobicity of
nonpolar amino acids. Table 5-2 lists the hydrophobicity of various amino acids. The average
hydrophobicity of a peptide can be calculated by using the following formula:
In which, G is the free energy change of the side chains of amino acids and n is the
number of resides in the peptide.
Peptides with Q greater than 6.85kJ/mol are bitter and those with Q less than 5.43kJ/mol
are not bitter. No rules have been found for the taste of peptides with Q in the range
5.43~6.85kJ/mol. However, exceptions have been found. For example, all peptides with
molecular weight more than 6000 taste light despite of the Q value. If Gly is attached to one
or both ends of a peptide, the peptide tastes bitter even though Q is less than 5.43kJ/mol. This
is possible due to the less steric hindrance of Gly that facilitates the contact with bitterness
receptors. For this reason, it has been proposed to exclude Gly from Q calculation. Arg-Arg,
Lys-Ala, Val-Ah, Arg-Gly-Pro, and Ser-Lys-Gly-Leu, are also exceptions to the rule. The Q
values of these peptides are less than 5.43kJ/mol, but they taste bitter.
Besides, the bitterness intensity of peptides with similar Q values might differ
significantly. The bitterness intensity of Gly-Gly-Gly-Leu is greater than its three positional
isomers and that of Leu polymers are Leu-Leu-Leu-Leu, Leu-Leu-Leu, Leu-Leu, and Leu in
decreasing order. In the case of bitter peptides in cheese, the bitter taste disappears after the
Gln at the N terminal is cyclized, though the Q value is not changed. These inconsistencies
indicate that the bitterness intensity of peptides is also affected by their molecular weights and
higher structures in addition to Q values.
142
Amino acid
Ala
Arg
Asn
Asp
Cys
Gln
Glu
Gly
His
Ile
G0(side chain)/(kj/mol)
2.09
2.1
0
2.09
4.18
-0.42
2.09
0
2.09
12.54
Amino acid
Leu
Lys
Met
Phe
Pro
Ser
Thr
Trp
Tyr
Val
G0(side chain)/(kj/mol)
9.61
6.25
5.43
10.45
10.87
-1.25
1.67
14.21
9.61
6.27
MSG
Animal meat
Fish meat
Shrimp, crab
Shellfish
Octopus, squid
Kelp
Vegetable
Mushroom
Soy sauce
+
+
+
+++
++
+++
5-IMP
5-GMP
Sodium
succinate
+++
+++
++
+++
+++
+++
+++
Note: MSG, monosodium glutamate; 5-IMP, 5-inosine monophosphate; 5-GMP, 5-guanosine monophosphate.
Proteins
143
Many fruit acids, such as malic acid, tartaric acid, and citric acid, enhance the taste of
foods. The combination of anyone of the acids with lactic acid can improve the odor
of soybean product. Besides, citric acid juice enhances the taste of strawberry.
Fumaric acid and maleic acid can suppress the unpleasant odor of garlic.
Glutathione enhances the taste of meat broth. Polyphosphates improves the taste of
chicken meat and cheese.
The diamine salts of dicarboxylic acids with carbon atom number ranging from 3 to
10 can be used as the substitutes of table salt.
It is proposed that all flavor enhancers show a common structure O-(C)n-O, in which, n
ranges from 3 to 9. In another word, the compounds must contain an alkyl chain with 3~9
carbons and the two ends must be negative charged. Compounds with 4~6 carbons have the
highest enhancing ability. The alkyl chain can be straight, branched, or cyclic and the carbon
atoms can be replaced by O, N, S, and P. The negative charges on the two ends of the
molecule are crucial for the enhancing ability. If the carboxylic acid group is esterified,
amidated, or converted to lactone or lactam upon heating, the enhancing ability is obviously
reduced. The negative charge of an end can be replaced by a negative dipole. For example,
the enhancing abilities of tricholomic acid and ibotenic acid are 5~30 times higher than that
of L-MSG.
For economic and safety reasons, only Glu- and nucleotide-type flavor enhancers have
gained commercial applications.
(2) Glu-type flavor enhancers.
Flavor enhancers containing Glu are fatty compounds and have specific spatial
configuration for their functions. The negatively-charged groups at the two ends, such as
COOH, SO3H, and SH, determine the flavor enhancing capability and hydrophilic groups,
such as L-NH2OH, assist in the capability. Dipeptides or tripeptides with hydrophilic amino
acids attached to the carboxylic end of Glu have the flavor enhancing ability, but those with
hydrophobic amino acids attached are bitter, as shown in Table 5-4.
It is noteworthy that all the amino acids have more than one taste. Table 5-5 lists the
tastes of three amino acids.
The flavor enhancing capability of MSG is affected by the environmental pH. MSG has
the highest enhancing ability in pH6.0. Besides, temperature also affects the ability. When
MSG is heated for a long time or at 120C, inter-molecular dehydration occurs and
pyroglutamic acid (shown below) is generated. This product losses the flavor enhancing
ability and is toxic to human body.
144
Relatively ability
1.00
0.08
0.10
5~30
0.10
Delicious
Sweet
0
0.15
0.10
0.10
0.10
0.15
0.20
2.00
2.00
Bitter
0.1
1.8
0.1
0.1
Nearly 0
0.1
1.0
0.1
0
Delicious taste
21.5%
71.4%
1.2%
Sour
64.2%
3.4%
5.6%
Salty
2.2%
13.5%
0.6%
Sweet
0.8%
9.8%
1.4%
Bitter
5.0%
1.7%
87.6%
In addition, MSG is racemized under alkaline solutions when heated and loses flavor
enhancing ability. Hence, MSG should be added after dishes or soups are cooked.
(3) Nucleotide-type flavor enhancers.
Flavor enhancers of this type are aromatic heterocyclic compounds. The hydrophilic
ribose phosphate determines the flavor enhancing ability and e hydrophobic substituents
attached to the aromatic heterocycle assist in the ability.
Proteins
145
2. STRUCTURE OF PROTEIN
2.1. Primary Structure
Primary structure is the sequence of amino acid residues in proteins and is decided by
the genetic codes in genes. The primary structure decides the higher structures of proteins. All
proteins are composed of 20 amino acids and the combination of these components leads to
the occurrence of tremendous number of proteins with different spatial structures and
biological functions.
146
involved in -helix formation, because it cannot rotate or hydrogen bond with other amino
acids readily. The presence of glycine affects helix stability, because its side chain (H)
occupies the minimum space.
The -sheet structure is characterized by the following:
(1) The -sheet structure is an extended structure. Amino acid residues involved are
arranged in a zigzag pattern and their residues are located on the upside or downside of the
pleat plane. The angle between adjacent peptide bond planes is 110.
(2) The conformation is stabilized by hydrogen bonding of C=O and NH between
adjacent strands of a peptide.
(3) When adjacent strands run in the same direction, the peptide chains are parallel.
When the chains run in opposite directions, a planar, antiparallel sheet structure is stabilized.
Both parallel and antiparallel sheets can occur in one peptide.
(4) In parallel -sheet, the distance between any two adjacent residues is 0.65 nm and
that in anti-parallel -sheet is 0.7 nm.
Proteins
147
electrovalent bond;
hydrogen bond;
c
hydrophobic bond;
d
Vander Wasls force;
e
disulfide bond.
b
Figure 5-3 shows the combination pattern of the subunits of hemoglobin. The structures
of subunits in a protein may be the same or different. For example, the coat protein of tobacco
streak virus consists of 2200 identical subunits and normal hemoglobin A is a tetramer
containing two subunits and two subunits. The smallest subset of different subunits of a
protein is defined as the protomer. For example, the aspartate carbamyl transferase contains
six protomers and each protomer consists of one catalytic subunit and one regulatory subunit.
Some proteins can further aggregate into polymers and each repeating unit is called a
monomer. According to the number of monomers, protein polymers can be divided into
dimer, trimer, oligomer and multimer. For example, insulin might occur as dimer and
hexamer in human body.
148
3. CLASSIFICATION OF PROTEINS
3.1. Classification by Amino Acid Composition and Quantity
According to the composition of amino acids and their contents in proteins, proteins are
divided into complete, partially complete, and incomplete proteins.
Proteins
149
3.2.1. Albumin
Albumin refers to any protein that is soluble in water and moderately soluble in
concentrated salt concentrations. Albumin can be precipitated by saturated ammonium
sulphate. Albumin occurs widely in nature. Leucosin in wheat seeds, blood plasma proteinand
ovalbumin in eggs are examples of albumin.
3.2.2. Globulin
Globulins are insoluble in water but soluble in diluted salt, acid, or alkaline solutions and
can be precipitated by half-saturated ammonium sulphate. Globulins have important
biological functions. Legumin in soybean seeds, seroglobulin in blood, myoglobulin in
muscle, and immunoglobulins are of this category.
3.2.3. Histone
Histones are highly alkaline proteins and are soluble in water or diluted acid solutions.
Histones contain rich quantity of Arg and Lys and are the structural components of
chromosomes.
3.2.4. Protamine
Protamines are small, arginine-rich proteins and are soluble in water and diluted acid
solutions. Protamines contain abundant alkaline amino acids and lack Trp and Tyr. The
proteins are found in mature sperm cells and replace histones late in chromosome the haploid
phase of spermatogenesis.
3.2.5. Prolamin
Prolamins are a group of plant storage proteins with high proline contents and found in
the seeds of cereal grains. They are characterized by a high glutamine and proline content and
are generally soluble only in 70%~80% ethanol solutions.
150
3.2.6. Gluten
Glutens are contained in plant seeds, such as barley and rye. Proteins of this category are
insoluble in water or diluted salt solutions but soluble in diluted acid and alkaline solutions.
3.2.7. Albuminoid
Proteins of this category are not soluble in water or salt, diluted acid and diluted alkaline
solutions and occur mainly in skins, hairs, and nails. The roles of such proteins include
protection and support, forming connective tissue, tendons, bone matrices, and muscle fiber.
Keratin, collagen, elastin, and fibroin are all albuminoids.
Proteins
151
4. PROTEIN DENATURATION
4.1. Definition of Denaturation
When a protein is exposed to such physical stresses as heating and ultraviolet irradiation
or such chemical stresses as strong acid and base, its properties are changed, such as decrease
of solubility and loss of activity, but the primary structure remains unaltered. This process is
termed denaturation. Denaturation is an extremely important property of proteins and
markedly affects food processing.
152
Trypsin and hemoglobin also undergo reversible denaturation. After trypsin is denatured
by heating at 70~100C for a short time in an acidic solution, the enzyme loses its catalytic
activity. When the solution is cooled down in a proper rate, trypsin can recover all its
properties.
Haemoglobin can be denatured by low-concentration sodium salicylate. After sodium
salicylate is removed, the protein can restore to its natural conformation. However, the
denaturation of most proteins is irreversible. For example, egg protein is gelated when
cooking and this process is irreversible; soybean protein is irreversibly denatured in tofu
production.
The reversibility of protein denaturation is related to the denaturation agent species,
protein property and the degree of protein conformation destruction. Generally, in reversible
denaturation, the tertiary and quaternary structures of proteins are destroyed, but secondary
structures remain intact. In contrast, in the irreversible denaturation, the secondary, tertiary
and quaternary structures are all interrupted.
Proteins
153
protein purity and pH. The denaturation of most proteins can be detected in the temperature
range 45~50C and the process is accelerated when the temperature is elevated to 55C.
Denaturation occurring at lower temperatures involves only the disruption of non-covalent
bonds and proteins become unfolded. For example, natural serum albumin is of the oval shape
with the axial ratio of 3:1, while the axial ratio of denatured serum albumin increases to 5:5.
Such denaturation induced by short-time exposure to low temperatures is reversible. When
the temperature increases to 70~80C, disulfide bonds are broken. Hence, protein
denaturation occurring in long-time high-temperature treatment is irreversible.
Heat treatment leads to protein denaturation by disrupting hydrogen bonding and many
other secondary bonds that maintain protein conformation. It is estimated that the rate of
denaturation increases by up to 600 folds when the temperature increases by 10C in the
denaturation temperature range.
The sensitivity of a protein to thermal denaturation depends on multiple factors, such as
protein property, protein concentration, water activity, pH, ionic strength and ion species.
Proteins, enzymes, and microbes are more resistant to thermal denaturation in watercontaining conditions than in dry conditions. Besides, high concentration of denatured protein
hinders the renaturation process.
The temperature used in the thermal processing of foods is generally around 100C and
the central temperature of materials often exceeds 70C. Hence, most proteins are denatured
and pathogens are inactivated during thermal processing of foods.
4.4.2. Radiation
The impact of radiation on proteins depends on the energy and wavelength of the rays
used. Ultraviolet radiation can be absorbed by aromatic amino acid residues (tryptophan,
tyrosine and phenylalanine) and can change the conformation of proteins. Radiation by highenergy rays disrupts disulfide bonds. radiation and other ionizing radiation can also make
conformation changes, amino acid oxidization, covalent bond disruption, ionization, proteins
free radical formation as well as polymerization.
4.4.3. Denaturation at Interfaces
The denaturation of proteins attached to water-air, aqueous-nonaqueous solution, and
water-solid interfaces is generally irreversible. Proteins are surfactants and tend to migrate to
the interface and be adsorbed. The adsorption rate of proteins is controlled by diffusion rate of
natural proteins to the interface and the absorption stops when the interface is saturated by
denatured proteins (about 2mg/m2). Figure 5-5 indicates that the migration and absorption of
globular proteins in the aqueous-nonaqueous interface.
During the migration to interfaces, proteins interact with high-energy water molecules
(compared with the water molecules far away from the interface) at the interface. The
hydrogen bonding between protein molecules is then disrupted and the protein conformation
becomes slightly unfolded (Figure 5-5b). Because more hydrophobic groups are in contact
with water, the partially unfolded protein is hydrated and activated and transforms to an
unstable state. The protein further extends and unfolds at the interface and the hydrophobic
and hydrophilic residues are positioned in the water and non-aqueous phases respectively,
leading to protein denaturation at the interface. Proteins that are mainly stabilized by disulfide
bonds are not readily absorbed at the interface. Hence, these proteins are less susceptible to
denaturation at interface.
154
b)
c)
The interfacial properties of proteins are important for their applications in various food
systems. For example, proteins absorbed at interfaces are beneficial for the formation and
stabilization of emulsions and foams. To keep the natural conformation and functional
properties of proteins, dispersion systems, such as foams and emulsions, should be avoided
during food processing and separation.
4.4.4. pH
It is irreversible that protein denaturation occurs in mild and extreme pH conditions.
Extreme pH changes the ionization of some groups in polypeptide chains and disrupts the
hydrogen bonding required for maintaining conformation and the electrostatic interaction
between differently charged groups. If the pH is lowered far below the isoelectric point (pI) or
elevated above the pI, the protein will contain only positive or negative charges. The charges
will repel each other and prevent the protein from aggregation. In areas with large charge
density, the intramolecular repulsion may be great enough to cause unfolding of the protein.
In some cases the unfolding may be extensive enough to expose hydrophobic groups and
Proteins
155
156
This same reaction is used in reverse in cases of acute heavy metal poisoning. In such a
situation, a person may have swallowed a significant quantity of a heavy metal salt. As an
antidote, a protein such as milk or egg whites may be administered to precipitate the
poisonous salt. Then an emetic is given to induce vomiting so that the precipitated metal
protein is discharged from the body.
157
Proteins
a)
Peak 1
Peak 3
Peak 2
0.2 mw
0.1 MP2
Peak N
200 MP2
400 MP2
600 MP2
800 MP2
Rescan
50
55
60
65
70
75
80
85
Temperature (C)
b)
40
45
Figure 5-7. Thermograms of beef muscle, heated at 10 C min1 after treatment at different pressures in
air for 20min at 20C and 40C [7].
Although the combination of high pressure and thermal treatment has complex effect on
protein properties, it has wide applications in food processing:
Improving texture and tenderizing by causing protein unwinding and aggregation;
Extending shelf life by inactivating enzymes, microbes, and toxins activity;
Increasing digestibility;
Increasing the ability of maintaining flavors, pigments and vitamins by increasing the
surface hydrophobicity due to unwinding;
Improving product flavor and overall acceptability.
158
Food Systems
Beverage
Soup, sauce, salad dressing, dessert
Sausage, cake, bread
Meat, gell, bakery product, cheese
Conglutination
Elasticity
Meat, bread
Emulsification
Foamability
Fat and flavor binding
Proteins involved
Lactalbumin
Gelatin
Muscle protein, egg protein
Musscle protein, egg protein, milk
protein
Muscle protein, egg protein,
lactalbumin
Musscle protein, cereal protein,
milk protein
Muscle protein, egg protein,
lactalbumin
Egg protein, lactalbumin
Milk protein, egg protein, cereal
protein
The sensory properties of foods result from the complex interaction between various
food ingredients. For example, the flavor, texture, color and shape of a cake is contributed by
the combination of the thermal gelation capacity, foaming capacity, water holding capacity,
emulsification, elasticity and browning reaction of the materials used. Hence, proteins as food
materials must have multiple functional properties (Table 5-7). Animal proteins, such as those
derived from milk, egg and meat, are mixture of multiple protein components and thus have
diverse physical and chemical properties. For example, egg white has good water holding,
gelling, conglutination, emulsification, foaming, and thermal coagulation capabilities and
these properties are contributed by ovalbumin, conalbumin, ovomucin, lysozyme and other
albumins and their interactions. Plant proteins, such as those from soybean and oilseeds, are
also mixtures of multiple protein components.
However, these proteins have only limited functional properties and are only used in
common foods in less quantity.
Proteins
159
migrate to the air-water or oil-water interface and form highly viscoelastic film at the
interface. The interface system of proteins is more stable than that formed by surfactants.
Table 5-7. Functional properties of proteins required for various food [9]
Food
Beverage, soup, sauce
Formed bakery products
Dairy products
The substitute for egg
Meat products
Meat extender
Food film
Dessert
Functionality required
Solubility in solutions of different pH, thermal stability, viscosity,
emulsifying and water holding capacity
Casting and viscoelastic film forming, coherence, thermal denaturation,
gelation, swelling, emulsification, foaming, browning reaction
Emulsification, fat retention, viscosity, foaming, gelation, coagulation
Foaming, gelation
Emulsifying, gelation, coherence, absorption and retention of water and
fat
Absorption and maintain of water and fat, insolubility, hardness,
chewiness, coherence, thermal denaturation
Coherence, adhesion
Dispersity, emulsification
160
the interface occur in the train conformation, the segments suspended in the aqueous phase
are arranged as loops, while the peptide chains with the N- and C- terminal in the aqueous
phase are present mainly in the tail conformation. Of the three conformations, the train
conformation occurs in higher probability than the other two conformations and exhibits
lower interfacial intension.
)NTERFACE
-ODERATE PROBABILITY
OF ADSORPTION
.O ADSORPTION
(YDROPHILIC
SURFACE
3TRONG PROBABILITY
OF ADSORPTION
.ONPOLAR SURFACE
(YDROPHOBIC CORE
!QUEOUS PHASE
Figure 5-8. Probability of protein adsorption to the interface as a function of hydrophobic domain
number [11].
1IBTF
USBJO
*OUFSGBDF
UBJM
MPPQ
1IBTF
Figure 5-9. Configuration of flexibility polypeptide on interphase [12].
The stability of a protein at the interface determines the mechanical strength of the film
formed at the interface and the film strength is also affected by the electrostatic attraction, and
hydrogen bonding, and hydrophobic interaction between molecules. Disulfide bonds increase
the film viscoelasticity. When the concentration of protein in the interfacial film reaches
about 20%~25% (W/V), gelation occurs. To maintain the stability viscoelasticity of the gelled
film, the secondary interactions involved must be in balance. If the hydrophobic interaction is
too strong, the protein flocculates, aggregates, and even precipitates. If the electrostatic
repulsion far exceeds electrostatic attraction, a thick cohesive membrane is not formed
readily.
161
Proteins
Table 5-8. Emulsifying capability index (EAI) of some proteins [12]
EAI (m2/g)
pH6.5
pH8.0
197
149
166
153
119
142
Protein
BSA
Casein ache sodium
-lactoglobulin
Powder form lactalbumin
Protein
hemoglobin
Yeast protein
lysozyme
Ovalbumin
EAI (m2/g)
pH6.5
pH8.0
75
8
59
50
49
Note: The data were obtained when proteins are dispersed in 0.5% PBS buffer of ionic strength of 0.1.
The emulsifying capability of a protein can be evaluated by droplet size and distribution,
emulsifying activity, emulsion capacity, and emulsion stability.
Emulsifying activity refers to the total interfacial area of an emulsion. The emusifying
activity of a protein is often presented as the emulsifying activity index (EAI), namely the
interfacial area created per unit mass of protein. The EAI of a protein can be determined
easily in the turbidimetric method. The turbidity of an emulsion can be calculated by the
following equation:
Emulsion capacity (EC) is the volume (ml) of oil that can be emulsified by per gram of
protein before phase inversion (a change from oil-in-water emulsion to water-in-oil) occurs.
In the determination of TC, oil or melted fat are added at a constant rate and temperature to an
aqueous protein solution that is continuously agitated. Phase inversion is detected by an
abrupt change in viscosity or color (usually a dye is added to the oil).
EMULSIFYING ACTIVITY INDEX %!)-G
Figure 5-10. Effect of molecular weight on EAI (DH is the degree of hydrolysis) [13].
162
Note: - 0.1mol/L NaCl; 0.2 mol/L NaCl; 0.5mol/L NaCl; 1.0mol /L NaCl.
Figure5-11. Effect of pH and NaCl concentration on the emulsion volume of peanut protein isolate [14].
The emulsion stability (ES) is measured as the final volume of the emulsion after
centrifuging the initial volume or standing for several hours at specified conditions. It may
also be determined as the quantity of oil or cream separated from the emulsion, or the time
required for the emulsion to release a specified quantity of oil.
163
Proteins
In most cases, the disperse phase is air or carbon dioxide and the continuous phase is
composed of two films of proteins adsorbed on the interface between a pair of air bubbles,
with a thin layer of liquid between them. The diameters of bubbles might range from 1m to
several centimeters, depending on the surface tension and viscosity of the aqueous phase and
energy input. Evenly distributed small bubbles can impart foods with desired consistency,
exquisite texture, and softness and improve the dispersivity and flavor. The formation of
bubbles is shown in Figure 5-12.
&
%
$
"
GAS LATEX
LIQUID
BUBBLE
Protein type
-Lactoglobulin
Foaming power at
0.5% protein
concentration (W/V)
480
600
Fibrinogen
360
40
500
240
760
The pH is an important factor that affects the foaming ability and foam stability of
proteins. Generally, high solubility is a prerequisite for good foaming ability and foam
stability. However, insoluble protein granules, such as fibrillin in its isoelectric point, may
164
impart good foam stability. Some proteins give rise to small to foam volume in their
isoelectric points, but the produced foams have excellent stability, such as globulins in pH
5~5, glutelin in pH 6.5~7.5, and lactalbumin in pH 4~5. Some protein-stabilized foams are
more stable in extreme pH values, possible due to increased viscosity of involved proteins.
The foams in most foods are formed in other pH than the isoelectric points of contained
proteins.
Sugars suppress the expansion of protein-stabilized foams, but increase the foam
stability. This is because sugars can increase the viscosity of the bulk phase and reduce the
drainage of the lamella fluid. Sugars can stabilize the conformation of proteins and hinder
their adsorption and unfolding on the interface. Hence, proteins cannot produce large
interfacial area and foam volume in the presence of sugars. This is why sugars are often
added after the foam expansion has already been completed in the manufacture of meringue
and other sugar-containing foods.
Lipids in low concentrations (about 0.1%) seriously impair the foam ability of proteins.
This is because lipids are more surface-active than proteins. Lipids readily adsorb at the airwater interface and inhibit adsorption of proteins during foam formation. Besides, lipid films
lack the cohesive and viscoelastic properties necessary to withstand the internal pressure of
the foam bubbles, the bubbles rapidly expand, then collapse during whipping. Thus, lipid-free
whey protein concentrates and isolates, soy proteins, and egg proteins without egg yolk
display better foaming properties than do lipid-contaminated preparations.
Partially denatured proteins have improved foaming abilities than their nature forms.
Moderate heat treatment can enhance the foaming ability of soybean protein (70~80C) and
lactalbumin (40~60C). Although moderate heat treatment increases the expansion capacity,
it decreases the foam stabilization. Excessive heat treatment might impair the foaming ability
of proteins.
To obtain enough quantity of foam, the whipping operation must last long enough in
suitable strength for sufficient unfolding and adsorption. However, excessive whipping can
reduce the expansion volume and foam stability. For example, ovalbumin is very sensitive to
excessive whipping. Whipping of ovalbumin for 6~8min can lead to coagulation-flocculation
in the air-water interface. These insoluble proteins could not be completely absorbed on the
interface and the viscosity of the formed liquid sheet cannot meet the requirement of high
stability of foams.
Most proteins contain more than one subunit. Hence, the foaming ability of a protein is
also affected by the interaction between the subunits absorbed on the interface. For example,
the excellent foaming ability of egg whit has been attributed to its protein composition.
Acidic proteins can get improved foaming ability when complexing with an alkaline protein.
No close correlation between emulsifying ability and foaming ability has been found for
protein.
Salts affect the foaming of proteins by influencing the solubility, viscosity, unfolding
and aggregation of proteins. The foaming ability and foam stability of most globular proteins,
such as bovine serum albumin, egg albumin, gluten and soy proteins increase with increasing
concentration of NaCl. This behavior is usually attributed to neutralization of charges by salt
ions. However, some proteins, such as whey proteins, exhibit the opposite effect: Both foam
ability and foam stability decrease with increasing concentration of NaCl (Table 5-10).
Bivalent cation ions, such as Ca2+ and Mg2+, in concentration 0.02~0.04mol/L could bridge
Proteins
165
with the carboxyl group of proteins to form protein films with good viscoelasticity. Hence,
the presence of these ions can increase the foam stability.
5.2. Viscoelasticity
Viscoelasticity is the property of materials that exhibit both viscous and elastic
characteristics when undergoing deformation.
Table 5-10. Effect of NaCl on the foaming ability and foam stability of whey protein
isolate [17]
Concentration of
NaCl(mol/L)
0.00
0.02
0.04
0.06
0.08
0.10
0.15
Wheat protein is very unique among food proteins because it can produce dough with
both viscous and elastic properties. When a mixture of wheat flour and water (about 3:1 ratio)
is kneaded, a dough with viscoelastic properties forms that is suitable for making bread and
other bakery products.
These unusual dough characteristics are mainly attributable to the proteins in wheat flour.
Wheat flour contains 20% soluble and 80% insoluble protein fractions. The soluble proteins
are primarily albumin, globulin-type enzymes and minor glycoproteins. These proteins do not
contribute to the dough-forming properties of wheat flour. The major storage protein of wheat
is gluten. Gluten is a heterogeneous mixture of proteins, mainly gliadins (soluble in
70%~90% ethanol) and glutenins (insoluble in water or ethanol, but soluble in acidic and
alkaline solutions). Gluten can entrap gas during fermentation to produce the viscoelastic
property. Besides, the starch granules, pentosan, polar and non-polar lipids, and soluble
proteins in wheat flour facilitate the formation of the viscoelastic protein network and dough
texture. Gluten is rich in Gln (more than 33% of the amino acid residues) and hydroxylcontaining amino acids. Hence, the amino acids can form hydrogen bonding readily and this
property contributes to the water adsorption and cohesion-adhesion property of gluten. About
30% of gluten's amino acid residues are hydrophobic, and the residues contribute greatly to its
ability to form protein aggregates by hydrophobic interactions and to bind lipids and other
nonpolar substances.
Cysteine and cystine residues account for 2~3% of gluten's total amino acid residues.
During formation of the dough, these residues undergo sulfhydryl-disulfide interchange
reactions resulting in extensive polymerization of gluten proteins.
Several physical and chemical transformations occur during mixing and kneading of a
mixture of wheat flour and water. Under the applied shear and tensile forces, gluten proteins
absorb water and partially unfold. The partial unfolding of protein molecules facilitates
hydrophobic interactions and sulfhydryl-disulfide interchange reactions, which result in
166
formation of thread-like polymers. These linear polymers in turn are believed to interact with
each other, presumably via hydrogen bonding, hydrophobic associations, and disulfide crosslinking, to form a sheet-like film capable of entrapping gas.
Because of these transformations in gluten, the resistance of the dough increases with
time until a maximum is reached, and this is followed by a decrease in resistance, indicative
of a breakdown in the network structure. The breakdown involves alignment of polymers in
the direction of shear and some scission of disulfide cross-links, which reduces the polymer
size. The time it takes to reach maximum dough strength during kneading is used as a
measure of wheat quality for bread makinga longer time indicating better quality.
The development of the viscoelastic dough is thought to be related to the extent of
sulfhydryl-disulfide interchange reactions. This is supported by the fact that when reductants,
such as cysteine, or sulfhydryl blocking agents, such as N-ethylmaleimide are added to
dough, viscoelasticity decreases greatly. On the other hand, addition of oxidizing agents, such
as iodate and bromate, increase the elasticity of the dough. This implies that wheat varieties
that are rich in SH and S-S groups might possess superior bread-making qualities, but this
relationship is unreliable. Thus, the role of sulfhydryl-disulfide interchange reactions in the
development of viscoelastic dough is poorly understood.
The strength of dough is related to the contents of glutenin and completely insoluble
residue proteins. Experiments on wheat flour supplemented with glutenins and gliadins of
different proportions indicate that glutenins determine the elasticity, cohesiveness, mixture
tolerance, extensibility, the expansion of dough and the mobility of gliadins. Suitable
proportions of the two categories of proteins are important for bread making.
High glutenins contents can increase the cohesiveness of dough and suppress the
expansion of entrapped CO2, while high gliadins contents increase the elongation and make
the gluten film fragile and permeable, leading to poor CO2 retention and bread collapse.
The different effects of glutenins and gliadins on bread-making may be related to the
differences in their structure and composition. In gluten these exist as single polypeptides
with molecular weight ranging from 30,000 to 80,000. Although gliadins contain about 2~3%
half-cystine residues, they apparently do not undergo extensive polymerization via
sulfhydryl-disulfide interchange reactions. The disulfide bonds appear to remain as
intramolecular disulfides during dough making. Dough made from isolated gliadins and
starch is viscous but not viscoelastic.
Glutenins are heterogeneous polypeptides with molecular weight ranging from 12,000 to
130,000. These are further classified into high-molecular-weight (M.W. >90,000, HMW) and
low-molecular-weight (M.W. <90,000, LMW) glutenins. In gluten, glutenin polypeptides are
present as polymers joined by disulfide cross-links, with molecular weights ranging into the
millions. Because of their ability to polymerize extensively via sulfhydryl-disulfide
interchange reactions, glutenins contribute greatly to the elasticity of dough. Therefore, an
optimum ratio of gliadins and glutenins seems to be necessary to form viscoelastic dough.
Some studies have shown a significant positive correlation between HMW glutenin content
and bread quality in some wheat varieties, but not in others. Available information indicates
that a specific pattern of disulfide crosslink association among LMW and HMW glutenins in
gluten structure may be far more important to bread quality than the amount of this protein.
For example, association/polymerization among LMW glutenins which have the similar
structure form the HMW gliadin. This type of structure contributes to viscosity of the dough,
but not to elasticity. In contrast, if LMW glutenins link to HMW glutenins via disulfide cross-
Proteins
167
links (in gluten), then this is believed to contribute to dough elasticity. It is possible that in
good-quality wheat varieties, more of the LMW glutenins may polymerize with HMW,
whereas in poor-quality wheat varieties, most of the LMW glutenins may polymerize among
themselves. These differences in associated states of glutenins in gluten of various wheat
varieties may be related to differences in their conformational properties, such as surface
hydrophobicity, and reactivity of sulfhydryl and disulfide groups.
Baking does not lead to the re-denaturation of gluten, because glutenins and gliadins
occur naturally in partially unfolded form and are further unfolded during kneading. When
heated in 70~80C, gluten loses water and the water is absorbed by gelatinized starch
granules. Hence, gluten can maintain the softness and water content (40%~50%) of bread in
baking.
Soluble protein fractions, including albumin- and globulin-type proteins, are denatured
and coagulated during baking. This partial gelling is beneficial for the cohesion of crumbs.
Hence, supplementation of external proteins is good for bakery foods quality, such as
nutrition fortification. However, not all proteins are beneficial for gluten network formation.
For example, supplementation of wheat flour with albumin- and globulin-type proteins, such
as whey proteins and soy proteins, adversely affects the viscoelastic properties and baking
quality of the dough. These proteins decrease bread volume by interfering with formation of
the gluten network. Addition of phospholipids or other surfactants to dough counters the
adverse effects of foreign proteins on loaf volume. In this case, the surfactant/protein film
compensates for the impaired gluten film. Although this approach results in acceptable loaf
volume, the textural and sensory qualities of the bread are less desirable than normal.
5.3. Gelation
Gelation is the process of aggregation and ordered network formation of denatured
proteins. The gelation of proteins is very important for some foods, including various dietary
products, jelly, gelatin gel, soybean protein gel, and textured vegetable proteins. Tofu, which
is a favorite food in China, is a typical food prepared by protein gelation.
Heating is necessary for the formation of most protein gels. The addition of salts,
especially those containing Ca2+, improves the gelation rate and gel strength. Proteins can
also interact with polysaccharides to form gels. For example, the positively-charged gelatin
can bind to negatively-charged sodium alginate through nonspecific ionic interaction to form
gel with a high melting point (80C).
Many protein gels are highly hydrated and each gram of protein can hold up to more
than 10 grams of water. Many food components can be trapped in the network of protein gels.
The water contents of some protein gels might reach up to 98%. Although the trapped water
has properties similar to the water in dilute solutions, the water cannot be squeezed out easily.
5.4. Hydration
The conformation of each protein in a solution is affected by their interactions with
water. The interaction between proteins and water also occurs in solid foods. In addition, dry
concentrated proteins or protein isolates must be hydrated before use. Hence, the hydration
168
and rehydration properties of proteins markedly affect their applications in the food industry.
Figure 5-13 illustrates the sequence of interactions occurred between dry protein and water.
Dry
protein
Multilayer
water is formed
Liquid water
condenses
Solution
is formed
Protein starts
swelling
Protein
disperses in
water
Figure 5-13. Sequence of the interactions between dry protein and water [10].
5.5. Solubility
It is a long process for proteins to reach their equilibrium solubility and the protein
solubility varies with the pH, ionic strength, and temperature of the environment and protein
concentration. The solubility of most proteins decreases irreversibly when heated. However,
heat treatment is unavoidable during food processing and protein denaturation might occur
during extraction and purification even in mild conditions. Hence, the nitrogen solubility
index (NSI) of soybean protein powder, concentrated soybean protein, and soybean protein
isolate vary in the range 10%~90%.
Proteins
169
The solubility of proteins is essential for determining the optimum conditions of protein
extraction, purification and separation and is an important indicator of its application range.
The degree of insolubility can be used as a measure to evaluate the denaturation and
agglutination of proteins. It is reported that proteins with greater initial solubility can disperse
quickly and yield well dispersed hydrocolloid system with macrostructure and smooth
texture. In addition, high initial solubility facilitates the diffusion between of proteins to the
gas/water and oil/water interface for enhanced their surface activity.
5.4. Viscosity
The viscosity or consistency of a liquid reflects its resistance to flow under an applied
force or shear stress and can be represented in viscosity coefficient , which is defined as the
ratio of shear stress to shear rate (or flow rate). The viscosity of protein fluids is largely
related to the apparent diameter of dispersed protein molecules or protein particles. The
apparent diameter of proteins is decided by the following parameters: (1) the inherent nature
of protein molecules, such as molar concentration, molecular size, molecular volume,
molecular structure and charge; (2) protein-solvent interaction, which affects the swelling and
solubility of proteins and the hydrokinetics of the fluid surrounding protein molecules; (3)
protein-protein interaction. The interaction determines the size of protein aggregates and the
interaction opportunity increases in high protein concentrations.
The viscosity coefficient of protein-containing solutions, such as homogenates,
emulsions, pastes and gels, might decrease with the increase of shearing stress. This behavior
is known as shear thinning. During shearing, protein molecules are redirected to the flow
direction and the friction drag is reduced as a result. Besides, the break of hydrogen bonds
and other weak bonds can cause the dissociation of protein aggregates and network. The
break of weak bonds is a slow process so that the shear stress and apparent viscosity
decreases with the proceeding of shearing before the protein fluid reaches steady flow. When
the shearing force is no longer applied, the original aggregates or network can or cannot be
reformed. If the aggregates or networks can be completely or partially reformed, the change
of viscosity coefficient is irreversible.
The viscosity or consistency of protein system is an important property for liquid and
semisolid-type foods such as beverages, broth, sauces and cream. The fluid property of
protein dispersion systems is of practical significance in determining the optimum operation
conditions. For example, during transfer, blending, heating, cooling, and spray drying, the
fluidity of protein dispersion systems significantly affects the transfer of both mass and heat.
170
categories differ markedly in their solubility. Sarcoplasmic proteins can be extracted by water
or buffers with low ionic strength (0.15mol/L or lower), myofibrillar protein can be extracted
only in high salt concentrations, and matrix proteins are insoluble. Sarcoplasmic proteins
contain large amounts of glycolytic enzymes and many other enzymes in addition to
myoglobin and haemoglobin, which affect the color of meat.
Myofibrillar proteins account for about half of animal skeletal muscle proteins. These
proteins are intensively charged hydrated and are insoluble under physiological conditions.
Matrix proteins participate in the formation of connective tissues. Collagen, reticulum
and elastin are examples of matrix proteins. Collagen is fibrous and occurs in all muscle
tissues. Reticulin refers to a type of fiber in connective tissues composed of type III collagen.
The proteins crosslink and form a fine mesh network. This network acts as a supporting mesh
in soft tissues such as liver, bone marrow, and the tissues and organs of the lymphatic system.
Elastic fiber is composed of the protein fibrillin and elastin made of simple amino acids such
as glycine, valine, alanine, and proline. Elastin helps skin to return to its original position
when it is poked or pinched. Elastin is also an important load-bearing tissue in the bodies of
vertebrates and used in places where mechanical energy is required to be stored. These matrix
proteins are less water soluble than sarcoplasmic and myofibrillar proteins.
6.2. Casein
Milk contains multiple types of proteins and the proteins exhibit different properties
(Table 5-11). In skimmed milk, casein accounts for about 80% of total protein. Casein is a
mixture of phospho-contaning proteins and precipitate out from skimmed milk at pH4.6 and
20C. Casein is extremely hydrophobic and occurs as micelles in milk. Casein is composed of
s1-casein, casein, -casein, s2-casein and -casein. The diameters of casein micelles range
from 50nm to 300nm with molecular weight range of 107~31010 Daltons. Casein micelles
are aggregated by sub-micelles, which has a diameter range from 10 to 20nm and molecular
weight range from 3105 to 6105.
Sub-micelles consist of s1-casein, -casein, s2-casein and -casein and the fractions
aggregate through hydrophobic interaction. The core of sub-micelles is hydrophobic in
contrast to the hydrophilic surface. The carbohydrate-rich -casein is restricted on a region of
the surface through self-association. Therefore, the surface of sub-micelles contains one
carbohydrate-rich regions and one phosphate-rich region that is formed by other caseins.
Casein micelles are the aggregation of sub-micelles. The electrostatic interaction
contributed by colloidal calcium phosphate facilitates the aggregation of sub-micelles. The
aggregation occurs between the negatively charged serine residue on casein and the
positively-charged colloidal calcium phosphate, which occurs in Ca9 (PO4)6 clusters. Because
-casein contains no phosphate groups, the electrostatic interaction occurs only between casein and -casein.
During casein micelle formation, sub-micelles with low content of -casein or without casein are located in the interior of casein micelle. When the surface of the micelle is
completely covered by -casein, the micelles stop growing up.
171
Proteins
12~15
3~4
9~11
2~4
22068~23724
25230
23944~24092
19007~19039
2~4
0.6~1.7
0.4
18205~18363
14147~14175
66267
0.3~0.6
0.05~0.1
0.05~0.15
0.05~0.1
0.02~0.1
153000~163000
146000~154000
385000~417000
1000000
79000
172
The compact spherical structure of gliadin is related to the intramolecular disulfide bond.
Glutenins associate with each other through inter-molecuar disulfide bonding. Hence,
glutenins are found as large and stretched associated molecules. Glutenin is insoluble due to
intermolecular disulfide bonds, but treatment with reducing agents increases its solubility.
The formation of gluten is the result of both covalent and non-covalent interactions of
multiple protein constituents. Glutenins contribute to the formation of the network structure,
while gliadin and other proteins are trapped within the structure. Wheat flour contains 12%
protein, 70% starch and 2% fat. During kneading, these components are incorporated into the
gluten network structure and a starch-protein-fat composite matrix is formed.
The reduction of disulfide bonds during kneading the re-oxidation of sulfhydryl during
dough storage occur mainly in cross-linked glutenin. The reduction of disulfide bonds
facilitates the gluten relaxing and enhances the non-covalent interactions between fat, starch
and other additives, leading to the formation of a continuous starch-protein-fat complex.
Proteins
173
174
The development of single cell protein resources has bright prospect. However, the high
content of nucleic acid in most single-cell proteins restricts their direct consumption by
consumers. Heat and alkaline treatment can improve the digestibility and amino acid
availability of single cell protein and reduce nucleic acids contents. Long-term toxicological
study indicates that heat- or alkaline-treated single cell protein is nontoxic.
Table 5-12. Essential amino acid contents and nutritive values of proteins derived from several foods
(mg/g protein) [18, 19]
Item
His
Ile
Leu
Lys
Met+Cys
Phe+Tyr
Thr
Trp
Val
Total
Protein content (%)
Chemical score /% (by
FAO/WHO pattern)
PER
BV(on rat)
NPU
Egg
Milk
Beef
Fish
Wheat
Rice
Corn
Source
Barley
22
54
86
70
57
93
47
17
66
512
12
100
27
47
95
78
33
102
44
14
64
504
3.5
100
34
48
81
89
40
80
46
12
50
480
18
100
35
48
77
91
40
76
46
11
61
485
19
100
21
34
69
23(1)
36
77
28
10
38
336
12
40
21
40
77
34(1)
49
94
34
11
54
414
7.5
59
27
34
127
25(1)
41
85
32(2)
6(2)
45
422
/
43
3.9
94
94
3.1
84
82
3.0
74
67
3.5
76
79
1.5
65
40
2.0
73
70
/
/
/
Soybean
Broad bean
Pea
Peanut
Kidney
bean
20
35
67
32(1)
37
79
29(2)
11
46
356
/
55
30
51
82
68
33
95
41
14
52
466
40
100
26
41
71
63
22(2)
69
33
8(1)
46
379
32
73
26
41
70
71
24(2)
76
36
9(1)
41
394
28
82
27
40
74
39(1)
32
100
29(2)
11
48
400
30
67
30
45
78
65
26
83
40
11
52
430
30
/
/
/
/
2.3
73
61
/
/
/
2.65
/
/
/
/
/
/
/
/
Note: Chemical score is defined as the proportion of the content of a limiting amino acid in the material to that of the reference protein.
176
Amino
acid
His
Ile
Leu
Lys
Met+Cys
Recommended pattern
Infant
Preschool
(2~5)
children
26
19
46
28
93
44
66
44
42
22
Amino acid
Adults
16
13
19
16
17
Phe+Tyr
Thr
Try
Val
Total
Recommended pattern
Infant
Preschool
(2~5)
children
72
22
43
28
17
9
55
25
460
241
adults
19
9
5
13
127
The proteins derived from major cereals and beans are deficient in at least one essential
amino acid. For example, the proteins of rice, wheat, barley and oat, are deficient in Lys but
rich in Met and this is reversed for the proteins of beans and seeds of oil crops. The proteins
of some seed plant seeds, such as peanuts, are deficient in both Met and Lys. Essential amino
acids with contents lower than that in reference protein are defined as limiting amino acids.
Adults that intake proteins only from crops and beans cannot maintain health and children
that intake only one of the two kinds of protein mentioned above cannot grow in the normal
rate. Table 5-12 lists the contents of essential amino acid in some proteins.
Generally, the proteins derived from plants and animals contain enough His, Ile, Leu,
Phe, Trp and Val and these amino acids are often not limiting amino acids in common foods.
However, Lys, Thr, Trp and sulfur-containing amino acid are often present in insufficient
quantity and are regarded as limiting amino acids.
Mixing a protein that deficient in an essential amino acid with another protein that is rich
in the essential amino acid can increase the nutrition value of the protein. For example, the
mixture of cereal protein and bean protein can provide complete and balanced essential amino
acids. The nutritive value of proteins can be improved also by supplementing the
corresponding limiting amino acids. For instance, supplementation of Met and Lys improves
the nutritive value of cereal and bean proteins.
If the protein or protein mixture contains all the essential amino acids and the contents
and proportions of the amino acids can maintain the optimum growth rate and health
conditions for consumers, the protein or protein mixture is though to have an ideal nutritive
quality. Table 5-13 lists the ideal amino acid distribution patterns for adults and children.
7.2. Digestibility
Protein digestibility is defined as the proportion of absorbed nitrogen to ingested
nitrogen. The contents of essential amino acids in proteins are important indicators of protein
quality. However, the utilization of these amino acids determines the real quality of proteins.
Table 5-14 lists the digestibility of various foods proteins in human body. It could be seen
that plant proteins have higher digestibility than animal proteins.
The digestibility of proteins is affected by the following factors:
(1) Structure: The structure of proteins markedly affects their hydrolysis by enzymes.
Generally, native proteins are more resistant to enzymatic hydrolysis than their denatured
forms and the hydrolysis of insoluble fibrous proteins is more difficult than that of thoroughly
denatured globular proteins.
177
Proteins
Table 5-14. Digestibility of some food proteins in human body [19]
Protein source
Egg
Milk, cheese
Meat, fish
Corn
Refined rice
Whole wheat
Refined flour
Gluten
Oat
Digestibility (%)
97
95
94
85
88
86
96
99
86
Protein source
Pea
Peanut
Soybean meal
Soybean protein isolate
Kidney bean
Corn products
Wheat products
Rice products
Wheat
Digestibility (%)
88
94
86
95
78
70
77
75
79
(2) Antinutrients: Most vegetable proteins isolated and protein concentrates contain
trypsin inhibitors, chymotrypsin inhibitor, and exogenous lectins. The inhibitors prevent the
complete hydrolysis of proteins derived from legumes and oil seeds by trypsin. Lectins hinder
the absorption of amino acids in intestines. Heat treatment can destroy these antinutrients and
make proteins more susceptible to digestion. In addition to the antinutrients mentioned above,
proteins derived from plants also contain phytic acid, tannin and other anti-nutrients.
(3) Association with other components: Association with polysaccharides and dietary
fiber reduces the hydrolysis speed and thoroughness of proteins.
(4) Processing: Heat and alkaline treatment can cause chemical reactions in proteins,
such as Lys residue generation. These changes reduce the digestibility of proteins. Besides,
Millard reactions might occur between reducing sugars and proteins. These reactions reduce
the digestibility of Lys residues.
178
8.1.1. Boiling
Boiling is a common processing method in the food industry. Boiling does not reduce
the quantity of proteins or essential amino acids of fish and meat. Boiling of milk neither
affects the amino acid content nor reduces the bioavailability. The egg white and yolk have
different sensitivity of heat treatment. The digestibility of raw egg white is only 50%, but raw
yolk can be digested and absorbed completely. Moderate cooking of eggs can yield of nearly
100% of digestibility and biological value due to heat denaturation of proteins. Moist heat
treatment is desired for most vegetable proteins, especially for proteins derived from beans.
Moist heat treatment increases the nutritive value of bean proteins due to protein denaturation,
inactivation of protease inhibitors and toxic substances, and disrupt of tissues and starch
granules.
Enzymes, such as lipase, lipoxygenase, protease, and polyphenol oxidase, can be
inactivated during blanching or steaming. Enzyme inactivation can prevent the formation of
undesired colors and flavors and the loss of vitamins. Heat treatment of rape seeds inactivates
myrosinase and avoids the formation the goitrogenic 5-vinyl-2-sulfur-oxazolidinone.
8.1.2. Pasteurization
It is generally believed that either the tank pasteurization method or the high-temperature
short time pasteurization has only slight effects on milk proteins, though whey proteins are
partially denatured. Extensive studies on infants, school-age children, adults and experimental
animals indicate that the nutritional value of milk is not affected by pasteurization.
Sealed container must be heated thoroughly until the contents are sterile. The required
intensity of heat treatment depends largely on the physical state of the contents. In
Proteins
179
pasteurization, the heat transferred from the vessel wall to the center in semi-solid foods is
much less than in foods containing liquids as the heat transfer medium. High-frequency
oscillatory electron heating and aseptic canning can overcome these problems, but their
applications are still very limited.
Pasteurization reduces the biological value of liquid milk by 6%, lysine content by 10%
and cystine content by 13%. The decrease in biological value may be due to the loss of
cystine. Pasteurization has much more significant effects on concentrated milk. Hence,
pasteurization can significantly reduce the bioavailability of proteins with limited lysine
contents.
180
Proteins
181
182
of the glycosidic linkage yields reducing groups, which undergo typical Maillard reaction
with another molecule of lysine. It has been reported that sucrose at relatively high levels in
oil seeds may be largely responsible for the damage to protein quality observed when they are
severely processed [22].
(2) Protein-lipoid interactions
The reactions between oxidized lipids and proteins have been extensively reported.
However, no general conclusions can be drawn on the reactions, because lipids are oxidized
in multiple modes. During oxidation, unsaturated fatty acids firstly bind to catalysts to
produce free radicals. Free radicals then react with oxygen to form hydrogen peroxides,
which can undergo reactions in a variety of ways. Some of the products are carbonyl
compounds that can participate in Maillard reactions. These products are subject to either
degradation or polymerization.
When oxidized lipids and proteins are incubated, cross-linking occurs between lipid free
radicals and proteins, which reduces the protein solubility, increases the resistance to
digestive enzymes, and destroy most amino acids. Then, sulfur-containing amino acids are
oxidized by hydroperoxides and methionine is converted to methionine sulfoxide. Free
methionine sulfoxide as a methionine source is the same as methionine. However, methionine
sulfoxide in peptides or proteins is less bioavailable than methionine, because it is resistant to
enzymatic hydrolysis. Cystine is quickly degraded and cysteic acid is one of the degradation
products. Cysteic acid is not a source of cystine for human body.
The newly formed active carbonyl compounds can react with the amino group of Lys
resides in a way similar to browning reactions. These reactions make Lys physiologically
unavailable.
In electrostatic fields, oxidized lipids can react with amino group-free proteins to yield
simple compounds. In this case, the nutritive loss of proteins is very small.
(3) Protein-aldehyde interactions.
In addition to the interactions between carbonyl and amino groups mentioned above, two
special reactions of proteins with aldehydes have also been identified during food processing.
One is the reaction with gossypol during cottonseed processing. The other is the reaction with
formaldehyde during meat fumigation. Both the two reactions decrease the bioavailability of
lysine.
Proteins
183
significantly affect the functional properties of proteins. The degree and result
(conformational change and aggregation) of thermal denaturation depend largely on the
nature of proteins and environmental conditions. Mammalian collagens start to unfold,
dissociate, and dissolve when heated to 65C in the presence of large quantity of water. In
contrast, actins undergo contraction, aggregation and water holding capacity reduction under
same conditions.
Caseinate monomers are very resistant to heat treatment. Vigorous heat treatment dose
not affect the properties of caseinate. Mild heat treatment dose not lead to the destruction or
generation of covalent bonds or serious changes of higher structures in proteins. Hence, from
the nutritional point of view, the changes induced by mild heat treatment are beneficial.
Heat treatment can eliminate the toxic effects of lectins in legumes, because the lectin is
a thermal unstable protein which can bind polysaccharides. It can reduce the nutritional value
of natural plant proteins in the diet. The presence of lectins can form compounds by
combining intestinal brush border membrane polysaccharide, which can diminish the abilities
of shifting and digestion in amino acid, produce toxicity to human and animal; heat treatment
can eliminate their harmful effects.
Protease inhibitors in foods, including trypsin inhibitors and chymotrypsin inhibitors, are
inactivated during heat treatment. High temperature treatments, such as high-pressure
sterilization, puffing, sterilization, cooking and baking, can destroy all antinutrients factors
(Figure 5-14). Therefore, moderate heat treatment can markedly improve the nutritional value
of vegetable proteins.
Many proteins, such as soybean globulin, collagen and egg albumin, are more digestible
after moderate heat treatment.
Figure 5-14. Effect of steaming on trypsin inhibitor activity and protein efficiency ratio of soybean
meal feed [20]
After heat treatment, the proteins are more susceptible to enzymatic hydrolyze due to
unfolding and amino acid residues exposure. Besides, heat treatment can remove off-odor
compounds in soybean protein and avoid the undesired flavor caused by lipid oxidase.
8.3.2. Dehydration
When the water in a protein solution is removed, aggregation occurs to the proteins. This
is the case especially when water is removed by evaporation at high temperatures, because the
184
solubility and surface activity decline sharply. Hence, the effects of drying on the functional
properties of protein should not be ignored. Drying changes the size and internal and surface
porosity of particles and consequently alters the wettability, absorption, diapersion and
dissolution of food proteins. When water is quickly removed as steam, particles shrink in the
minimum level and salts and carbohydrates migrate to the dried surface, yielding porous
powder particles. This change can be observed in freeze-drying and spray-drying.
Introduction of bubbles to protein solution before drying or the implementation of controlled
aggregation during drying can be applied to increase the porosity of particles.
8.3.3. Irradiation
Irritation causes inter- and intra-molecular cross-linking of proteins or peptide bond
breakdown in foods with low moisture content. In the presence of catalase, Tyr is oxidized
and condensed to dityrosine.
8.3.4. Oxidation
Oxidants are important additives in the food industry. For example, hydrogen peroxide is
sterilization and bleaching agent which can be used as a low-temperature fungicide in
package. It can also been used to improve the color of fish protein concentrates, flours and oil
seed protein isolates. Benzoyl peroxide can oxidize cysteine in flour to cystine so as to
enhance gluten strength and bleach flour. In some cases, benzoyl peroxide can also be used in
whey powder bleaching. Peroxides are also found in foods without artificially added oxidants
and these peroxides are often the reason for the degradation of proteins present in the foods.
Light oxidation, irradiation, trace metals, oxygen, hot air drying and aeration during
fermentation can all induce oxidative denaturation of amino acids in proteins.
Trp is the most sensitive amino acids to oxidation, followed by tyrosine and histidine in
sequence. The oxidation of sulfur-containing amino acids occurs mainly in the sulfurcontaining side chains and that of aromatic-containing amino acids mainly occurs in the side
chains containing aromatic rings.
8.3.5. Maillard Reaction
Foods containing proteins and reducing carbohydrates or carbonyl compounds (such as
aldehydes and ketones produced by lipid oxidation) are subject to Maillard reactions during
processing and storage. These reactions yield brown or black melanoidins, which impart
breads and bakery products with the brown color. The formation of melanoidins is
accompanied by the cross-linking of a small amount of proteins. The cross-linking
significantly reduces the digestibility of these proteins. Studies on some protein-carbohydrate
model systems reveal that melanoidins are mutagenic and the capacity depends on the degree
of Maillard reactions. Melanoidins are insoluble in water and are only weakly absorbed on
intestinal wall. Hence, melanoidins are only slightly physiologically toxic to human.
However, the low molecular weight precursors of melanoidin are absorbed easily.
8.3.6. Enzyme Treatment
Enzymatic hydrolysis can improve the quality of food proteins. For example, papain can
tenderize meat and chymotrypsin can coagulate casein. Papain, bromelain, pepsin and
protease produced by microorganisms can partially hydrolyze thermal denatured or solvent
denatured proteins and improve their solubility. The hydrolytes can be used in acidic or hot-
Proteins
185
processed drinks. The hydrolytes can also be used as alternative protein sources for patients
allergic to milk and gluten or those with digestive tract diseases.
Partial hydrolysis can improve the emulsifying and foaming abilities of thermally
denatured proteins, because the increased solubility of proteins facilitates their diffusion to
the oil/water and gas/water interfaces. However, when the degree of hydrolysis exceeds
3%~5%, the viscosity and thickness of protein layer absorbed on the interface are insufficient
to stabilize emulsion and foam. Hydrolysis reduces the volume of proteins, which is
unfavorable for the gelling ability and viscoelasticity of proteins, but limited hydrolysis of
gluten can enhance the expansion degree of dough in bread making and improve the flakiness
of biscuits.
In addition, proteases can connect low molecular weight peptides through peptide
transferring to produce new larger peptides, namely proteinoids.
186
Peptides with molecular weight greater than 6kD cannot the action sites of taste
receptors and are hence tasteless. Whether a peptide with molecular weight less than 6kD is
bitter and its bitter intensity is related to its hydrophobicity. For details, see Section 5.1.3.
9.2. Off-Odors
Some protein products must undergo the deodorizaton process to remove off-odor
compounds bound to proteins. Ketones, aldehydes, alcohols, phenols, and lipid oxidation
products can produce beany flavor, rancidity, bitterness, and harsh taste. These compounds
can bind to proteins. When the proteins are cooked or chewed, these compounds are released
and the undesired tastes or odors are delivered to consumers, which markedly reduce the
acceptability of foods.
In addition to off-odors, proteins can also serve as the carrier of flavors. For example,
textured vegetable proteins can impart the meat flavor. Ideally, the desired volatile flavor
components should bind to carriers during storage and processing and be released rapidly and
completely in the oral cavity upon ingestion. Any factors that change the conformation of
proteins affect the binding to volatile compounds to proteins. In the presence of water
facilitates the binding to polar compounds to proteins, but shows no effect on that of nonpolar
compounds. Volatile compounds have only limited diffusion in dried protein components.
However, when the water activity is slightly improved, volatile compounds diffuse to their
binding sites rapidly. Casein can bind more volatile carbonyl compounds, alcohols and esters
in neutral and alkaline conditions than in acidic solutions. Oxidates and sulfates in high
concentrations can cause protein unfolding and thus improve the binding of proteins to
carbonyl compounds. Agents that can dissociate proteins or interrupt disulfide bonds improve
the binding of proteins to volatile compounds. When oligomers are dissociated to subunits,
the hydrophobic areas between subunits are masked during conformation change of the
subunits. Hence, the binding to nonvolatile compounds is reduced.
Thorough hydrolysis of proteins reduces their ability of binding volatile compounds. For
example, one kilogram of soybean protein can bind 6.7 mg caproaldehyde. After the protein
is hydrolyzed by acidic protease, the binding capability is reduced to 1 mg/kg protein. Hence,
the beany flavor of soybean protein can be alleviated by hydrolysis. Thermally denatured
proteins generally have improved volatile binding capabilities. For example, when 10%
soybean protein isolate is heated at 90C for 1~24h in the presence of caproaldehyde and is
then free dried, the amount of caproaldehyde bound is 3~6 times more than that of unheated
protein. Dehydration process, such as free drying, can release more than 50% of bound
volative compounds. However, if a volatile compound has a low vapour pressure and is
present in low content, it can be well retained after the treatments. It should be noted that the
presence of lipids is beneficial for the binding and retention of volative compounds, including
those generated by lipid oxidation.
Proteins
187
derivates, and dihydrochalcone and their derivates. The potential of perilla aldehyde and its
derivates as sweetener has also attracted much attention.
Some naturally occurring amino acids have been found to be sweet, including Gly, DAla, L-Ala, D-Ser, L-Ser, D-Thr, L-Thr, D-Trp, D-Pro, D-hydroxyproline, and D-Glu. Some
amino acid derivates are also found to be sweet. For example, the specific saccharinity of 6methyl-D-Trp reaches 1000 and is a potential novel sweetener.
In 1969, it was found that many dipeptide derivates of aspartic acid are sweet and
phenylalanine methyl ester (aspartame) has been approved by FDA for use in foods as a
sweetener. Aspartame is the sweetest compound among all sweeteners identified and is 2.7
times sweeter than sucrose. These dipeptide sweeteners are non-sugar compounds. Their
components are natural molecules and can be metabolized by human body. Besides, their
sweetness curves fit that of sucrose very well and the sweetness tastes very well. The
shortcoming is that they are unstable in high temperatures.
Sweet dipeptide derivatives have the following structural characteristics:
The two amino acids are of the L form.
The amino acid in the N terminal is Asp and its COOH and NH2 groups are free.
Another amino acid is neutral and one of the ends must be esterified. The smaller the
ester group, the sweeter the dipeptide.
The sweet intensity decreases with the increase of molecular weight.
188
importance of careful selection of HHP treatment times and flavor concentrations for desired
outcomes in food application [31].
Milk protein-flavor interactions are very dependent on the conformational state of a
protein. Therefore, factors such as pH, temperature, and high pressure that influence protein
conformation can markedly change flavor binding characteristics of proteins. Interactions of
vanillin with soy, casein, and whey proteins Bindings of vanillin with casein and whey
protein were enthalpy driven, while the interaction of vanillin with soy protein was highly
entropy driven. The researchers inferred that conformational changes of soy protein might be
important in binding of vanillin [32].
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[1]
[2]
[3]
[4]
[5]
[6]
[7]
[8]
[9]
[10]
[11]
[12]
[13]
[14]
[15]
[16]
[17]
[18]
[19]
Guang B, Lin H, Wang GC. Food Protein Chemistry. Beijing: Chemical industry press,
2005.
Murray RK, Granner DK, Rodwell VW, Mayes PA. Harper's Biochemistry. 25th
edition. McGraw-Hill Companies, 1999.
http://www.hemaquest.com/indications/hemoglobin.asp.
Xie, BJ. Food chemistry. 1st edition. Beijing: Science Press, 2004: 255.
Damodaran S. Influence of protein conformation on its adaptability under chaotropic
conditions. International Journal of Biological Macromolecules, 1989, 11:2-8.
Han JM, Ledward DA. High pressure/thermal treatment effects on the texture of beef
muscle. Meat Science, 2004, 68: 347-355.
Wang DF. Food Chemistry. 1st edition. Beijing: Chemistry Industry Press. 2007: 118.
Xie BJ. Food chemistry. 1st edition. Beijing: Science Press, 2004: 259.
Xie BJ. Food chemistry. 1st edition. Beijing: Science Press, 2004: 260.
Hu WW, Xie BJ. Food Chemistry. 1st edition. Beijing: Science Press, 1992: 165.
Damodaran S. Interfaces, protein films, and foams. Advances in Food and Nutrition
Research. 1990, 34: 1-79.
Xie BJ. Food chemistry. 1st edition. Beijing: Science Press. 2004: 280.
Wang DF. Food Chemistry. 1st edition. Beijing: Chemistry Industry Press. 2007: 118.
Xie BJ. Food chemistry. 1st edition. Beijing: Science Press. 2004: 278.
Xie BJ. Food chemistry. 1st edition. Beijing: Science Press. 2004: 281.
Pusztai A, Clarke EMW, Grant G, King TP. The toxicity of Phaseolus vulgaris lectins.
Nitrogen balance and immunochemical studies. Journal of the Science of Food and
Agriculture. 1981, 35: 701-711.
Zhu H, Damodaran S. Effects of calcium and magnesium ions on aggregation of whey
protein isolate and its effect on foaming properties. Journal of Agricultural and Food
Chemistry. 1994, 42: 856-862.
Eggum BO, Beames RM. The nutritive value of seed proteins. In: Gottschalk W,
Mller PH. Seed Proteins: Biochemistry, Genetics, Nutritive value. Berlin: Springer.
1983: 499-531.
FAO/WHO/UNU. Energy and Protein Requirements, Report of a Joint
FAO/WHO/UNU Expert Consultation. World Health Organization Technical Report
Series. 1985: 724.
Proteins
189
[20] Lund D. Effect of commercial processing on nutrients. In: Karmas E, Harris RS.
Nutritional Evaluation of Food Processing. New York: Van Nostrand Reihhold. 1988:
319-354.
[21] Wang DF. Food Chemistry. 1st edition. Beijing: Chemistry Industry Press. 2007: 124.
[22] Hurrell RF, Carpenter KJ. Mechanisms of heat damage in proteins. The role of sucrose
in the susceptibility of protein foods to heat damage. British Journal of Nutrition. 1977,
38: 285-297.
[23] Je JY, Park PJ, Kim, SK. Antioxidant activity of a peptide isolated from Alaska pollack
(Theragra chalcogramma) frame protein hydrolysate. Food Research International.
2005, 38: 45-50.
[24] Kim SY, Je JY, Kim SK. Purification and characterization of antioxidant peptide from
hoki (Johnius belengerii) frame protein by gastrointestinal digestion. The Journal of
Nutritional Biochemistry. 2007, 18: 31-38.
[25] Song R, Wei RB, Zhang B, Yang ZS, Wang DF. Antioxidant and Antiproliferative
Activities of Heated Sterilized Pepsin Hydrolysate Derived from Half-Fin Anchovy
(Setipinna taty). Marine Drugs. 2011, 9: 1142-1156.
[26] Song R, Wei RB, Zhang B, Yang ZS, Wang, DF. Optimization of the Antibacterial
Activity of Half-Fin Anchovy (Setipinna taty) Hydrolysates. Food and Bioprocess
Technology. 2011: 1-11.
[27] Rajapakse N, Mendis E, Jung WK, Je JY, Kim SK. Purification of a radical scavenging
peptide from fermented mussel sauce and its antioxidant properties. Food Research
International. 2005, 38: 175-182.
[28] Virtanen T, Pihlanto A, Akkanen S, Korhonen H. Development of antioxidant activity
in milk whey during fermentation with lactic acid bacteria. Journal of Applied
Microbiology. 2007, 102: 106-115.
[29] Minelli A, Bellezza I, Grottelli S, Galli F. Focus on cyclo(His-Pro): history and
perspectives as antioxidant peptide. Amino acids. 2008, 35: 283-289.
[30] Khn J, Considine T, Singh H. Binding of Flavor Compounds and Whey Protein
Isolate as Affected by Heat and High Pressure Treatments. Journal of Agricultural and
Food Chemistry. 2008, 56: 10218-10224.
[31] Liu XM, Powers JR, Swanson BG, Hill HH, Clark S. High Hydrostatic Pressure
Affects Flavor-binding Properties of Whey Protein Concentrate. Journal of Food
Science. 2005, 70: C581-C585.
[32] Li Z, Grn IU, Fernando, LN. Interaction of Vanillin with Soy and Dairy Proteins in
Aqueous Model Systems: A Thermodynamic Study. Journal of Food Science. 2000,
65: 997-1001.
ISBN: 978-1-61942-125-7
2012 Nova Science Publishers, Inc.
Chapter 6
VITAMINS
1
ABSTRACT
Vitamin is one important group of nutrients that determines the nutritional value of
foods. These compounds play extremely important role in many metabolisms in organism
as cofactors of various enzymes and long-term vitamin deficiency can cause various
diseases and even death. Besides, some vitamins, such as Vc and sulfur-containing
compounds, also markedly affect the color and flavor of foods. This chapter introduces
the structures, properties, physiological functions and deficiency symptoms, and stability
of the vitamins that have been identified one by one. Then, the factors that influence
vitamin contents in foods and the changes of vitamins during processing and storage are
discussed.
1. CLASSIFICATION OF VITAMINS
Vitamins are classified by their biological and chemical activities, as well as the
chronological order of being found, but not their structures. Basically each "vitamin" has a
multiple chemical substances (called vitamers) that show similar biological activity, rather
than having a fixed chemical structure. For example, Vitamin A includes retinol, retinal, and
four known carotenoids. The classification and some functions of vitamins are summarized in
Table 6-1.
Vitamins are classified into two water-soluble and fat-soluble ones according to
solubility. Among the 13 vitamins identified, the eight members of the B family and vitamin
C are water soluble, while vitamins A, D, E, and K are fat soluble.
192
Category
Watersoluble
Name
VB1
Synonyms
Thiamine, Antineuritic factor
Physiological functions
Antineuritic Prevent beriberi
VB2
Riboflavin
VB3,VPP
VB6
VB9
VB12
Fat-soluble
VB7,VH
Cyanocobalamin,
hydroxycobalamin,
methylcobalamin
Biotin
V B5
Pantothenic acid
VC
Ascorbic acid
VA1,2
Antixerophthalmic vitamin,
carotenoids,
retionol, retinal
VD1,3
Cholecalciferol, Lexacalcitol,
Resistant rickets
VE
VK1,2,3
Because water-soluble vitamins can dissolve in body fluid and can not be stored readily,
consistent daily intake is required. On the other hand, fat-soluble vitamins, absorbed through
the intestinal tract with the help of lipids (fats), can be easily accumulated in the body. Watersoluble vitamins are readily excreted from the body so their consumption can be simply
checked by the degree of urinary output.
2. VITAMINS IN FOODS
As described above, vitamins are a class of natural organic compounds that maintains the
normal physiological functions of human body. Although, the amount required for daily diet
is only several micrograms or milligrams, they are essential for human health.
Microorganisms in intestines can synthesize some vitamins, but the quantity far from the need
of human body. Therefore, vitamins have to be largely provided by foods.
2.1. Vitamin A
Vitamin A, including vitamin A1 (retinol) and vitamin A2 (3-dehydroretinol), is also
called antixerophthalmic vitamin, and its deficiency can cause night-blindness,
193
Vitamins
hyperkeratosis, and keratomalacia. Vitamin A is needed by the retina of the eye as the lightabsorbing molecule of retinal, without which the vision will be lost. An oxidized form of
vitamin A retinoic acid, is a hormone-like growth factor for epithelial and other cells.
Vitamin A was discovered in 1917 by Elmer McCollum (University of WisconsinMadison),
Lafayette Mendel (Yale University) and Thomas Burr Osborne (Yale University). In 1919,
Steenbock (University of Wisconsin) proposed that yellow plant pigments (beta-carotene)
might be vitamin A, which was named as fat-soluble factor A". Vitamin A exists in animal
tissues, plant tissues and fungi.
(1) Structure.
Structures of vitamin A and its precursors are shown in Table 2.
Structure
Relative
activity
-carotene
50
-carotene
25
-Apo-8carotenal
25-30
Zeaxanthin
Canthaxanthin
Astacin
Lycopene
0
194
the beta-ionine ring. Usually vitamin A refers to vitamin A1, retinol. The biological effect of
vitamin A2 is about 40% of that of vitamin A1.
In foods of animal origin, the major form of vitamin A is an ester, primarily retinyl
palmitate, which is converted to retinol in small intestine. Retinol can be converted to its
visually active aldehyde form, retinal. The associated acid (retinoic acid), a metabolite that
can be irreversibly degraded from vitamin A, has only partial vitamin A activity, and does not
function in the retina for the visual cycle.
Food carotenoids, mainly include beta-carotene and lutein (Table 6-2), are also
precursors of vitamin A. Usually they have two connected retinyl groups, which are used in
the body to contribute to vitamin A activity. The well-known orange pigment of carrots (betacarotene), which shows some vitamin activities itself, is an important source of vitamin A.
(2) General properties.
Usually, vitamin A is a light yellow viscous liquid. Pure vitamin A1 is a light-yellowish
(or primrose yellow) crystal and melts at 62C-64C. Vitamin A is fat soluble and is stable
under alkali conditions or inert atmosphere. Vitamin A is thermal stable and is not destroyed
in temperatures up to 120C-130C, but it is liable to decomposition in exposure to air,
oxidants and ultraviolet radiation. Both vitamin A and carotene can react with antimony
trioxide in ethanol to produce dark blue yellow. This property has been used for the
spectrometric determination of vitamin A and carotene.
(3) Physiological functions and deficiency symptoms.
Vitamin A promotes the growth of human body. Besides, it maintains the integrity and
health of epithelial tissue and ensures the normal vision.
Deficiency of vitamin A for a long time can cause night blindness and loss of dark
adaptation. In subjects suffering severe vitamin deficiency, the keratinized epithelial cells at
gastrointestinal tract and eye cornea can even not be produced. The obvious characteristic of
vitamin A deficiency is xerophthalmia, such as cornea hyperemia, inflammation and sclerosis.
This is why vitamin A is also known as the antixerophthalmic vitamin. Excessive intake of
vitamin A (more than 65,000~500,000 international units) can result in poisoning, but the
symptoms can disappear several days later if vitamin A is excluded from the diet.
(4) Stability and degradation.
All naturally occurring carotenoids are present in the trans conformation. The compounds
can transform to the cis conformation and lose its activity when heating. The isomerization of
carotenoids occurs readily during storage, as shown in Table 6-3. In addition, exposure to
light, acids and watery iodine also causes the transform from cis- to trans-conformation of
carotenoids and retinols.
The destruction mechanisms of vitamin A precursors vary with processing conditions
(Figure 6-1). The cis-trans transformation of beta-carotenes upon heating occurs only in the
absence of oxygen. Beta-carotene is decomposed to a series of aromatic hydrocarbons at
higher temperatures and the major decomposition product is lonene, which has important
implications on food flavor. Carotene is often intentionally added to foods to produce aroma
during food processing.
Vitamins
Table 6-3. Distribution of -carotene isomers in fresh fruits and
processed vegetables [1]
Products
Status
Sweet potato
Fresh
Canned
Fresh
Canned
Fresh
Canned
Fresh
Canned
Fresh
Canned
Fresh
Pasteurized
Fresh
Canned
Fresh
Canned
Dehydrated
Canned
Fresh
Fresh
Carrot
Pumpkin
Spinage
Collard
Cucumber
Pickld cucumber
Tomato
Peach
Apricot
Nectarine
Plum
195
196
Content (mg/kg)
980-1860
870-1125
636-987
Oxygen, light, enzymes, and lipid hydroperoxide enhance the oxidative degradation of
carotene. Oxidation of beta-carotene first involves the formation of the 5, 6-epoxide, which
will isomerize to beta-carotene oxide, namely 5, 8-epoxide. Vitamin A and provitamin A are
usually inactivated in dehydrated foods, but the loss varies with the drying technology (Table
6-4). Maintenance of Aw and oxygen partial pressure in low levels can reduce the loss of
carotenoid and vitamin A.
2.2. Vitamin D
Vitamin D is also known as anti-rickets or anti-rachitis vitamin. Six members have been
ascertained, including Vitamin D2, Vitamin D3, Vitamin D4, Vitamin D5, Vitamin D6, and
Vitamin D7, among which Vitamin D2 and Vitamin D3 are the most important.
Vitamin D in food always coexists with vitamin A. Fat in fishes or liver in animals are
rich in vitamin D. The content of Vitamin D in fish oil from seafood is much high, followed
by egg yolks, milk, and butter. Sunlight can promot the synthesis of vitamin D in animals.
Thus, the levels of vitamin D in milk and cream produced in summer are more than those in
winter due to the stronger sunlight in summer.
(1) Structure.
The vitamin D members are steroids that contain the cyclopentanoperhy drophenanthrene
ring structure and they are distinguished by their structures of the branch chain R, as shown in
Figure 6-2. Vitamin D is found only in animal tissues, but most plants contain sterols, which
can be converted to vitamin D by ultraviolet light.
(2) General properties.
Vitamin D members are colorless crystal and fat soluble. Vitamin D is quite stable
against acids, alkali, and oxygen, but is readily destroyed by light and temperatures higher
than 160C.
(3) Physiological functions and deficiency.
Vitamin D regulates the metabolism of calcium and phosphorus and maintains the level
of calcium and phosphorus in blood. Hence, the deficiency of calcium and phosphorus is
often related to the level of vitamin in human body. The increased requirements of pregnant
and lactating women on calcium and phosphorus can be realized by vitamin D-reinforced
diets.
Vitamin D deficiency leads to osteomalacia and rickets. However, excessive intake of
vitamin D can cause posioning. The symptoms of acute vitamin D poisoning include loss of
appetite, nausea, vomiting, diarrhea, headache and polyuria and those of chronic poisoning
include weight loss, albinism, and even soft-tissue calcification or serious kidney failure.
197
Vitamins
CH 3
19
11 12 13
14
9
8
CH 2
2
3
1
4
10
5
R
17 16
15
HO
Vitamin D2
R=
CH
CH
CH
CH
CH3
Vitamin D3
R=
CH
CH
CH3
CH3
CH2
CH2
CH2
CH
R=
CH
CH2
CH2
CH
CH
CH3
Vitamin D5
R=
CH
CH2
CH3
Vitamin D6
R=
CH
R=
CH
CH3
CH
CH 2C H 3
CH
CH
CH3
Vitamin D7
CH
CH
CH
C H 2C H 3
CH2
CH
CH3
CH2
CH
CH3
CH3
CH3
CH2
CH2
CH3
CH3
Vitamin D4
CH2
CH3
CH3
CH3
CH3
CH3
CH3
2.3. Vitamin E
Vitamin E is also called as anti-sterility factor or tocopherol and is a family of eight
separate compounds, in which, -, -, -, -tocopherols are the most important and tocopherol is the most active. Hence, tocopherol sometimes refers solely to -tocopherol.
The contents of tocopherol in some foods are listed in Table 6-5. The content of vitamin
E is often expressed as international unit (IU). One IU of vitamin E is equal to 1 mg of D, L-tocopherol acetate or 0.667 mg of D--tocopherol.
(1) Structure.
Vitamin E is derivatives of benzo-3 H-pyran and its general structure is shown in Figure
6-3. The members of the vitamin E family differ in the structures of the three side chains, as
listed in Table 6-6.
(2) General properties.
Pure vitamin E is a transparent and light yellow oily liquid. It is fat soluble and is stable
against acid, alkaline and heating (up to 200C in the absence of oxygen), but it is susceptible
to oxidation by oxygen. Hence, vitamin E is an important natural antioxidant in foods.
Vitamin E is quiet stable under white light, but is easily destroyed by ultraviolet light.
(3) Physiological function and deficiency.
198
-T
-T3
-T
-T3
-T
-T3
- T3
56.4
0.013
17.9
40.3
27.2
9.0
9.1
0.013
0.007
0.021
0.002
5.37
0.008
5.19
2.45
0.039
2.80
0.196
0.214
0.16
0.153
0.207
0.394
0.437
0.87
1.1
0.417
0.4
0.43
13.1
60.4
38.3
56.6
0.471
0.84
0.023
0.03
0.078
0.089
6.17
0.026
13.2
0.087
0.922
37.1
0.457
2.52
0.043
0.002
4.0
16.4
6.9
Spinage
26.05
Beef
2.24
Flour
8.2
Barley
0.02
Notes: T-tocopherol; T3- tocotrienol.
9.14
1.7
7.0
2.8
]3
]3
Name
R1
R2
R3
Occurrence
Relative
biological value
- tocopherol
-CH3
-CH3
-CH3
Wheat embryo
- tocopherol
- tocopherol
- tocopherol
- tocopherol
- tocopherol
-CH3
-H
-H
-CH3
-H
-H
-CH3
-H
-CH3
-CH3
-CH3
-CH3
-CH3
-H
-H
Wheat embryo
Corn
Bean
Rice
Rice
0.5
0.2
0.1
0.5
0
- tocopherol
-CH3
-H
-CH3
Corn
0.5
1- tocopherol
-CH3
-CH3
-CH3
Rice
0.5
Vitamins
199
Figure 6-4. Oxidation pathway of -tocopherol initiated by peroxide free radicals [6].
2.4. Vitamin K
Vitamin K is found due to its blood coagulation functions. Two kinds of vitamin K have
been identified, including vitamin K1, which is extracted from alfalfa, and vitamin K1, which
is obtained from degraded fishes.
200
Vitamin K occurs mainly in plant tissues. Green leafy vegetables, such as alfalfa,
cabbage, cauliflower, spinach and cabbage, contain more vitamin K1 than vitamin K2, with
the latter derived mainly from the metabolism of intestinal bacteria.
(1) Structure.
Vitamin K1 and K2 are the derivatives of 2-methyl-1, 4-naphthoquinone and the two
compounds differ in their side chains, as shown in Figure 6-6.
(2) General properties.
Vitamin K1 is a viscous yellow oily liquid can be crystallized from alcohol solution
under low temperature, and its melting point is -20 C. Vitamin K2 is a yellow crystal and
melts in the temperature range from 53.5C to 54.5C. Both vitamin K1 and K2 are stable
201
Vitamins
against heating, but are readily destroyed by alkali and sunlight. K2 is more susceptible to
oxidation than K1.
(3) Physiological function and deficiency.
Vitamin K promotes blood coagulation and is essential for the synthesis of prothrombin
in liver. Vitamin K deficiency leads to reduced content of prothrombin in plasma and
prolonged duration of blood coagulation. Vitamin K will lose its promotion of prothrombin
synthesis in liver if liver dysfunction occurs. In addition, vitamin K also enhances intestines
peristalsis and secretion.
2.5. Vitamin B1
Vitamin B1 is also known as thiamin. Yeast is reported to have the highest content of
vitamin B1, followed by muscle, drupe, and eggs. Vitamin B1 in cereals occurs mainly in
cortex and embryo. Table 6-7 lists the contents of vitamin B1 in some cereal products.
(1) Structure.
Vitamin B1 contains a pyrimidine ring that contains an amino group and a thiazole ring
thatn contains a sulfur residue, as shown in Figure 6-7.
(2) Properties.
The hydrochloride salt of vitamin B1 is a white crystal. The crystal is stable at 100C for
24 hours, but is decomposed in temperatures higher than 249C. Vitamin B1 is water soluble
and one gram of vitamin B1 can dissolve in 1mL water, 18 mL glycerin, 100 mL 95% alcohol
or 315 mL anhydrous alcohol, but is insoluble in ethyl ether, acetone, chloroform or benzene.
Vitamin B1 has a smell similar to that of yeast and tastes bitter.
Table 6-7. Contents of vitamin B1 in some cereal products
(mg/100g Dry)[8]
Name
Wheat
Vitamin B1 content
0.37-0.61
Names
Brown rice
Vitamin B1 content
0.3-0.45
Bran
Embryo
Flour (85% yield)
(73% yield)
(60% yield)
Potato
0.7-2.8
1.56-3.0
0.3-0.4
0.07-0.1
0.07-0.08
0.08-0.1
Cortex
Rice embryo
Endosperm
Corn
Soybean
Pea
1.5-3.0
3.0-8.0
0.03
0.3-0.45
0.1-0.6
0.36
202
Vitamin B1 is stable in solutions with pH less than 3.5. Under these conditions, the
vitamin can maintain its activity even when heated at 120C; however, it is easily destroyed
when the pH exceeds 3.7. For example, 25% of thiamin is lost when heated in 97C at pH 4.3
for 1 hour and the value reaches 80% when the pH is further increased to 7.0. Though vitamin
B1 is readily damaged by high temperatures in alkaline conditions, cooking is insufficient to
completely destroy the vitamin in rice. During bread bakery, about 15~30% of the total
amount of vitamin B1 in flour is lost.
Both vitamin B1 and its pyrophosphate salt can be oxidized by mild oxidant (such as the
alkaline solution of potassium ferricyanide) to produce the dark blue fluorescence-emitting
thiochrome. This reaction has been used to quantitative determination of vitamin B1. The
structure of thiochrome is shown in Figure 6-8:
Thiamine can be converted to thiamine pyrophosphate (TPP, Figure 6-9) by thiamine
kinase in the presence of ATP. TPP plays an important role in sugar metabolism.
(3) Physiological function and deficiency.
Vitamin B1 participates in the oxidative decarboxylation of -keto acid, such as pyruvic
acid and - ketoglutaric acid, as cocarboxylase. Vitamin B1 deficiency results in the
accumulation of pyruvic acid in blood. Meanwhile, the accumulated pyruvic acid inhibits the
activity of dehydrogenase and leads to the accumulation of lactic acid. Hence, vitamin B1 is
essential for sugar metabolism.
Vitamin B1 is of special importance for consumers with starch as the main energy source.
It is reported that the amount of vitamin B1 required is propontional to the amount of
carbohydrates consumed and it is recommended that 1 microgram of vitamin B1 is needed for
the metabolism of 1 gram of carbohydrates.
The early symptom of vitamin B1 deficiency includes nervous system disorder, mental
and physical fatigue, dyspepsia and loss of appetite. If vitamin B1 cannot be supplemented in
time, the patients develop polyneuritis or beriberi. In this stage, the patients become poor in
heath status and other symptoms include lower limb edema, nerve paralysis, loss of muscle
contraction capacity, and even death.
(4) Stability and degradation.
Vitamin B1 is the most unstable among all the vitamins identified and is susceptible to the
influence of aw, pH, temperature, ionic strength, buffer solution and the presence of other
compounds. The degradation of vitamin B1 is initiated by the nucleophilic substitution of the
Vitamins
203
methylene carbon between the two rings. Therefore, vitamin B1 can be readily destroyed by
strong nucleophiles such as HSO3-.
Vitamin B1 is stable at low aw and room temperature. For example, nearly no loss of
vitamin B1 is observed when cereal foods with aw ranging from 0.1 to 0.65 are stored at
37C. In storage temperature 45C and aw 0.2~0.5, the decomposition of vitamin B1
increases. The maximum vitamin B1 degradation is observed in aw 0.5. As the aw further
increases, the loss of vitamin B1 decreases, as shown in Figure 6-10.
Temperature significantly affects the retention of vitamin B1 during storage (Table 6-8).
In 1.5C, no loss of vitamin B1 is detected in tomato juice, pea and orange juice after storage
for 12 months. When the storage temperature is elevated to 35C, up to 50% of vitamin B1 is
lost.
The relationship between vitamin B1 degradation rate and pH is shown in Figure 6-11.
The same relationship is observed in either phosphate buffer or cereal. That is, the
degradation of vitamin B1 increases with the rise of pH.
Similar to other other-water soluble vitamins, rinsing and boiling cause great loss of
vitamin B1. Table 6-9 lists the effect of various processing methods on the retention of
vitamin B1 in various foods.
The thermal degradation of Vitamin B1 can generate special flavor compounds, such as
hydrogen sulfide, furan, and dihydro-thiophenol. These compounds impart foods with special
flavor.
2.6. Vitamin B2
Vitamin B2 is also known as riboflavin and is found mainly in yeast, liver, milk, muscle
and yolk. In addition, Greenery vegetables, grain and germinated seed also contain vitamin
B2.
Figure 6-10. Relationship between vitamin B1 degradation rate and aw of cereal foods when stored at
45C [9].
204
Species
Species
Apricot
35
72
Tomato juice
60
100
Mungbean
Lima bean
8
48
76
92
Pea
Orange juice
68
78
100
100
Treatment
Retention (%)
Cereal
Potato
Extrusion, Cook
Fried after immerse in water for 16 hr
Fried after immerse in sulfurous acid solution for 16 hr
Boiled in water or carbonate after immerse in water
Various heat treatments
Various heat treatments
Various heat treatments
48-90
55-60
19-24
23-52
82-97
80-95
77-100
Soybean
Smashed potato
Vegetable
Freeze or fried
fish
Vitamins
205
(1) Structure.
Riboflavin is the condensation product of D-ribitol and 7, 8-dimethyl-isoalloxazine. The
structure of vitamin B2 is showed in Figure 6-12.
(2) General properties.
Riboflavin is an orange needle crystal and tastes bitter taste. This vitamin melts in 282 C
and sparingly soluble in water, but readily soluble in alkaline solutions.
The aqueous solution of riboflavin generates yellow fluorescence in wavelength range
440~500nm. This property can be used to spectrometrically determine the content of the
compound.
Riboflavin is more thermal stable than vitamin B1. After dried yeast is heated in 120 C
for several hours, nearly all vitamin B1 is lost, but vitamin B2 is completely retained.
Riboflavin is unstable in the presence of light and ultraviolet, especially in alkaline and
high temperature conditions. In the presence of light, riboflavin in alkaline solutions is
converted to lumiflavin. This product has the same color and fluorescence emission capability
as riboflavin. In acidic or neutral solutions, riboflavin is transformed to lumichrome, which
can emit blue fluorescence. The structures of the two compounds are illustrated in Figure 613.
(3) Physiological function and deficiency.
Vitamin B2 is an essential cofactor for enzymes involved in cellular respiration and
dehydrogenation. Vitamin B2 deficiency leads to reduced respiration capacity and retarded
metabolism. The symptoms of vitamin B2 deficiency include stomatitis, angular cheilitis, eye
keratitis, and dermatitis.
(4) Stability and degradation.
Riboflavin is stable against thermal treatment and oxygen. Riboflavin is resistant to light
in acidic solutions, but is readily decomposed by light in alkaline solutions. In light-induced
decomposition, photochemical degradation occurs in ribitol to generate inactive lumiflavin
and a series of free radicals (Figure 6-14). Lumiflavin has stronger oxidizability than
riboflavin and its generation accelerates the destruction of other vitamins, especially Vc. The
special off-odor of sunlight-exposed milk has been attributed to the light-induced
decomposition of riboflavin.
206
CH CO NH CH2
CH3 OH
Figure 6-15. Structure of vitamin B5.
CH2
COOH
207
Vitamins
4
5 3
61 2
CONH2
COOH
N
Nicotinic acid
N
Nicotinamide
Pantothenic acid is light yellow and viscous. It is soluble in acetic acid and water, but
insoluble in chloroform and benzene. In neutral solutions, pantothenic acid is resistant to heat,
oxidation and reduction, but can be decomposed -alanine and other compounds by acids,
bases, and dry heating. The calcium salt of pantothenic acid is a colorless crystalline powder.
Calcium pantothenate tastes slightly bitter and is water soluble. It is stable against light and
air, but its aqueous solutions of pH 5~7 can be destroyed by heat.
In organisms, pantothenic acid takes effect mainly in the form coenzyme A (CoA) form.
(3) Physiological function.
Pantothenic acid is the coenzyme of many enzymes involved in carbohydrate, lipid and
protein metabolism and plays an important role in the transfer of the acetyl group.
Pantothenic is also essential for the growth of some microorganisms.
(4) Stability and degradation.
Pantothenic acid is stable in neutral solutions, but is easily decomposed in acid solutions.
In the pH range 6~4, its decomposition rate increases with the increase of acidity. Due to the
heat liability and strong hygroscopicity of pantothenic acid, the calcium salt of pantothenic
acid has been commercially used as an alternative. The changes of pantothenic acid contents
in foods are affected by processing methods in addition to the materials. For example, the loss
of pantothenic acid in pasteurized milk is usually less than 10%. The loss of pantothenic acid
in vegetables is about 10-30 % and most of vitamin is lost during rinsing. The bioavailability
of dietary pantothenic acid is about 51%.
2.8. Vitamin B3
Vitamin B3 is known as vitamin PP and is famous for its anti-pellagra capability. Two
members of the family have been identified, including nicotinic acid and nicotinamide. Both
te two compounds occur widely in yeasts, liver, muscle, milk, peanut, and soybean. The
cortex and embryo of cereal grains also contain high levels of the two compounds.
(1) Structure.
Both nicotinic acid and nicotinamide are the derivates of pyridine and their structures are
shown in Figure 6-16.
(2) Properties.
Both nicotinic acid and nicotinamide are colorless needle crystals. Nicotinic acid melts in
235.5-236C. It is sparingly soluble in water but readily soluble in ethanol. The melting point
of nicotinamide is 129-131C and the compound is readily water soluble. Nicotinic acid is the
most stable among all the vitamins identified and is not destroyed by light, air, heating, acids,
or bases. Nicotinamide is converted to nicotinic acid in acidic solutions upon heating.
208
Nicotinic acid can react with cyanogen bromide to yield a yellow-green compound. This
reaction has been used for the quantitative analysis of nicotinic acid and nicotinamide.
The double bond between C4 and C5 can be reduced. Hence, the two compounds can be
present either in oxidized or reduced form.
Nicotinamide implements its in vivo function as nicotinamide dinucleotide (NAD, also
known as coenzyme I) or nicotinamide dinuclotide phosphate (NADP, CoII). NADP can be
converted from NAD by phosphorylation with ATP.
(3) Physiological functions and deficiency.
Nicotinamide is a main component of CoI and CoII, which are the coenzymes of many
dehydrogenases. Nicotinamide in the two enzymes occur either in the reduced and oxidized
states and the transformation between the two states realize the transfer of hydrogen (Figure
17).
Nicotinamide deficiency results in pellagra. The symptoms in the early phase include
symmetrical dermatitis in hands, cheeks, foreheads and other naked areas, gastrointestinal
disorders, mouth and tongue inflammation, indigestion and diarrhea. If nicotinamide is not
supplemented in time, the patients might suffer neurological disorder and even death.
(4) Stability and degradation.
As mentioned previously, nicotinic acid is the most stable vitamin. However, nonchemical processing of vegetables, such as dressing and rinsing, can cause loss of this vitamin
as other water-soluble ones. The loss of nicotinic acid of pork and beef during storage is
attributed to biochemical reactions, roasting seems to have no effect the content of nicotinic
acid. No loss of nicotinic acid is detected in processed diary products.
2.9. Vitamin B6
Vitamin B6 is also called adermine and includes pyridoxine, pyridoxal, and
pyridoxamine. Vitamin B6 widely distributes in animals and plants. Wheat germ, rice bran,
soybean, peanut, yeast, liver, fish and meat are the major storage pool of this vitamin.
(1) Structure
Pyridoxine, pyridoxal and pyridoxamine are the derivatives of pyridine and their
structures are shown in Figure 6-18.
(2) Properties.
Pyridoxine, pyridoxal and pyridoxamine are colorless crystals and are readily soluble in
water and alcohol. The three compounds are stable in acidic conditions, but are easily
destroyed in alkaline conditions. Pyridoxine is heat tolerant, but the other two compounds are
not.
Vitamins
209
Pyridoxine can be converted to pyridoxal or pyridoxamine and all the three compounds
can be phosphorylated, of which, pyridoxal phosphate and pyridoxamine phosphate (Figure
6-19) are the major active forms of vitamin B6 and they are the coenzymes of amino acid
decarboxylases and amino transferases.
(3) Physiological functions and deficiency.
Vitamin B6 is the coenzyme of amino acid decarboxylases and amino transferases and
participates in many metabolism reactions. Long-term deficiency of vitamin B6 may cause
skin irritation and damage of the central nervous system and hematopoietic organ.
(4) Stability and degradation.
The three members of vitamin B6 exhibit excellent thermal stability, of which,
pridoxamine is the most stable and is selected in food fortification. In the presence of oxygen,
vitamin B6 can be transformed to inactive 4-pyridoxine acid by UV irradiation. Vitamin B6 is
easily degraded in alkaline solutions, but is stable in acidic conditions.
Vitamin B6 can react with amino acids to produce Schiff base when heated (Figure 6-20).
In acidic solutions, the formed Schiff base undergoes further dissociation. In addition, the
Schiff base can rearrange to yield many cyclic compounds.
Vitamin B6 suffers more or less loss during processing. For example, about a half of the
vitamin is lost in sterilized liquid milk and the loss further increases during storage for 7~10
days. High temperature-short time pasteurization (92C, 2~3s) causes only a loss of 30% in
milk, but the values reaches up to 84% when sterilized in 119~120C for 13 to 15 min.
210
2.10. Vitamin H
Vitamin H is also called biotin and includes - and -biotin, of which, the former exists
in yolk and the later in liver. Biotin widely distributes in plant and animal tissues. Most of
vitamin H is bound with proteins and only a little portion occurs in the unbound state. Many
organisms can synthesize biotin on their own. In human body, part of this vitamin is
synthesized by intestinal bacteria.
(1) Structure.
Both the two members of biotin are thionic compounds and they are differentiated by
their side chains, as shown in Figure 6-21.
(2) Properties.
Biotin is a colorless needle crystal and its melting point is 232~233C. Biotin is soluble
in hot water and ethanol, but is insoluble in ether or chloroform. It is stable against light,
heating, acids, but can be destroyed by high temperatures and oxidants.
(3) Physiological functions and deficiency.
Biotin is the cofactor of many carboxylases. It is the carrier of CO2 in many CO2 fixation
reactions. Because biotin can be synthesized intestinal microorganisms in addition to intake
from foods, biotin deficiency occurs rather occasionally compared with other vitamins. The
symptoms of biotin deficiency include dermatitis, muscle pain, hypersensitivity, fatigue,
anorexia, and slight anemia.
211
Vitamins
Folic acid is a bright yellow crystal and is sparingly soluble in water. It is easily
destroyed by light in aqueous solutions. Caron atoms in positions 5, 6, 7, 8 can be reduced by
NADPH2, positions to yield tetrahydrogen folic acid (THFA).
THFA is the carrier of many one-carbon groups, such as formyl, formaldehyde, and
methyl and plays important role in the synthesis of proteins and nucleic acids.
(3) Physiological function and deficiency.
Folic acid is involved in the synthesis of proteins and nucleic acids. Its deficiency can
cause blood diseases and the symptoms include pernicious anemia, glossitis and
gastrointestinal problems. Because intestinal bacteria can synthesize folic acid, the incidence
of folic acid deficiency is very low.
(4) Stability and degradation.
Dihydrofolate (FH2) and tetrahydrofolate (FH4) are easily oxidized in air and are
sensitive to pH. The two compounds are the most stable in pH ranges 8-12 and 1-2. In neutral
solution, FH4 and FH2, and folic acid are quickly oxidized to p-aminobenzoyl-L-glutamic
acid (PABG), pteridine, xanthine, 6-methyl pterin and many other pterin derivatives. FH4 is
oxidized more quickly in acidic solutions than in alkaline solutions and its oxidation products
include PABG and 7,8-dihydro-pterin-6-carboxyl aldehyde. Reducing agents, such as thiol
and ascorbic acid, can slow down the oxidation of FH2 and FH4.
The stability of several derivatives of THFA follows the decreasing order of 5-formyltetrahydrofolate > 5-methyl-tetrahydrofolate > 10-methyl-tetrahydrofolate > tetrahydrofolate.
Table 6-11. Loss of folic acid in some foods during processing [11]
Foods
Eggs
Liver
Atlantic plaice
Cauliflower
Carrot
Meat
Grapefruit juice
Tomato juice
Corn
Flour
Meat or
vegetables
Processing methods
Oil fried or cooking
Cooking
Cooking
Boiling
Boiling
-radiation
Canned or storage
Canned
Storage in dark for 1 year
Exposure to light for 1 year
Refining
Milling
Canned storage for 3 years
Canned storage for 5 years
212
The loss of folic acid in foods varies with food species and processing technologies, as
listed in Table 6-10.
Vitamins
213
Vitamin B12 is the coenzyme of many enzymes and participates in a variety of reactions.
For example, it is the carrier of methyl and is involved in the biosynthesis of methionine and
thymine. Besides, vitamin B12 increases the bioavailability of folic acid.
Vitamin B12 synthesized by intestinal microbes must combine with the special
mucoprotein (also known as endogenous factor) secreted by gastricism for its adsorption.
Lack of the endogenous factor retard the absorption of vitamin B12 and causes pernicious
anemia and lesions in nervous system, tongue and gastricism.
(4) Stability and degradation.
Vitamin B12 in aqueous solutions is stable in pH range 4~6 in dark environments and
room temperature, but it is quantitatively destroyed in alkaline solutions upon heating.
Reducing agents in low levels protect vitamin B12 from destruction, but those in high
concentrations have opposite effects. Trivalent iron salts can stabilize vitamin B12, but
bivalent iron salts rapidly destroy the vitamin.
2.14. Vitamin C
(1) Structure.
Vitamin C, or ascorbic acid, is an acid derivative of hexose. Vc occurs widely in fresh
fruits and vegetables. Only L-ascorbic acid is bioactive. The structure of vitamin C is shown
in Figure 6-25.
(2) Properties.
Vc is a colorless sliced crystal and melts in 190-192C. It is soluble in water and ethanol
and its aqueous solutions taste sour. Vc is unstable against heating, sunlight exposure, and
metal ions such as such as Cu2+, Fe3+. However, it is quite stable in oxalic acid or
metaphosphoric acid solutions. Vc is a strong reducing agent and can be reversibly oxidized
to the dehydrogenated form (Figure 6-25). Vitamin C has been widely used as an antioxidant
in the food industry.
L-ascorbic acid can reduce the blue dye 2, 6-dichlorophenol-indophenol to the colorless
leuco and react with 2,4-dinitrophenylhydrazine to yield colored hydrazone. These reactions
can be used for the qualitative and quantitative analysis of Vc.
214
R-CO-CO-COOH
Vitamins
215
Vc has been used as natural antioxidant in foods. For example, because Vc can reduce oquinone compounds and thus inhibit enzymatic browning, it has been used as a bread
improver. In addition, Vc can protect folic acid and other oxidizable compounds from
oxidation. Vc is also an effective free radical scavenger. It can remove singlet oxygen,
reducing oxygen and carbon-centered radicals, and regenerate other anti-oxidants such as
copherol. The changes of Vc content during food storage in an indicator of food quality
change. Because Vc is water soluble and is sensitive to heat, pH, and oxygen, processing and
storage cause serious Vc loss in foods. Figure 6-28 shows the effects of heating time on Vc
216
content, Figure 6-29 indicates the retention of Vc in various processing methods, and Figure
6-30 illustrates the relationship between Vc destruction rate and aw.
Figure 6-30. Relation between water activity and the rate of Vc destruction. O: Orange juice crystal; :
Treatment of food materials with sulfur dioxide reduces the loss of Vc. Besides, sugar
and sugar alcohols protect Vc from oxidative degradation, possibly due to their combination
with ions.
217
Vitamins
Light
Oxidant
Reductant
Heat
Moisture
Acid
Base
VA
+++
+++
++
++
VD
+++
+++
++
++
++
VE
++
++
++
++
VK
+++
++
+++
VC
+++
++
++
++
+++
B1
++
++
++
+++
B2
+++
++
+++
B5
++
B6
++
++
++
B12
++
+++
++
++
+++
+++
Folic
acid
Biotin
++
+++
+++
++
++
++
++
218
Color
Average weight of a
single fruit/g
33.4
green
10.7
3
4
5
6
7
57.2
102.5
145.7
159.9
167.6
green
green-yellow
red-yellow
red
red
7.6
10.9
20.7
14.6
10.1
These enzymes might change the chemical structure and activity of vitamins. For
example, dephosphorylation of VB6, thiamine or riboflavin significantly affects the activities
of the vitamins
The most important factors that affect vitamin stability during storage and processing are
temperature and time, because the activities of enzymes are directly relevant to temperature
and reaction time. For example vitamin C oxidase specifically catalyzes the oxidation of
vitamin C; the loss of beta carotenes in dehydrated food is 15% after storage for 10 days and
the value reaches up to 98% after storage for 60 days.
Foods undergo multiple reactions during storage and processing and these reactions
significantly affect the sensory properties and vitamin contents of the foods. For example,
lipid oxidation produces hydrogen peroxide and epoxide, which initiate the oxidation of
carotenoid, tocopherol, and vitamin C; furthermore, hydrogen peroxide is decomposed to
carbonyl compounds, which can react with thiamine, vitamin B, and pantothenic acid and
lead to loss. In addition, carbonyl compounds generated in non-enzymatic browning of
carbohydrates also partially contribute to the loss of some vitamins. The stability of vitamins
is storage method dependent (Table 6-14).
219
Vitamins
Table 6-14. Losses of vitamins in different storage technologies [18]
Methods
Frozen
storage
Storage after
sterilization
Number of
vegetable
speciess
10(2)
7(3)
Vitamin A
Vitamin B1
Vitamin C
12(4)
20
24
24
26
0-50
10
0-32
0-61
67
56-83
0-45
42
14-50
0-56
49
31-65
0-78
51
28-67
Note: (1) All vegetables were heated and dehydrated before storage.
(2)
Vegetables including asparagus, lima bean, kidney bean, brocoli, cauliflower, green pea, potato,
spinage, cabbage and tender corn.
(3)
Vegetables treated with hot water including asparagus, lima bean, kidney bean, green pea, potato,
spinage, and tender corn; (4) Average value.
Figure 6-31. Relationship between vitamins retention ratio and wheat flour yield [20].
Boiling
60%
88%
78%
77%
66%
Steam
89%
90%
93%
97%
93%
220
REFERENCES
[1]
[2]
[3]
[4]
[5]
[6]
[7]
[8]
[9]
[10]
[11]
[12]
[13]
[14]
Chandler, LA; Schwartz, SJ. HPLC separation of cis-trans carotene isomers in fresh
and processed fruits and vegetables. Food Science, 1987, 52, 669-672.
Pesck, CA; Warthesen, JJ. Kinetic model for photoisomerization and concomitant
photo-degradation of -carotenes. Journal of Agricultural and Food Chemistry, 1990,
38, 1313-1315.
Dellamonica, ES; McDowell, PE. Comparison of beta-carotene content of dried carrots
prepared by three dehydrated process. Food Technology, 1965, 19, 1597-1599.
Van Niekerk, PJ. Determination of vitamins, in HPLC in Food Analysis. 2nd ed. San
Diego: Academic Press, 1988.
Thompson, JN; Hatina, G. Determination of tocopherols and tocotrienols in foods and
tissues by high performance liquid chromatography. Journal of Liquid
Chromatography, 1979, 2, 327-344.
Herbert, V. Present Knowledge in Nutrition. 6th edition. Washington DC: International
Life Science Institute Nutrition Foundation, 1988.
Machlin, LJ. Vitamin E in commercial processing on nutrients. In Machlin LM.
Handbook of Vitamins. 2nd ed. New York: Marcel Dekker, 1991
Cort, WM; Borenstein, JH. Nutrient stability of fortified cereal products. Food
Technololgy, 1976, 30, 52-62.
Dennison, DJ; Kirk, J. Storage stability of thiamin and riboflavin in a dehydrated food
system. Journal of Food Processing and Preservation, 1977, 1, 43-54.
Freed, MS; Brenner, S; Wodicka, VO. Prediction of thiamin and ascorbic acid stability
in canned stored foods. Food Technology, 1949, 3, 148-151.
Emilia, L; Jana, K. Vitamin losses: Retention during heat treatment and continual
changes expressed by mathematical models. Journal of Food Composition and
Analysis, 2006, 19, 252276.
Woodcock, EA; Warthesen, JJ. Riboflavin photochemical degradation in pasta
measured by high performance liquid chromatography. Food Science, 1982, 47, 545555.
Weisinger, H; Hinz, HJ. Kinetic and thermodynamic parameters for Schiff base
formation of vitamin B6 derivatives with amino acids. Archives of Biochemistry and
Biophysics, 1984, 235, 34-40.
Bonjour, JP. Biotin. In: Machlin LJ, ed. Handbook of Vitamins. 2nd edition: New York:
Marcel Dekker, 1991.
Vitamins
221
[15] Flavia. NI. Lipoic acid: a unique antioxidant in the detoxification of activated oxygen
species. Plant Physiology and Biochemistry, 2002, 40, 463470.
[16] Tannenbaum, S. Ascorbic acid. In: Fennema, O. (Ed.), Principles of Food Science Part
I Food Chemistry. Marcel Dekker, New York, 1976, 477544.
[17] Plank, R. Handbuch der Kltetechnik. Bd. XIV. Berlin: Springer-Verlag, 1966.
[18] Maleski, W; Markakis, P. A research note. Ascorbic acid content of developing tomato
fruit. Journal of Food Science, 1971, 36, 537-539.
[19] Lund, D. Nutritional Evaluation of Food Processing. 3rd editon. New York: Van
Nostrand Reihhold, 1988.
[20] Moran, R. Biotin. Present Knowledge in Nutrition. International chemical form.
Nutrition, 1959, 122, 533-545.
[21] Zhao, H. The loss of vitamin in the process of cooking and food processing. Foreign
medical and hygiene anthology, 2003, 30, 221.
ISBN: 978-1-61942-125-7
2012 Nova Science Publishers, Inc.
Chapter 7
MINERALS
Dongfeng Wang1, Lina Yu2, Haiyan Li1, Bin Zhang1,
Shuhui Wang3 and Xingguo Liang1
1
ABSTRACT
Among the 92 natural chemical elements identified to present, 81 of them have been
found in human body and 25 elements are found to be essential to life, which are termed
essential minerals. Essential minerals are widely involved in metabolisms in human body
as cofactors or activators of enzymes and some play important role in maintaining
osmotic pressure and cell membrane integrity. Besides, some minerals are important
constituents of human tissues, such as calcium and phosphorus in bone and teeth. This
chapter concerns the classification, distribution, property, and function of minerals and
their occurrence in foods. Besides, the changes of minerals in foods during harvesting,
processing, and storage are also highlighted in this chapter.
1. INTRODUCTION
1.1. Definition and Classification
To present, 115 chemical elements have been discovered, including 23 artificial and 92
natural ones. Of the 115 elements, 81 have been discovered in human bodies. According to
their importance to human body, elements are divided into 3 classes:
Essential elements
Essential elements support the normal biochemical processes of human body. Deficiency
of elements of this class leads to impaired functions of human body and the functions can be
224
restored in the early stage of the deficiency if the elements are supplemented in time.
Essential elements have special physiologic functions and cannot be replaced by other
minerals. To present, 29 elements have been found essential for the human body, including
oxygen (O), carbon (C), hydrogen (H), nitrogen (N), calcium (Ca), phosphorus (P), potassium
(K), sodium (Na), chlorine (Cl), sulfur (S), magnesium (Mg), ferrum (Fe), fluorine (F), zinc
(Zn), cuprum (Cu), vanadium (V), stannum (Sn), selenium (Se), manganese (Mn), iodine (I),
nickel (Ni), molybdenum (Mo), chromium (Cr), cobalt (Co), bromine (Br), arsenic (As),
silicon (Si), boron (B), and strontium (Sr). The former 11 elements account for up to 99.95%
of the total amount of the 29 elements in human body and are termed main or macro
elements. The remaining 18 elements are trace elements and account for only 0.05% of the
total amount.
Potential beneficial elements or supplementary elements
Elements of this class are beneficial to the physiological activities of human body when
their contents are in normal levels. However, the elements are toxic when they are present in
high levels. Rubidium (Rb), aluminum (Al), niobium (Nb), zirconium (Zr), lithium (Li), and
some rare earth elements (REEs) belong to this class.
Toxic elements
Toxic elements are also referred to as contamination elements or toxic trace elements.
These elements exert their toxicity even in very low concentrations. Bismuth (Bi), stibium
(Sb), beryllium (Be), cadmium (Cd), mercury (Hg), plumbum (Pb), and thallium (Tl) are
important toxic elements.
The elements except C, H, O, and N are termed minerals. Based on the contents in foods,
minerals are divided into main minerals, trace minerals, and ultra-trace minerals. Main
minerals include Na, K, Ca, P, Mg, S, and Cl; trace minerals include Fe, F, I, Zn, Se, Cu, Mn,
Cr, Mo, Co, and Ni; and ultra-trace minerals include Al, As, Ba, Bi, B, Br, Cd, Cs, Ge, Hg,
Li, Pb, Rb, Sb, Si, Sn, Sm, Ti, Sr, Tl, W, and V.
Minerals
225
The distribution of minerals in the environment and human body is displayed in Figure 72. Living organisms have evolved regulatory measures to maintain essential mineral contents
in normal ranges. That is to say, a living organism can maintain a mineral in a constant range
when the element intake is insufficient or excessive.
Figure 7-1. Distribution of macro and trace elements in the element periodic table [8].
Figure7-2. Distribution of elements in the seawater (upper), human body (middle) and crust (lower).
(Data in graph are log c; the unit of c is mg/kg) [5].
Functions
Growth promotion and essential for plant growth
Closely correlated with bone growth
Component of hemoglobin, myoglobin and cytochrome
Involvement in enzyme activity, nucleic acid structure and protein synthesis
Component of thyroxine
Cofactor of many metalloenzymes
Component of glutathione peroxidase and participation in liver function and
muscle metabolism
Activation of enzyme and participation in hematopoiesis
Component of molybdoenzymes
226
Mineral
Cr
Mg
Si
P
Co
Ca
S
K
Na
Cl
Functions
Effect of insulin intensive and glucose utilization promotion
Activation of enzyme and component of bone
Participation in skeletogeny
Component of ATP
Component of VB12
Component of bone and involvement in neural transmission
Component of proteins
Electrochemical and messenger function and extracellular cations
Electrochemical and messenger function and extracellular cations
Electrochemical and messenger function and extracellular anions
227
Minerals
metabolic antagonist of Cd, competing with Cd for the thiol of metallothionein. Pb is more
poisonous in the absence of Fe and Cr in the diet; Se can complex with Hg and reduce Hg
toxicity. The valence significantly influences the toxicity of metals. As3+ is much more toxic
than As5+; methyl arsenic acid and dimethyl arsenic acid are moderately toxic, while
arsenobetaine and arsenocholine are almost non-toxic. Cr3+ is an essential trace element,
while Cr6+ is toxic and Cr2O72- is a strong carcinogen.
Hence, in evaluating the bioavailability and safety of a mineral in foods, its existence
state must be taken into consideration. Generally, only very few minerals are present as free
ions in foods.
O
C
H
N
H2 C
CH2
Zn
N
H
C
O
Note: Left: Zn(Gly)22H2O, Midmost Glycine tripeptide mineral complex, M = Cu (II) or Ni (II); Right:
Glycine tetrapeptide cupric complex.
Figure 7-3. Structures of mineral-peptide complexes.
228
for Cu(II) and other divalent minerals and the -OH group plays less role in coordination with
Cu(II). The OH group on 1-C of GlcNH2GalNH2 is the main coordination group for divalent
minerals, but if the -OH on 1-C is not available due to steric hindrance, such as that in
aminosaccharide derivatives, other OH groups participate in the coordination. Nagy L et al.
[6] studied the structural parameters of carbohydrate-mineral complexes by EXAFS
(extended X-ray absorption fine structure spectroscopic) and the results are given in Table 72. It could be seen that minerals in foods can form various complexes with carbohydrates and
their derivatives.
Table 7-2. Structural parameters of carbohydrate-mineral complexes
Ligands
Fru
Rib
GlcNH2
Adenosine
Uridine
HyA
N-D-glugly
N-D-glugly
N-D-glugly
PHTAc
PHTAc
Binding Interaction
Fe-O
FeC
FeFe
Cu-O(eq)
Cu-O(ax)
CuC
Cu-O(eq)
Cu-O(eq)
Cu-O(ax)
CuC
Cu-O(eq)
Cu-O(ax)
CuC
Cu-O(eq)
Cu-O(ax)
CuC
Cu-O(eq)
Cu-O(ax)
CuC
Zn-O
ZnC
Cu-O(eq)
Cu-N(eq)
Cu-O(ax)
CuC
CuCu
Ni-O,N
NiC
Co-O,N
CoC
CoCo
Zn-O,N
ZnC
ZnO,C,S
Mn-O,N
MnC
MnO,C,S
N
6
4
1
4
2
2
3
1
2
2
4
2
2
4
2
2
4
2
2
4
2
2
2
2
4
1
6
6
6
6
1
4
6
6
6
6
8
/pm
195
277
310
191
230
271
193
193
234
274
191
232
275
192
234
279
191
234
313
202
299
190
190
215
270
297
204
285
200
290
303
205
290
286
216
305
375
/pm
9.8
7.9
7.0
7.5
13.0
10.0
7.7
7.7
13.0
10.0
5.4
7.8
8.4
7.9
7.9
9.6
8.2
3.2
13.0
8.1
13.2
5.6
5.6
2.5
2.8
11.4
7.6
5.4
11.9
11.7
7.6
8.0
10.0
14.0
9.5
11.0
18.0
229
Minerals
Ligands
PHTAc
PHTAc
LacA
Mal
GlcA
Sacc
Mal
GlcA
Binding Interaction
Ag-N
Ag-S
AgC
Ni-O,N
NiC
NiO,C,S
Mn(IV)-O
Mn(IV)-O
Mn(IV)-O
Mn(III)-O
Mn(III)-O
Mn(III)-O
N
1
1
4
6
6
8
6
6
6
6
6
6
/pm
203
230
294
203
284
390
208
208
209
209
206
208
/pm
5.0
4.6
19.0
8.0
9.5
15.0
2.3
3.5
1.9
3.6
1.0
3.3
Note: N, coordination number; , atomic distance; , Debye-Waller factor; Fru, D- Fructose; Rib, DRhamnose; GlcNH2, 2-amino-2-deoxy-D-Glucose; HyA, Hyaluronic Acid; N-D-glugly(N-Dgluconylglycine, a pseudopeptide derivative glucono-delta-lactone and glycine); PHTAc, [2(polyhydroxyalkyl)thiazolidine-4-carboxylic acid]; LacA, D-lactobionic acid; Mal, maltitol 4-O-D-glucopyranosyl-D-glucitol; GlcA, D- Gluconate; Sacc, D- Sucrose; Ara, L- or D- Arabinose.
230
macrochelated outer sphere (Figure 7-5B) respectively. In the former structure, N-7 of
adenine directly binds to the mineral, but the -phosphate group coordinates through H2O. In
the later structure, N-7 of adenine coordinates with mineral through H2O, whereas the , , phosphate groups directly link with the mineral (Figure 7-5).
Table 7-3. Content of phosphorus coordinated with phytic acid in
plant food
Food
Oat
Wheat
Barley
Rye
Rice
Corn
Peanut
a)
Food
Potato
Kidney Bean
Carrot
Orange
Lemon
Walnut
Soybean
Minerals
231
b)
Figure 7-5. Two simplified structural models of (ATP) 2-Chelate inner ring (A) and external ring (B)
coordination sphere (M indicates a mineral ion) [7].
b)
Figure 7-6. Structure of porphine. In (a) and (b), the structure is numbered in
different ways.
232
Substituents
1
2
3
4
5
6
7
Protoporphyrin IX
M
V
M
V
M
P
P
Mesoporphyrin IX
M
E
M
E
M
P
P
Deuteroporphyrin IX
M
H
M
H
M
P
M
Hematoporphyrin IX
M
B
M
B
M
P
P
Spirograhic porphyrin IX
M
F
M
V
M
P
P
Corproporphyrin III
M
P
M
P
M
P
P
Aetioporphyrin III
M
E
M
E
M
E
E
Uroporphyrin III
A
P
A
P
A
P
P
Note: A=-CH2COOH, B=-CH (OH) CH3, E=-C2H5, F=-CHO, M=-CH3, H=-H, P=-CH2CH2COOH, V=CH=CH2.
Porphyrins can form complexes with Fe2+, Fe3+, Zn2+, Co2+, Cu2+, Mg2+ and other mineral
ions, such as Fe in hemoglobin and Mn in chlorophyll.
Heme (Figure 7-7) consists of an iron atom and a planar porphyrin ring. The iron in the
center is connected with the N-atoms of four pyrrole rings through coordination bonds, and
the fifth coordination point is provided by a histidine residue in globin, and the remaining
sixth coordination point comes from negatively charged atoms in other ligands, such as H2O.
Heme can connect with globin to form myoglobin (Figure 7-8).
Three types of hemes, namely heme a, heme b and heme c, have been found. Heme a is
the prosthetic group of cytochrome c oxidase; heme b is an iron-protoporphyrin IX complex
(Table 7-4) and it is the prosthetic group of hemoglobin, myoglobin, cytochrome b,
cytochrome p-450, catalase and peroxidase; heme c is the prosthetic group of cytochrome c.
Chlorophyll is a green pigment in the higher plants and photosynthetic organisms. It has a
planar molecule and consists of four pyrrole rings connected through the methylene bridge.
The Mg in center is connected with the N-atoms of four pyrrole rings through coordination
bonds (Figure 7-9). Many chlorophyll species have been identified, such as chlorophyll a, b, c
and d, as well as bacteria chlorophyll and chlorobium chlorophyll. Chlorophyll a and b occur
widely in plant-derived foods in the ratio 3:1. Chlorophyll is transformed to pheophytin
during food processing. In acidic conditions, the Mg atom in chlorophyll is replaced by
Minerals
233
hydrogen atoms and the resultant pheophytin is dark olive-brown. Heating accelerates the
transformation. In addition to hydrogen, Mg can also be replaced by other divalent minerals,
such as zinc and copper.
Vitamin B12 consists of a corrin ring and has four pyrrole subunits. Because cobalt is
essential for its bioactivity, Vitamin B12 is also known as cobalamin. Vitamin B12 is a red
crystal and its systematic name is -(5,6-dimethylbenzimidazolyl)cobamidcyanide. In the
structure, the cobalt atom combines with four inner nitrogen atoms in the corrin ring. If the
sixth coordination site is replaced by cyanide, VB12 is transformed to cyanocobalamin; if the
cyanogroup connected with cobalt is replaced by the hydroxyl group, VB12 is converted to
hydroxocobalamin, which is the ubiquitous form of VB12 in nature. If the cyano group is
replaced by the nitroso group, nitriocobalamin is generated. Nitriocobalamin is found mainly
in some bacteria. The structure of Vitamin B12 is given in Figure 7-10.
234
acidic amino acids, the amino group in basic amino acids, the imidazolyl group in histidine,
the sulfhydryl group in cysteine, and the thioether group in methionine, can coordinate with
minerals. However, only the groups in suitable sites can form complexes with minerals.
Figure 7-11 is the schematic diagram of carboxypeptidase A. Zn2+ coordinates with the
protein constituent through two imidazole groups and a carboxyl group in the protein.
Metals are involved in the activity of a large number of enzymes and such enzymes are
known as metalloenzymes. Zn, Fe, Cu, Mn, Mg, Mo, Co, K, and Ba are the most important
cofactors for such enzymes.
Living organisms synthesize a large variety of proteins for the storage and transport of
minerals.
Minerals
235
Ferritin
Ferritin is mainly distributed in the spleen, liver and bone marrow of animals, as well as
in plants chloroplasts and certain fungi. Its main physiological function is to store unused or
excessively absorbed iron.
Transferrin
Transferrin is mainly distributed in body fluids and cells of vertebrates. A large variety of
transferrins have been identified, such as serotransferrin in serum and lactotransferrin in milk
and lacrimal gland secretion. Serotransferrin is a class of mineral-binding glycoproteins with
molecular weight about 7.7~7.4 104. After the transferrin releases all Fe3+ irons, the protein
constituent can combine with other divalent or trivalent ions other than iron, such as Cu2+,
Zn2+, Cr3+, Mn3+, Co3+, and Ga3+.
Iron-sulphur protein
Iron-sulphur proteins are characterized by the presence of the Fe-S chromophore and
their molecular weight is about 10 kD. All the Fe atoms in the proteins have variable valence.
The proteins participate in redox reactions in organism as the electron transfer group and are
involved in biological oxidation, nitrogen fixation and photosynthesis.
Cuprein
Cupreins are copper-containing proteins and superoxide dismutase is a typical example of
such proteins. To present, more than forty kinds of cupreins have been found. Cupreins with
blue color are called blue copper proteins and those without the blue color are called nonceruloplasmins.
Minerallothionein
Metallothionein (MT) was firstly separated from horse kidney in 1957. Later, it was
found that MT is widespread in nearly all organisms. MTs are a category of induced protein
with a molecular weight about 6~10 kD. MTs are characterized by their high Cys contents,
reaching up to 25~35%. The functions of MTs include anti-oxidation, free radicals
scavenging, heavy metal complexing, and mineral storage. The structures of MTs are highly
conserved. Many minerals, such as Cd, Pb and Zn, can induce the synthesis of MTs.
One of the most important functions of MTs is to the alleviate toxicity of heavy metals.
The affinity of MTs to some heavy metals follow the order Cd2+ > Pb2+ > Zn2+. Because the
MT level is positively correlated with contaminant level, it is widely used as an indicator of
environmental pollution.
Capasso, C. et al [1] determined the three-dimensional structure of MT-nc obtained from
the Antarctic fish (Notothenia coriiceps). NMR analysis showed that MT-nc is composed of
the - and - domains. The -domain in the C-terminal consists of eleven Cys residues and
four mineral atoms, and the -domain in the N-terminal has nine Cys residues and three
mineral atoms (Figure 7-12).
The ninth cystine of MT-nc in the domain is different from that of mammals.
236
The terminal amino acid sequence of mammal-derived MTs is CXCC (C denotes Cys, X
denotes any amino acid), while the sequence of fish MT is CXXXCC. This difference
attributes to the different structures of their domains.
Except few exceptions, the N-terminals of mammal-derived MTs are acetyl Met, and the
carboxyl-terminals are Ala. Each MT molecule contains 20 Cys residues and the Cys residues
are in the same positions. The Cys residues can form five Cys-X-Cys units, one Cys-Cys-XCys-Cys unit and one Cys-X-Cys-Cys unit.
Although the amino acid compositions of MTs in different animal are quite similar, the
MTs differ in the metal binding capacity. Generally, each MT molecule can bind seven
mineral ions and the affinities of some metals to MTs follow the increasing order Zn2+ < Pb2+
< Cd2+ < Cu2+ < Ag+ < Hg+.
a)
b)
a
b
Phytochelatins
Phytochelatins are firstly found in plants and have similar metal binding capabilities as
MTs. It is estimated that more than 90% of Cd2+ in plant cells are bound with phytochelatins.
The general formula of phytochelatins is (-Glu-Cys)n-Gly. Phytochelatins are major
heavy metal binding peptides in plants and some yeast species. The biosynthesis of
phytochelatins is induced rapidly after exposure to heavy metals, especially Cd2+ and Hg2+.
Heavy metals in living organism are present in both the soluble and insoluble forms, in
which, soluble heavy metals bind mainly to phytochelatins. Phytochelatins from different
crops have the following common characteristics: (1) the molecules have similar structure, as
237
Minerals
shown in Figure 7-14; (2) the Glu residue locates in the N-terminal; (3) the amino acid
connected with Glu--oxo is Cys; (4) the -Glu-Cys unit occurs repeatedly in the structure.
Ca
Ca
Ca
Ca
238
Minerals
239
Figure 7-18. Schematic relationship between biological activity and relative concentration of minerals.
240
derived foods contain high contents of phosphates, oxalic acid and tannic acids and these
compounds can precipitate Fe by complexing with it, which further reduces Fe utilization.
The presence of reducing agents in plant-derived foods improves Fe utilization. Generally, the
bioavailability of Fe in animal-derived foods is higher than that in plant-derived foods, as
shown in Figure 7-19.
The utilization of Fe is associated with its sources, existence state and diet structure. For
example, phosphoric acid in milk can precipitate Fe and reduces its utilization; polyphenols in
tea can complex with Fe and affect its utilization; diet with insufficient Cu decreases Fe
absorption, because Cu is essential for hemoglobin synthesis.
The absorption of Fe is also affected by individual or physiological factors. People
suffering Fe deficiency or anemia absorb Fe easily and women generally have a better
absorption than men. Besides, the possibility of Fe deficiency decreases with age increase.
3.2.2. Toxicity
All minerals are toxic when they are present in high levels in foods. In addition to
contents, the toxicity of minerals is also affected by the following factors.
Figure 7-19. Utilization of Fe element in different sources. 1 to 12 represents rice, spinach, beans, corn,
lettuce, wheat, soybean, iron, protein, bovine, fish, hemoglobin, and beef, respectively.
Minerals
241
methyl arsenate 700~2600, arsenocholine 6500 and betaine arsenate complex >10,000. It
could be seen that volatile inorganic arsenic is the most toxic. Arsenocholine and betaine
arsenate are often considered non-toxic.
Poisoning mechanism of heavy metals
The poisoning mechanisms of heavy metals are rather complex and affected not only by
their contents in the body, but also by the exposing pathway, metabolism, and health
conditions of ingesters. In general, heavy metals exert their toxicity in one or more of the
following mechanisms:
Heavy metals disrupt the functional groups in biomolecules. For example, Hg(II)
and Ag(II) can bind with SH of Cys residues in enzymes and block the
participation of SH in enzymatic reactions.
Heavy metals replace the essential metals in biomolecules. The activity of many
enzymes is closely related to the metal cofactors. The activity of metalloenzymes is
easily destroyed by the replacement of metal factors. For example, Be(II) can
replace the Mg(II) in Mg(II)-containing enzymes.
Heavy metals change the conformation of biomolecules. Heavy metals can bind to
various biomolecules, such as proteins, nucleic acids and change their
conformations. For example, Pb2+, Cd2+ and Ni2+ can bind to double stranded DNA
(dsDNA) and this interaction leads to different modifications in the dsDNA
structure.
242
Hg, Pb and Cd are well-known toxic metals, but the intake of certain components may
strengthen or weaken their toxicity. For example, lipopolysaccharides increase the
accumulation of Hg in mice and augment the Hg-induced nephrotoxicity.
Table 7-5. Minerals contents in some foods [2, 9]
Food
Fried eggs
Wheat bread
Graham bread
Salt-free macaroni
Cooked rice
Instant rice
Mature black soybean
Red cashew
Whole milk
Skim milk /nonfat milk
Ameican cheese
Sayda cheese
Farmhouse cheese
Low fat yogurt
Vanilla ice-cream
Overbark baked potato
Underbark boiling otato
Palm cabbage, crude stem
Palm cabbage, cooked stem
Crude shattering carrot
Cooked freezing carrot
Fresh entire tomato
Canned tomato juice
Attains (defrosting)
Attains
Apple (skin)
Banana (peeling)
Roasted beef (cans)
Roasted veal (cans)
Roasted chicken breast
Roasted chicken drumstick
Cooked salmon
Canned salmon with bone
Ca
57
35
20
5
10
10
24
25
291
302
261
305
63
415
88
20
10
216
249
15
21
6
17
17
52
10
7
5
6
13
10
6
203
Mg
13
6
26
13
42
42
61
40
33
28
10
12
6
10
9
55
26
114
130
8
7
14
20
18
13
6
32
21
28
25
20
26
25
P
269
30
74
38
81
81
120
126
228
247
316
219
139
326
67
115
54
297
318
24
19
30
35
30
18
10
22
176
234
194
156
234
277
Content / mg/100g
Na
K
Fe
290 138
2.1
144 31
0.8
180 50
1.5
1
22
1.0
5
42
0.4
5
42
0.4
1
305
2.0
2
356
3.0
120 370
0.1
126 406
0.1
608 69
0.2
264 42
0.3
425 89
0.1
150 531
0.2
58
128
0.1
16
844
2.8
7
443
0.4
123 1470 4.0
141 1575 4.5
19
178
0.3
43
115
0.4
11
273
0.6
661 403
1.0
2
356
0.2
0
237
0.1
1
159
0.3
1
451
0.4
50
305
1.6
68
389
0.9
62
218
0.9
77
206
1.1
56
319
0.5
458 231
0.9
Zn
2.0
0.2
1.0
0.4
0.6
0.6
1.0
0.9
0.9
0.9
1.3
1.3
0.4
2.0
0.7
0.7
0.4
2.0
2.1
0.1
0.2
0.1
0.3
0.1
0.1
0.1
0.2
3.7
3.0
0.8
2.4
0.4
0.9
Cu
0.06
0.04
0.10
0.07
0.01
0.01
0.18
0.21
0.05
0.05
0.01
0.01
0.03
0.10
0.01
0.62
0.23
0.40
0.23
0.03
0.05
0.09
0.18
0.08
0.06
0.06
0.12
0.08
0.13
0.04
0.07
0.06
0.07
Se
8
8
16
19.0
13.0
13.0
7.9
1.9
3.0
7.6
3.8
7.0
7.3
5.5
4.7
1.8
1.2
0.9
1.1
0.8
0.9
0.6
0.4
0.4
1.2
0.6
1.1
243
Minerals
Zn
19.48
19.47
17.64
Cu
1.779
2.549
0.702
Fe
17.18
20.13
24.97
Mn
15.46
24.25
25.36
Ca
27.59
59.48
32.00
Mg
12.27
12.00
11.42
244
Table 7-7. Effect of trace element supplementation in cattle feed on the minerals content
of milk (mg/100g)
Fe
Cu
Zn
Mn
K
Na
Ca
Mg P
0.122 0.032 0.417 0.008 81.60 83.70 144.0 11.00 98.60
0.137 0.007 0.442 0.010 68.39 85.34 77.67 10.06 82.09
Experimental group
Control group
Table 7-8. Effect of different processing methods on some trace elements content in
instant fiddlehead (mg/100g dry weight)
Processing methods
Ca
Mg
Fe
Mn
Cu
Zn
Before processing
62.5
238.0
32.0
8.1
27.4
9.5
(1)
80.0
140.9
30.6
7.3
22.4
7.1
(2)
80.1
169.5
21.1
7.3
20.3
7.0
(3)
80.6
127.0
27.6
5.1
20.2
5.7
(4)
88.0
157.3
20.7
7.7
15.5
7.9
Note: (1) natural dehydration plus blanching; (2) natural dehydration without blanching; (3) salting-out
dehydration plus blanching; (4) salting-out dehydration without blanching.
g/100g
Loss (%)
Steam blanching
7.9
3.0
56
Na
0.5
0.3
43
Ca
Mg
P
Nitrite
2.2
0.3
0.6
2.5
2.3
0.2
0.4
0.8
0
36
36
70
Cu
Material
0.21
Water boiling
0.10
Fluctuati
on (%)
0.00
-52.38
Baking
Potato chip
0.18
0.29
-14.29
+37.20
Processing method
Cu
Potato mesh
0.10
0.27
Fluctuati
on (%)
-52.38
+28.57
Fast potato
Peeling potato
0.17
0.34
-19.05
+61.90
The effect of processing method on Cu content in potato shown in Table 7-10. Cu content
is slightly increased in the frying potato crisp and peeling potato.
245
Minerals
Can
La
State
Al
Sn
L
0.10
5
S
0.7
10
Bean
La
L
0.07
5
S
0.15
10
Small green pea
La
L
0.04
10
S
0.55
20
Parsley heart
La
L
0.13
10
S
1.50
20
Sweetcorn
La
L
0.04
10
S
0.30
20
Mushroom
P
L
0.01
15
S
0.04
55
Note: a. La = Lacquered can; P = T in plate can; b. L = Liquid, S = Solid.
Fe
2.8
4.8
9.8
26
10
12
4.0
3.4
1.0
7.4
5.1
16
REFERENCES
[1] Capasso, C; Carginale, V. Solution structure of MT-nc, a Novel Metallothionein from
the Antarctic Fish Notothenia coriiceps. Structure, 2003, 11, 435-443.
[2] ESHA Research. The Food Processor Plus, ESHA Research, Salem, OR, 1992.
[3] Ji, L; Huang, J; Mo, T. Bioinorganic Chemistry an Introduction (Second), Guangdong:
Zhongshan University Press, 2001
[4] Kan, JQ. Food Chemistry. Beijing: China Agricultural University Press; 2008.
[5] Liu, Y. An idea on trace elements as nutrients of organism. Journal of Peking University
(Natural Science), 1986, (3): 121.
[6] Nagy, L; Szorcsik, A. Equilibrium and structural studies on metal complexes of
carbohydrates and their derivatives. Journal of Inorganic Biochemistry, 2002, 89, 1-12.
[7] Sigel, H; Sigel, A. Metal Ions in Biological Systems. 1st edition. New York: Marcel
Dekker, 1995.
[8] Tang Renhuan. On the Biological Element Spectrum in Organism. Acta Scientiarum
Naturalium Universitatis Pekinensis, 1996, 32, 790-803.
[9] U. S. Department of Agriculture (1976-1986). Composition of Foods. Agriculture
Handbook Nos.8-1 to 8-16. Human Nutrition Information Service, USDA, Hyattsville,
MD.
[10] Yang, P. Introduction of Bioinorganic Chemistry, Xian: Xian Jiaotong University
Press, 1991.
ISBN: 978-1-61942-125-7
2012 Nova Science Publishers, Inc.
Chapter 8
FOOD FLAVORS
Xiaoxiong Zeng1 and Guaoqing Huang2
1
ABSTRACT
The special tastes or aromas of foods are contributed by abundant small-molecular
weight compounds and these compounds significantly affect the acceptability of foods by
consumers. This chapter firstly concerns the major tastes and their perception by human
beings. Then, the major flavor compounds in various foods, including fruits, vegetables,
and meats are elucidated in detail. Besides, reactions that contribute to the formation of
flavors during food processing and storage are also presented in detail in this chapter.
Foods should not only meet the needs of consumers on nutrition, but also provide
desirable flavors so that consumers can enjoy the foods. Flavor is an important aspect that
determines food quality, and affects the intake and absorption of nutrients in foods.
Flavor is an overall integrated perception of all contributing senses (smell, taste, sight,
feeling, and sound) at the time of food consumption. The evaluation and preference to
flavors differ significantly among individuals, areas, and ethnics. Flavor together with
nutritional value and security determine consumers acceptance of foods.
The flavor of food is contributed by multiple compounds in addition to
environmental factors. The development of modern analysis techniques, such as
chromatography and mass spectrometry, provides great convenience for further study of
food flavor. However, since food flavor is a physiological perception, neither qualitative
nor quantitative methods can accurately measure or describe a food flavor yet.
248
249
Food Flavors
Factors affecting taste perception.
The perception of tastes is affected by many factors. In addition to dietary habits, health
status, age and other individual factors, taste perception is also affected by the following:
Temperature: the optimum temperature for taste sensation is between 10-40 C and taste
receptors are the most sensitive at 30 C. When the temperature is lower than 10 C or higher
than 50 C, the sensation becomes dull. It can be seen from Table 8-1 that the salty taste is the
most sensitive to temperature variation and the sour taste of citric acid is the least sensitive.
Solubility: the intensity of a taste is related to the solubility of the taste compound,
because taste receptors or free nerve endings are stimulated only by dissolved compounds.
Table 8-1. Threshold values of several taste compounds
Taste compounds
Taste
Quinine sulfate
Sucrose
Sodium chloride
Citrate
Bitter
Sweet
Salty
Sour
Threshold (%)
25 C
0 C
1.010-4
3.010-4
0.1
0.4
0.05
0.25
2.510-3
3.010-3
Generally, taste compounds that dissolve quickly are perceived in a very short time and
the sensation disappears very fast. For example, sucrose is readily soluble. Its sweetness is
perceived rapidly after ingestion, but the sensation lasts only a short time. In contrast, the
sweetness of saccharin is perceived slowly, but the sensation can last for a relative long time.
Presence of other taste compounds: Interactions might occur between different taste
compounds.
a.
Enhancing: the presence of a taste compound could enhance the intensity of another
taste. For example, table salt in concentration 0.017% enhances the sweetness of
sucrose solution (15 %).
b. Modification: the presence of a taste compound might change the taste of another
compound. For example, water tastes sweet if table salt or quinine has been
perceived before.
c. Elimination: the presence of a taste compound reduces or eliminates the intensity of
another taste. For example, any one of sucrose, citric acid, table salt, and quinine can
reduce the taste intensity of the other three compounds. In wines or beverages, the
sweetness of sugars weakens the sour taste and vice versa.
d. Multiplication: when two taste compounds are present at the same time, the intensity
of the tastes increases significantly. For example, the mixture of sodium glutamate
and 5-inosinic acid has markedly improved delicious taste than alone and maltol
significantly enhances the sweet taste in beverages and candies.
e. Adaptation: adaptation refers to the gradual decline of taste intensity with prolonged
stimulation. The time required for the recovery of taste sensation varies with tastes.
The time needed for recovery of sour taste sensation after adaptation is 1.5~3 min
and that for sweetness, bitterness, and salty is 1~5 min, 1.5~2.5 min and 0.3-2 min
respectively.
250
The interactions between tastes are very complicated and are affected by both
psychological and physicochemical factors. The mechanisms involved are not well
understood yet to present.
Sweet Taste
Sweetness is the most popular taste for consumers. It improves the palatability and
certain properties of foods. The intensity of sweetness is expressed in relative sweetness by
using 10 % sucrose solution as reference. Table 8-2 lists the relative sweetness of several
sweeteners.
The mechanism of sweet taste can be explained by the AH/B through proposed by Robert
Shallenberger and Terry Acree in 1963. It is supposed that the initial event in the perception
of sweetness is the hydrogen bonding of a stimulant to receptors on the tongue. Each sweet
compound possesses an electronegative atom A (usually N or O) covalently connected with a
hydrogen atom (AH). Hence, the AH can be hydroxyl (-OH), imino (-NH) or amino (-NH2)
group. AH functions as the proton donor. The sweet compound contains another
electronegative atom B (usually N, O, S, or Cl), which is 0.25-0.4 nm away from the AH
group and acts as the proton receptor. The sweetness receptor contains the AH/B unit. When
the AH/B unit of a sweet compound binds to the AH/B unit in the receptor through hydrogen
bonding, the taste nerve is stimulated and the sweet taste is perceived. Figure 8-1 shows the
AH/B structure of chloroform, saccharin and glucose.
This theory has been successfully used to explain the sweet sensation of many
compounds. However, this theory has some limitations. It can not explain why the sweet
intensities of sugars and D-amino acids that contain the AH/B structure differ significantly
and why the optical isomers of amino acids have different tastes.
Table 8-2. Relative sweetness of several sweeteners (with sucrose as 1.0)
-D-fructose
-D-glucose
-D-galactose
-D-mannose
Relative
sweetness
1.0-1.75
0.40-0.79
0.27
0.59
Xylitol
0.9-1.4
Sweetener
Chloroform
Sweetener
Relative sweetness
D-tryptophan
glycyrrhizic acid
saccharin
Naringin dihydrochalcone
35
200-250
200-700
100
Neohesperidin dihydrochalcone
1500-2000
Saccharin
Glucose
Food Flavors
251
Sweet receptor
Figure 8-2. Schematic showing the relationship between AH/B and sites in the saporous sweet unit for
-D-fructopyranose [1].
To solve these problems, Kier extended the AH/B theory. He proposed that each sweet
compound also contains a lipophilic region in addition to the AH/B structure. The lipophilic
region might be methylene (-CH2-), methyl (-CH3) or phenyl (-C6H5) groups. All the three
active units (AH, B and region ) must be arranged correctly in space so that the units can
contact with receptor molecules. The relationship between the three groups can be illustrated
in Figure 8-2.
Bitter Taste
The bitter taste is unpleasant on its own, but its combination with other tastes can provide
foods with special flavor, such as in tea, coffee, beer, and balsam pear. Strychnine is the
bitterest substance (threshold 0.0016 %) ever found and quinine is often used as reference in
the assessment of bitter intensity of other substance.
The sensation of the bitter taste is similar to that of the sweet taste. Bitter compounds
posses the AH/B entity and can interact with receptors through hydrogen bonding. The
difference is that the proton donor (AH) in bitter compounds are OH, C(OH)COCH3,
CHCOOCH3, or NH and the proton donor (B) is CHO, COOH, or COOCH3. In addition,
the distance between AH and B is 0.15 nm, which is much less than that in sweet compounds.
Naturally occurring bitter compounds are alkaloids, terpenoids, and glycosides in plants
and bile in animals.
Caffeine, theobromine, theophylline: caffeine, theobromine and theophylline are
derivatives of purine and are important bitter substances in foods. Caffeine occurs in tea,
coffee and cacao, and theophylline is found in cacao and tea (Figure 8-3). All the three
alkaloids can stimulate the central nervous system.
Naringin and neohesperidin: naringin and neohesperidin are main bitter taste compounds
in citrus fruits and are mainly distributed in the peel of the fruits. Both the two compounds are
flavanone glycosides and are water soluble. The bitterness of naringin is related to the l2
glycosidic bond between rhamnose and glucose. Enzymatic hydrolysis of the linkage yields
products without bitterness (Figure 8-4).
252
R1
R3
R1=R2=R3=CH3
caffeine
R1=H R2=R3=CH3 theobromine
R1=R2= CH3 R3= H theophylline
R2
Enzyme
humulone
cis-isohumulone
trans-isohumulone
R1
cholic acid
R2
Figure 8-6. Structures chenocholic acid, deoxycholic acid and cholic acid.
Bitter substance in beer: the bitter taste of beer is contributed by the bitter substances
originally contained in hops and those generated during brewing. The major bitter substances
in beer are -acids, such as humulone, cohumulone, adhumulone. Hops are often added as the
mashed malted barely (or malt extract) is boiled in water. During this boiling process the
modestly bitter -acids undergo thermal isomerization to form extremely bitter iso--acids.
(Figure 8-5).
Bile acid: bile acid is an extremely bitter fluid secreted by the liver of most vertebrates. It
is involved in the digestion of lipids in the small intestine and the adsorption of fat-soluble
vitamins. The major bitter compounds in bile acid are chenocholic acid, deoxycholic acid, and
cholic acid (Figure 8-6). If bile acid leaks from gallbladder during the processing of livestock,
poultry and aquatic products, the bitter taste cannot be removed even after repeated washing.
Food Flavors
253
Sour Taste
The sour taste is produced by hydrogen ion of organic acid, inorganic acids and acidic
salts. Moderate sour intensity yields pleasant sensation and enhances appetite. Generally, the
intensity of the sour taste is positively related to the concentration of hydrogen ion in
solutions. When the H+ concentration is too high (pH <3.0), the sour taste becomes
intolerable and sour intensity changes can no longer be perceived. The sensation of the sour
taste is affected by counter ion species and the buffering capacity of food medium. For
example, the sour intensities of five common acids in the same pH are in the following
decreasing order: acetate acid > formic acid > lactic acid > oxalate acid > hydrochloride yield.
Anions decide the characteristics of the sour taste, which is why the sour taste of sour
compounds differs.
Acidulants are important additives in food processing. The compounds not only impart
foods with desired sour taste, but also inhibit the growth of microorganisms. The most
commonly used acidulant in food industry is acetic acid, followed by citric acid, lactic acid,
tartaric acid, gluconic acid, malic acid, fumaric acid and phosphoric acid. Acetic acid is the
major active component of vinegar. Citric acid is the most widely used acidulant in food
industry. Malic acid is used to mask the lingering bitterness of synthetic sweeteners. Gluconic
acid--lactone can produce gluconic acid upon heating and is hence a slow-acting acidulant. It
can be used as leavening agent in biscuit processing and curing agent in tofu preparation.
Phosphoric acid is mainly used in the production of cola-type beverages.
Salty Taste
The salty taste is contributed by neutral salts and it is an indispensable and the most
fundamental taste in foods. This taste is the compromise of the effects of dissociated anions
and cations. Cations produce salty taste, while anions suppress the sensation of salty taste and
elicit other undesirable tastes. Whether an inorganic salt is bitter or salty depends on the
diameters of cations and anions. If the sum of the diameters of cation and anion of a
compound is less than 0.65 nm, the salt tastes salty; otherwise, the salt tastes bitter. For
example, the sum of the diameters of Mg2+ and Cl- is 0.85 nm and MgCl2 tastes quite bitter.
L-sodium
glutamate
L-sodium
glutamate
(MSG)
(MSG)
Inosine-5-monophate
(5-IMP).
Inosine-5'monophosphate (5-IMP)
Sodium chloride is the only substance known to evoke a purely salty taste in any
concentration that is suprathreshold. The optimum concentration of NaCl in liquid foods is
0.8-1.2 %. Because excessive intake of NaCl can cause negative impacts on health, the
development of NaCl substitutes has attracted much attention. For example, a mixture of 20
% of KCl and 80 % NaCl has been developed as a low-sodium salt.
Delicious Flavor
The delicious flavor is a very complex sensation. The flavor enhances the appetite of
consumers and makes foods tasted more delicious. When the concentration of a delicious
254
compound in foods is higher than threshold value, it evidently increases the delicious taste of
the food, and enhances the original flavor of the food even its concentration is lower than its
threshold value. Hence, delicious compounds are also known as flavor enhancers.
Delicious compounds can be divided into amino acid, nucleotide and organic acid types
and their typical representatives are L-sodium glutamate (MSG), 5-inosine monophosphate
(5-IMP), and sodium succinate respectively. MSG is the first discovered and commercially
available flavor enhancer. It occurs widely in nature and is abundant in kelps. 5-IMP is
widely found in chickens, fishes and broths and 5-IMP in animals is mainly generated by the
degradation of ATP in muscles. 5-Guanosine monophosphate (5-GMP) is the major
delicious component in mushrooms. Sodium succinate has been identified in poultry,
livestock and mollusks and the highest content is detected in shellfishes. It is also present in
low levels in fermented products, such as soy sauce, sauce, and yellow rice wine. Aspartic
acid and its sodium salt are the main delicious substances in bamboo shoots, though their
intensities are lower than that of MSG. The combination of IMP, GMP and MSG
significantly enhance the delicious taste of MSG. For instance, the delicious intensity of the
mixture containing 1 % IMP, 1 % GMP, and 98 % MSG is four times of that of MSG alone.
Pungency
Certain compounds found in some spices and vegetables cause characteristic hot, sharp
and stinging sensations that are known collectively as pungency. Pungent compounds
enhance the appetite and increase the secretion of digestive juice of consumers and they are
indispensable condiments in daily life. Based on sensation, natural pungent compounds are
divided into hot, aromatic and irritative types.
Hot compounds: pungent compounds of this type are odorless and can cause the burning
feeling in mouth. The pungent compounds in chili, black pepper and zanthoxylum belong to
this type.
Chili.
Capsaicinoids are the vanillyl amides of monocarboxylic acids with varying chain length
(C8~C11) and capsaicin is the active component in chili pepper. The contents of capsaicin in
chili peppers vary significantly with species. The contents of capsaicin in red chili, horn red
chili, Sam chili, and Uganda chili are 0.06 %, 0.2 %, 0.3 %, and 0.85 %, respectively.
Capsaicin
Black pepper.
Piperine is the major pungent compound in black pepper. Pepperine is an amide
compound and has three isomers, of which the isomers with more cis double bonds possess
255
Food Flavors
high pungency intensity. The liability of black pepper to light and storage is due to the
isomerization of piperine isomers.
Pipirine
Zingiberols
Zingerols
Zingerone
Eugenol
Isoeugenol
Irritative compounds: in addition to tongue and oral mucosa, compounds of this type are
also irritative to nose and eyes.
256
The pungency and irritability of these materials are contributed by mustard oil that is
generated through the hydrolysis of sinigrin. It is the collective of isothiocyanate. The
following active substances have been identified in mustard, radish, and horseradish:
CH2=CH CH2- NCS CH3CH=CH-NCS
allyl isothiocyanate propylene isothiocyanate.
CH3(CH2)3- NCS C6H5CH2-NCS
butyl isothiocyanate benzyl isothiocyanate.
Welsh onion, garlic, leek, and onion.
Disulfides are the major pungent and irritative substances in welsh onion, garlic, leek,
and onion. The pungent components of garlic are generated by the decomposition of alliin
and include diallyl disulfide and allyl propyl disulfide. The pungent components in leek and
onion are also sulfur-containing compounds. These substances are converted to sweet thiol
compounds when heated. This is why cooked onion and garlic taste sweet other than pungent.
Astringency
Astringency is the sensation of the aggregation of proteins in oral mucosa. Tannins and
polyphenols are major components in foods that cause astringency. Besides, some salts (such
as alum), aldehydes, organic acids (such as oxalic acid), and quinine acid are sometimes also
involved in astringency sensation. Mature fruits taste less astringent than immature fruits,
because polyphenols are decomposed, oxidized, or polymerized during maturation. Tea also
contains polyphenols, but their contents vary with processing methods. Red tea is less
astringent than green tea, because polyphenols are oxidized during fermentation. Astringency
is a characteristic taste of red wine. To obtain an acceptable astringency, measures must be
taken to reduce the contents of polyphenols in wines.
257
Food Flavors
Table 8-3. Main aroma components in some fruits
Fruit
Apple
Pear
Banana
Muskmelon
Peach
Isoamyl formate
Isoamyl acetate, isoamyl isovalerate
Diethyl sebacate
Ethyl acetate, agarolactone
Apricot
Grape
Amyl butyrate
Methyl o-aminobenzoate
Citrus
Peel
Juice
Fresh vegetables.
Many fresh vegetables have the smell of soil. This aroma is generated by methoxy alkyl
pyrazines, such as 2-methoxy-3-isopropyl pyrazine in fresh tomato and pee, 2-methoxy-3isobutyl pyrazine in green pepper, and 2-methoxy-3-sec-butyl pyrazine in red beet root. These
compounds are synthesized from the precursor leucine. The biosynthesis pathway of pyrazine
compounds in plants is shown in Figure 8-7.
enzyme
leucine
2-methoxy-3-isobutyl
pyrazine
Figure 8-7. Biosynthesis pathway of methoxy alkyl pyrazines in plant tissues [3].
258
acetone alkyl
garlic alcohol ammonia
1-allyl-1-subsurfuracid
S-propionaldehyde-S-oxidate
Figure 8-9. Reactions involved in the formation of garlic flavor compounds [5].
Food Flavors
259
The aroma precursor of mushrooms is lenthionine acid. The precursor can be hydrolyzed
by S-alkyl-L-cysteine sulfoxide lyase to produce the aromatic lenthionine (Figure 8-11). In
addition, benzyl isothiocyanate, phenethyl isothiocyanate, and benzaldehyde cyanohydrin are
also involved in the aroma formation of mushroom.
Other vegetables.
The major aromatic compounds in cucumber are carbonyl substances and alcohols and its
characteristic aroma is contributed by 2-trans-6-cis-nonadienal, trans-2-nonene aldehyde and
2-trans-6-cis-nonadienol. Besides, 3-cis-hexenal, 2-trans-hexenal, and 2-trans-nonnenal also
affect the aroma of cucumber. These flavor compounds are synthesized from linoleic acid and
linolenic acid.
More than 80 kinds of volatile compounds have been identified in tomato, in which, 3cis-hexenal, 2-trans-hexenal, -ionone, hexanal, -damascenone, 1-penten-3-one, 3-methyl
butyraldehyde, are major active compounds for tomato aroma. In heated products such as
260
ketchup, the aroma changes due to the formation of dimethyl sulfide, the increase of ionone, -damascenone and the decrease of 3-cis-hexenal and hexanal.
Potato contains only trace amounts of aromatic compounds. Pyrazines, including 2isopropyl-3-methoxy-pyrazine, 3-ethyl-2-methoxy-pyrazine and 2, 5-dimethoxy-pyrazine, are
the major active components in fresh potato. Volatile compounds in cooked potato are
carbonyl compounds (including saturated and unsaturated aldehydes, ketones and aromatic
aldehydes), alcohols (C3~C8 alcohols, linalool, neroli and geraniol), sulfur compounds
(mercaptan, sulfide and thiazole) and furan compounds.
A large variety of terpenes have been identified in the volatile oil of carrot, mainly
including -bisabolene, caryophyllene, and terpinolene. cis--Bisabolene, trans--bisabolene
and hypoxanthine contribute to the characteristic smell of carrot.
261
Food Flavors
HO
CH2COOCH 3
CH CN
CH 2CH=CHCH 2CH3
O
OH
Cis-jasmone
Jasmine lactone
Methyl jasmonate
Nerolidol
Red tea
Red tea undergoes fermentation during processing and has strong aroma. During
processing, tremendous reactions occur to produce hundreds of aromatic components. Hence,
red tea has obviously different aroma from green tea. Alcohols, aldehydes, acids and esters
are major constituents of the aroma of red tea and violet ketone plays important role in the
formation of the characteristic aroma.
O
O2
Cis-theaspirane
-carotene
-ionone
-damascenone
Carotenoids, amino acids, and unsaturated fatty acids are the aroma precursors for red
tea. During processing, -carotene is oxidized and decomposed to ionone (Figure 8-12),
which is further oxidized dihydroaclinidiolide and theaspirone.
Unsaturated fatty acids in tea, especially linolenic acid and linoleic acid, undergo
enzymatic oxidation during processing to produce C6-C10 aldehydes and alcohols. Meanwhile,
the fatty acids are also esterified by alcohols to yield esters with different aromas, such as
benzyl acetate, ethyl phenylacetate, methyl benzoate, and methyl salicylate. These
compounds have important effects on the aroma of tea.
Amino acids are also decomposed by enzymes to produce aldehydes, alcohols, and acids.
These compounds also contribute to the aroma of red tea.
262
enzyme
Pregnenolone
5-male-16-en-3-one
Aromatic compounds in cooked meats are generated in three ways: lipid oxidation and
hydrolysis; Maillard reaction between amino acids or proteins and reducing sugars; and
further decomposition or recombination of flavor compounds. The aroma compositions of
cooked meats vary with the cooking temperature and processing methods. Cooked pork
contains reduced volatile compounds (mainly aldehydes, ketones, carboxylic acids and sulfur
compounds). Some non-volatile compounds, including free amino acids, peptides,
carbohydrates, vitamins and nucleotides, are important aroma precursors of livestock and
poultry meats. When heated, the precursors undergo various chemical reactions to yield
characteristic aromas.
When fat-containing beef is cooked, abundant volatile compounds are produced,
including fatty acids, aldehydes, ketones, alcohols, ethers, furan, pyrrole, lactones, aromatic
hydrocarbons, sulfur compounds (thiazole, thiophene, alkyl sulfur, sulfide, disulfide
compounds) and nitrogenous compounds (oxazole, pyrazine). To present, more than 600
volatile compounds have been identified in cooked beef, of which acidic compounds have
only minor effect on the aroma. Instead, thiophenes, furan, pyrazine compounds and pyridine
compounds contribute largely to the characteristic aroma of cooked beef. The composition of
the characteristic aroma of cooked pork is similar to that of beef, except that the contents of or -lactones converted from 4 (or 5)-hydroxyl fatty acid precursors are higher than in cooked
beef. Besides, cooked pork contains more unsaturated carbonyl and furan compounds than
cooked beef. Because mutton contains less free fatty acids and unsaturated fatty acids than
beef or pork, cooked mutton with less carbonyl compounds. The characteristic aroma of
cooked chicken meat is provided by sulfide and carbonyl compounds, in which, carbonyl
compounds, such as 2-trans-4-cis-decadien-1-al, are the most important active components.
The aroma of boiled meats is provided mainly by neutral compounds, such as sulfides,
furan-type and benzene-type compounds, while that of roasted meats is contributed mainly by
basic compounds, such as pyrazine, pyrrole, pyridine, and carbonyl compounds. However,
regardless of the processing method, sulfur compounds are the most important active
components for meat aroma. If sulfur compounds are removed, cooked meats will lose their
aroma. The content of hydrogen sulfide significantly affects the aroma of cooked meat. When
the content is too high, the odor of rotten egg is perceived; however, when the content is too
low, the aroma intensity is reduced. Smoked meats have unique aroma and tastes. The smoke
used contains phenols, formaldehyde, acetaldehyde, acetone, cresol, fatty acids, alcohols,
pyromucic aldehydes, and guaiacol, in which, fatty acids, phenols, and alcohols play
important role in the formation of the unique taste and aroma of smoked meats.
Lipids play an important role in the formation of the aroma of livestock meats. When
tallow is heated, it is decomposed and generates abundant compounds, including esters,
hydrocarbons, alcohols, carbonyl compounds, lactones, pyrazine and furan compounds, which
Food Flavors
263
are important active components of beef aroma. The same decomposition products have also
been detected in heated lard. When pork is cooked at temperatures lower than 100 C, flavor
compounds derived from fat accounts for more than 50 % of total aroma compounds.
Aquatic Products
Volatile compounds in fresh aquatic products.
Generally, fresh marine fishes and freshwater fishes have only light odor and the odor is
mainly provided by volatile carbonyl compounds and alcohols, including aldehyde (C6, C8,
and C9), ketones and alcohols (such as 1-octene-3-one, 2-trans-nonyl aldehyde, cis-1-5octadiene-3-one and 1-octene-3-ol). These compounds are generated from the oxidation of
unsaturated fatty acids by lipoxygenase. As the freshness decreases, the compositions of the
odor change gradually and a characteristic fishy smell is perceived. This smell is caused by amino-valeraldehyde, -amino-valeric acid and hexahydropyridine compounds in fish skin
mucus, which are synthesized from basic amino acids. -Amino-valeraldehyde and -aminovaleric acid have strong fishy smell. Because fish blood also contains -amino-valeraldehyde,
fish blood also smells fishy.
264
Volatile sulfur compounds are always detected in degraded marine fishes, such as
hydrogen sulfide, methyl mercaptan, dimethyl sulfide and diethyl sulfide. These compounds
are also involved in the unpleasant odor of marine fishes.
Marine fishes might exhibit the smell of oxidized fish oil or cod liver oil during storage
due to the oxidation of polyunsaturated fatty acids. Linolenic acid, arachidonic acid and
docosahexaenoic acid are the main unsaturated fatty acids in fish oil, their auto-oxidation
decomposition products can cause unpleasant odor. The smell of the oxidation products
depends on the degree of oxidation. In the early phase of oxidation, the products have the
smell of cucumber. As the oxidation proceeds, the smell of cod liver oil appears.
265
Food Flavors
linoleic acid
lipoxygenase
peroxidelyase
hexanal
+lipoxygenase
+aldehyde
lyase
++--yde
lyase
oxygen acid
2-trans-hexenal
2-trans-6-cis-nonadienal aldehyde
Figure 8-19. Lipoxygenase catalyzed formation of aldehydes from long-chain polyunsaturated fatty
acids [10].
266
267
Food Flavors
enzyme
eugenol
enzyme
enzyme
p-cresol
cinnamyl
alcohol
lignin polymer
3-methoxy-4-hydroxybenzaldehyd(vanillin)
Figure 8-22. Volatile compounds produced in the synthesis of shikimic acid [12].
In the synthetic pathway of shikimic acid, aromatic compounds (phenylalanine and other
aromatic amino acid) can be produced from intermediate product in the pathway. Besides
aromatic amino acid, the pathway can also form other volatile compounds related to essential
oil. Aromatic components which are formed by fumigation of food, some of them are also
formed from compounds in the shikimic acid pathway as precursors, such as vanillin.
Cinnamyl alcohol is an important aroma component in cinnamon perfume. Eugenol is the
main flavor and pungent ingredients in clove. Some important flavor compounds in shikimic
acid pathway are showed in Figure 8-22.
Terpenoids Synthesis
Terpenoids are important aromatic compounds of citrus fruits. Terpenoids containing two
or more isoprene units are nonvolatile and do not directly involve in aroma sensation.
Sesquiterpenes neral and ngcuka ketone are the characteristic aroma components of orange
and grapefruit respectively. Citral and limonene are monoterpenes and possesses the unique
smell of lemon and sour orange respectively. The enantiomers of terpenes may exhibit quite
different smells. For example, l-carvone [4(R)-(-) carvone] has a strong aroma of spearmint,
while d-carvone has the characteristic aroma of sweet wormwood (Figure 8-23).
268
Non-Enzymatic Reactions
Maillard Reaction
The Maillard reaction can yield a large number of aromatic compounds and their contents
and proportion vary with substrate type, heating duration, and temperature. When the reaction
occurs in a low temperature for a short time, aromatic l actones, pyran compounds and furan
compounds as well as Strecker aldehydes are produced. When the reaction proceeds in high
temperatures for a long time, pyrazine, pyrrole and pyridine compounds with baking aroma
are formed.
Pyrazine compounds are important flavor compounds in all bakery foods and thermally
processed foods. It is generally believed that pyrazine compounds are generated through the
Strecker degradation between amino acids and -dicarbonyl compounds, which are the
intermediates of the Maillard reaction (Figure 8-25). Small sulfides formed in the Maillard
reaction also influenced the flavor of foods. For example, methionic aldehyde is the
characteristic aroma compound of boiled potatoes and cheese biscuits.
Methionic aldehyde is unstable and can be easily decomposed into methane thiol and
dimethyl disulfide, resulting in the increase of low molecular weight sulfides.
The thermal degradation produces H2S and NH3 are also involve in the flavor formation
through Maillard reaction. For example, H2S, NH3, and acetaldehyde are the thermal
degradation products of cysteine. They can react with hydroxy ketones formed in the Maillard
reaction to generate thiazoline, which has the flavor of cooked beef (Figure 8-26).
269
Food Flavors
Figure 8-24. Formation of volatile compounds in the heterolactic fermentation of citric acid and
glucose.
Figure 8-25. Formation of an alkyl pyrazine and small sulfur compounds through the Maillard reaction
[13].
cysteine
3-hydroxyl-2-butanone
Fig. 9-24. Methionine reacts with carbonyl compounds to form thiazoline
2,4,5-trimethyl-3-thiazoline
Figure 8-26. Formation of a thiazoline through the reaction between the thermal degradation products
of cysteine and carbonyl compounds [13].
270
REFERENCES
[1] Shallenberer, RS; Acree, TE. Molecular theory of sweet taste. Nature, 1967, 216, 480482.
[2] DeTaeye, L; DeKeukeleire D; Siaeno E; Verzele M. Recent developments in hop
chemistry. In European Brewery Convention Proceedings. Amsterdam: European
Brewing Congress, 1977; 153-156.
[3] Morgan, ME; Libbey, LM; Scanlan, RA. Identity of the musty-potato aroma compound
in milk cultures of Pseudomonas taetrolens. Journal of Dairy Science, 1972, 55, 666
[4] Whitfield, FB; JH. Last Vegetables. In: Maarse, H. Volatile Compounds in Foods and
Beverages. New York: Marcel Dekker, 1991; 203-269.
[5] Shankaranarayana, ML; Raghaven, B; Abraham, KO; Natarajan, CP. Sulphur
compounds in flavours. In: Morton, ID; Macleod, AJ. Food Flavours, Part A,
Introduction. Amsterdam: Elsevier Scientific, 1982; 169-281.
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271
[6] Govindarajan, VS. Pungency: the stimuli and their evaluation. In: Boudreau, JC. Food
Taste Chemistry. Washington DC: American Chemical Society, 1979; 52-97.
[7] Hiraider, M; Miyazaki, Y; Shibata, Y. The smell and odorous components of dried
shiitake mushroom, Lentinula edodes I: relationship between sensory evaluations and
amounts of odorous components. Journal of Wood Science, 2004, 50, 358-364.
[8] Gower, DB; Hancock, M Bannister, LH. Biochemical studies on the boar pheromones,
5a-androst-16-en-3-one and 5a-androst-16-en-3a-ol, and their metabolism by olfactory
tissue. In: Cagan, RH; Kare, MR. Biochemistry of Taste and Olfaction. New York:
Academic Press, 1981; 7-31
[9] Hebard, CE; Flick, GJ; Martin. Occurrenceand significance of trimethylamine oxide and
its derivatives in fish and shellfish. In: Martin, RE; Flick, GJ; Ward, DR. Chemistry and
Bilchemistry of Marine Products. Westport: AVI Publishing, 1982; 149-304.
[10] Blank, I; Lin, J; Vera, FA; Weli, DH; Fay, LB. Identification of potent odorants formed
by autoxidation of arachidonic acid: structure elucidation and synthesis of (EZZ)-2,4,7tridecatrienal. Journal of Agricultural and Food Chemistry, 2001, 49, 2959-2965.
[11] Tressl, R; Holzer, D; Apetz, M. Biogenesis of volatiles in fruit and vegetables. In:
Maarse, H; Groenen, PJ. Aroma Research: Proceedings of the International Symposium
on Aroma Research, 1975 in Zeist, the Netherlands. Wageningen: Centre for
Agricultural Publishing and Documentation, 1975; 41-62.
[12] Wittkowski, R; Ruter, J; Drinda, H; Rafiei-Taghanaki, F. Formation of smoke flavor
compounds by thermal lignin degradation. In: Teranishi, R; Takeoka, GR; Guntert, M.
Flavor Precursors: Thermal and Enzymatic Conversions. Washington DC: American
Chemical Society, 1992; 232-243.
[13] Mussinan, CJ; Wilson, RA; Katz, I; Hruza, A; Vock, MH. Identification and some
flavor properties of some 3-oxazolines and 3-oxazolines and 3-thiazolines isolated from
cooked beef. In: Charalambous, G; Katz, I. Phenolic, Sulfur, and Nitrogen Compounds
in Food Flavors. Washington DC: American Chemical Society, 1976; 133-145.
ISBN: 978-1-61942-125-7
2012 Nova Science Publishers, Inc.
Chapter 9
FOOD ADDITIVES
1
ABSTRACT
Food additives are substances intentionally added by manufacturers to foods to
preserve flavor or enhance taste and appearance. A substantial amount of food additives
with different functions have been widely used in the food industry and these compounds
contribute largely to the development of the industry. Due to the increased concern on
food safety and the rapid development of analysis techniques, the definition of food
additive has evolved greatly. This chapter firstly describes the evolution of the definition
of food additives. Then, various food additives are introduced briefly according to their
classification and the functions, properties and related aspects of important additives are
described one by one.
1. INTRODUCTION
1.1. Definition
Food additives are regulated substances and therefore defined in law. The definition of
food additives was firstly proposed by the FAO/WHO Joint Expert Committee for Food
Additives (JECFA) in 1955 as non-nutritive substances added intentionally to food,
generally in small quantities, to improve its appearance, flavor, texture, or storage properties.
This definition covered a rather narrow range and did not include flavorings and nutrients.
Since then, the definition evolves gradually and various definitions have been proposed by
different countries or organizations.
According to the Chinese Hygienic Standards for the Use of Food Additives (GB27602007), food additives refer to artificially chemosynthetic or natural substances to be added to
foods in order to improve food quality and color, flavor and taste, and meet the need of
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1.2. Classification
According to origin or source, food additives are divided into natural and artificial ones.
Food additives are also classified by functions in most cases. In China, food additives are
subdivided into 21 categories, including acidulant, anticaking agent, antifoaming agent,
antioxidant, bleaching agent, bulking agent, chewing gum base, coloring agent, color fixative,
emulsifier, enzyme preparation, flavor enhancer, flour treatment agent, coating agent, water
retention agent, nutrition enhancer, preservative, stabilizing and coagulating agent, sweeter,
thickener and others.
Among the 1500 kinds of food additives approved for use in China, more than 700 kinds
are spices and essence oils.
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4. Food additives cannot be applied for the purpose of concealing the quality deficiency
caused by the food itself or by processing.
5. The application ranges, dosages, and residues of food additives must comply with
related national standards and regulations, and try to minimize the using amount to bring
about the desired result.
6. Processing aids must be removed after processing, except those with allowed residues.
2. ACIDULANTS
2.1. Functions
Acidulants or acidity regulators are some acids and their salts, which serve a variety of
functions shown as the following:
(1) Flavoring to provide a desired taste and serve to intensify, enhance, blend of modify
the overall flavor of the product.
(2) Reduction of the pH to prevent or retard the growth of microorganisms and the
germination of spores, and to increase the lethality of the process.
(3) Maintainer or establishment of pH by serving as buffering agents. Usually a
combination of free acids and salts are used.
(4) Chelation of metal ions (Cu, Fe) to assist in minimizing lipid oxidation, reducing
color changes and controlling texture in some fruits and vegetables.
(5) Alteration of the structure of foods including gels made from gums (pectin,
carrageenan), and proteins.
(6) Interaction with proteins and emulsifiers to modify the structure of foods such as
doughs, alter the heat stability of proteins, and to serve as an emulsifier in processed cheese.
(7) Modification of sugar crystallization in hard candy manufacturing.
2.2. Acidulants
The usual use of acidulants in food are acidic, phosphoric, citric, malic, succnic, tartaric,
lactic, gluconic, glycolic, fumaric and adipic acid. The pKa or pKa1 of them are 4.75, 2.1,
3.08, 3.4, 4.2, 3.2, 3.86, 3.60, 3.03 and 4.43, respectively. Their structures are shown in
Figure 9-1:
The differences between acidulates are flavor, acidity, metal chelating and antimicrobial
activity, solubility, hydroscopicity and cost. Citric, malic, tartaric and gluconic acids have
similar taste which compliant with making beverage and candy. But for cola drink, using
phosphoric acid is more suitable. Fumaric and acitic acid have good antimicrobial activity,
and acetic acid (vinegar) is an important condiment and functional agent for Chinese food,
mayonnaise and pickles. Tartaric acid is often used to make leavening (bulking agent) owing
to its lower solubility.
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Gluconolactone can be used to make Doufu and also used as a ingredient for making the
leavening because it can change to gluconic acid gradually in hot water.
Lactic acid has special taste, which compliant with many dairy products and fermented
food, such as yoghourt and alcohol. Phosphoric, citric, malice, succinct and tartaric acids are
metal chelating agents, they can be used as antioxidant synergist.
3. SWEETENERS
3.1. Type and Functions
There are two types of sweeteners: caloric (nutritive) and noncaloric (non-nutritive). The
caloric sweeteners provide about 4 calories per gram. The noncaloric varieties provide zero
calories.
Caloric sweeteners provide sweet flavor and bulk when added to food. They also
maintain freshness and contribute to product quality. Caloric sweeteners act as a preservative
in jams and jellies, and a flavor enhancer in processed meat. They provide fermentation for
breads and pickles, bulk to ice cream, and body to carbonated beverage. Some caloric
sweeteners are rich in natural resources, e.g., sucrose and fructose. Some are mainly made by
processing sugar or other small molecule compounds, e.g., molasses and sugar alcohols.
Sugar alcohols are low glycemic sweetener that is safe for diabetics, and helps manage
healthy glucose levels, and does not promote tooth decay.
Non-caloric sweeteners are used in place of caloric sweeteners in some foods. They do
not provide calories, but they do provide the sweet taste. Most non-caloric sweeteners are
chemically sythenic. Some of them, e.g., saccharin, acesulfame K and sucralose are more
stable than sugar to high temperature and other conditions of food processing, e.g., they do
not go in for non enzyme browning. Almost all of them can use in the diet for diabetics and
obesity patients.
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3.4. ISO-Maltulose
Iso-maltulose, also known by the trade name Palatinose, is a disaccharide that is
commercially manufactured from sucrose hydrolysed via bacterial fermentation. It is a natural
constituent of honey and sugar cane and has a very natural sweet taste. It is particularly
suitable as a non-cariogenic sucrose replacement. Iso-maltulose is fully absorbed in the small
intestine as glucose and fructose. Like sucrose, it is fully digested and provides the same
caloric value of approximately 4 kcal/g. However, it is low-glycemic and low-insulinemia.
Because isomaltulose is released to the blood slowly, this sweetener avoids the sudden
increase of drop of blood glucose level. This leads to a more balanced and prolonged energy
supply in the form of glucose. In China, iso-maltulose is allowed to use in many foods and the
quantity of use is decided by the needing of food manufacture.
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4. PRESERVATIVES
4.1. Definition
Preservatives or antimicrobial agents play an important role in today's supply of safe and
stable foods. Preservative means any substance which is capable of inhibiting, retarding or
arresting the process of fermentation, retarding acidification or other deterioration of food or
masking any of the evidence of putrefaction. Preservatives work by preventing the growth of
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microbes (fungi, bacteria) or by killing the microbes. Food preservatives, low toxicity, are
commonly used in food processing. They should not pose significant health effects on
consumers during normal consumption.
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Table 9-1. Properties of some preservatives [2,3]
Compound
Benzoic acid
(benzoate)
Sorbic acid
(sorbate)
Parabens
Dehydroacetic
acid
Sodium
propionate
Sulfites
Nitrites
Effective
against
Yeast, mold,
bacteria
Yeast, mold,
bacteria,
Bacteria,mold,
yeast
Mold,yeast,
bacteria
Mold
Effective
pH range
2.5-4.0
Bacteria,mold,
yeast
Bacteria,mold,
yeast
2.5-5.0
Water easily,
Oil slightly
Water easily,
Oil slightly
Ethnol easily, Water
slightly
Ethnol easily, Water
slightly
Water easily,
Ethnol easily,
Water easily
4.0-5.5
Water easily
3.0-6.5
3.0-9.0
3-10
6-8
Solubility
Some food
applications
Jam,juice,sauce
Meat, juice,
bread
Sauce, beverage,
baking product
Pickles,
orange pulp
Baking product,
meat
Wine,
dried fruits
Meat
The latter is used more often because benzoic acid is sparsely soluble in water, and
sodium benzoate is more soluble. The undissociated form on benzoic acid is the most
effective antimicrobial agent. The optimum pH range ranges from 2.5 to 4.0, which makes it
an effective antimicrobial in highly acidic foods. Benzoic acid and sodium benzoate are
widely used in fruit drinks, cider, carbonated beverages, sauce, jams and pickles with 1.0 g/kg
or less as the ML for different foods.
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All of these forms of sulfur are known as free sulfur dioxide. Meanwhile, the bisulfite ion
(HSO3-) can react with aldehydes, dextrins, pectic substances, proteins, ketones, and certain
sugars to form addition compounds, which are known as bound sulfur dioxide.
Sulfurous acid inhibits molds and bacteria to a lesser extent yeasts. For this reason, SO2
can be used to control undesirable bacteria and wild yeasts in fermentations without affecting
the SO2- tolerant cultured yeasts. The antiseptic activity of SO2 highly depend on the pH. The
lower the pH, the greater the antiseptic action of SO2. The amount of SO2 added to foods is
self-limiting because the product may develop an unpleasant off-flavor at concentration from
200 to 500 ppm. The use of SO2 is not permitted in foods that contain significant quantities of
thiamine, because this vitamin is destroyed by SO2.
Because SO2 is volatile and easily lost to the atmosphere, the residual levels may be
much lower than the amounts originally applied. In China, the ML of sulfites are calculated
by means of the residual levels in the finished food. Different food has different maxium
residual quantity. For example, the maximum residual quantities for fresh and dried fruits
processed are 0.05 g/kg and 0.2 g/kg, respectively.
4.4.5. Natamycin
Natamycin (Figure 9-3) is a naturally occurring antifungal agent produced by
Streptomyces natalensis. Natamycin has a very low solubility in water; however, it is
effective at very low levels. Natamycin has been used for decades in the food industry as a
hurdle to fungal outgrowth in dairy products, meats, and other foods. It has a neutral flavor
impact, and less dependence on pH for efficacy. It may be applied by spraying a liquid
suspension, by dipping the product in an aqueous suspension, or by mixing it into the product
in a powdered form along with cellulose on whole, shredded, or soft cheeses.
4.4.6. Nisin
Nisin is an antimicrobial polypeptide, with a molecular weight of 3500, produced by
some strains of Lactococcus lactis. Nisin-like substances are wide products from lactic acid
bacteria.
http://upload.wikimedia.org/wikipedia/commons/a/a3/Natamycin.svg
Figure 9-3. Structure of natamycin [5].
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These inhibitory substances are known as becteriocins. Nisin can be used as a processing
aid against gram-positive organisms. It has been effectively used in preservation of processed
cheese. It is also used in the heat treatment of nonacid foods and in extending the shelf life of
sterilized milk [6].
5. ANTIOXIDANTS
5.1. Definition and Classification
Food antioxidants in the broadest sense are all of the substances that have some effects on
preventing or retarding oxidative deterioration that leads to rancidity, loss of flavor, color and
nutritive value of foodstuffs in foods.
Antioxidants can be classified into a number of groups: (1) Primary antioxidants which
can terminate free radical chains reactions and function as electron donors including the
phnolic antioxidants, butylated hydroxyanisole (BHA), butylated hydroxytoluene (BHT),
tertiary butyl hydroquinone (TBHQ), propylgallate (PG), natural and synthetic tocopherols
and so on. (2) Oxygen scavengers which can remove oxygen in a closed food system. Most
widely used compounds are Vitamin C, and related substances, ascorbyl palmitate, and
erythorbic acid (the D-isomer of ascorbic acid). (3) Chelating agents or sequestrants. They
remove metallic ions, especially copper and iron, that are powerful pro-oxidants. Citric acid is
widely used for this purpose. Amino acids and ethylene diamine tetraacetic acid (EDTA) are
examples of chelating agents. (4) Enzymatic antioxidants which can remove head space
oxygen dissolved, such as glucose oxidase. Superoxide dismutase can be used to highly
remove oxidative compounds from food systems. (5) Natural antioxidants which are present
in many spices and herbs. Rosemary and sage are the most potent antioxidant spices.
AH 2
ROO AH
AH
AH
ROOH
ROOH
A AH 2
AH
A
Chelating agents which have ability to bind metal ions have contributed significantly to
stabilization of food color, aroma and texture because traces of heavy metal ions can act as
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catalysts for lipid oxidation. Many natural constituents of food can act as chelating agents, e.
g., carboxylic acids (oxalic, succinic), hydroxy acids (lactic, malic, tartaric, citric),
polyphosphoric acids (ATP, pyrophosphates), amino acids, peptides, proteins and porphyrins.
Both ascorbic acid and glucose plus glucose oxidase and catalase can deplete O2 in food
system. When they react with oxygen, ascorbic acid becomes to dehydroascorbic acid, and
glucose becomes to gluconic acid, and H2O2, another product of the oxidation of glucose, can
be broken down to water by catalase. When the oxygen has been depleted completely, the
food oxidation will stop. However, owing to VitC, oxidation is based on a complex
mechanism with some active substance giving birth to the midway of the reaction, adding less
quantity of VitC will prooxidant.
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It can maintain freshness and quality of crude oils during long distance transportation,
and can offer protection to fried foods, thus enhancing their storage life and freshness. The
highest level of TBHQ permitted in the GSFA (USA) is 1 g/kg for frozen fish, fish fillet, and
fish products, and in the FDs use standard (China) is 0.2 g/kg for edible oils and fats, fried
food, curing meat class, and dried fishes. It is often used in conjunction with BHA, BHT and
PG to provide a synergistic antioxidant effect.
Tea polyphenols, antioxidant of glycyrrhiza and antioxidant of bamboo leaves are natural
antioxidants being extracted from tea, liquorice and bamboo. Tea polyphenols are water
soluble. Antioxidant of glycyrrhiza is unsoluble in water but in ethanol and ethyl acetate. The
antioxidant of bamboo leaves is soluble in ethanol. They are phenols substance, such as
catechins, flavonoids and phenolic acids. The ML of TP, AG and ABL in the FDs use
standard (China) are 0.3, 0.2 and 0.5 g/kg, respectively.
Rosemary extract is another natural antioxidant. The active ingredients are ursolic acid,
rosmarinic acid, conorsic acid, and conorsol. The ML of it in the FDs use standard (China) is
0.3 g/kg.
EDTA is abbreviation of disodium ethylene-diamine-tetraacetate, a famous chelating
agent in analysis chemistry. Phytic acid (inositol hexaphosphoric acid), orthophosphoric acid,
pyrophosphoric acid, triphosphoric acid, hexameta-phosphoric acid, tartaric acid, citric acid,
gluconic acid, and their salts are also good chelating agents. All of those chelating agent have
certain ability of antioxidant. In the use standard of FDs of China, the ML of EDTA and
phytic acid are 0.07 and 0.2 g/kg repectivesly. The orthophosphoric acid, pyrophosphoric
acid, triphosphoric acid, hexameta-phosphoric acid are classified also as water retention
reagents which can be use with high levels as 3-5 g/kg. The other chelating agents meationed
above can be used in food without level limits.
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not suitable for an individual with an allergy to soya, so labelling of the source of the
ingredient is vital to aid in consumer choice in products safe for individuals with specific
dietary requirements.
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Common Name
Monoglyceride (MG)
Acetylated Monoglyceride (AMG)
Lactylated Monoglyceride (LMG)
CMG
SMG
PolyGlycerol Ester (PGE)
Sorbitan Ester (SOE)
Tween
PG Ester (PGME)
Sugar Ester (SE)
Lecithin (LC)
When an emulsifier will be used for a purpose, knowing its classification is important
because different classes of emulsifier have different properties, function and safety. For the
student to learn the basical knowledge, the concept of HLB (hydrophile-lipophile balance)
should be understood. The Hydrophilic-lipophilic balance of a surfactant is a measure of the
degree to decide whether it is hydrophilic or lipophilic, determining by calculating values for
the different regions of the molecule, as described by Griffin in 1949 and 1954.
Griffin's method for non-ionic surfactants as described in 1954 works as follows:
HLB = 20Mh / M
Where, Mh is the molecular mass of the hydrophilic portion of the Molecule, and M is
the molecular mass of the whole molecule, giving a result on an arbitrary scale of 0 to 20. An
HLB value of 0 corresponds to a completely hydrophobic molecule, and a value of 20 would
correspond to a molecule made up completely of hydrophilic components.
The HLB value can be used to predict the surfactant properties of a molecule:
Value from 0 to 3 indicates an anti-foaming agent.
Value from 4 to 6 indicates a W/O emulsifier.
Value from 7 to 9 indicates a wetting agent.
Value from 8 to 18 indicates an O/W emulsifier.
Value from 13 to 15 is typical of detergents.
Value of 10 to 18 indicates a solubiliser or hydrotrope.
Some of emulsifies' HLB values are listed in Table 9-3.
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purposes. In China, those emulsifiers are extensively used in dairy, pasta, butter, and coffee
drinks, with ML from 5 g/kg to production need.
(2) Acetic acid esters of monoglycerides.
Acetic acid esters of monoglyceride, also called as acetylated monoglyceride, are an
emulsifier in which acetic acid is bound with monoglyceride. It has little emulsifying activity
but there are many characteristics and application fields as follows: Soft acetylated
monoglyceride is able to expand by more than 8 times with tension. It is an extremely stable
oil of which peroxide value does not increase even when heated at 97.7 C for 1000 hours.
The combination of liquid acetylated monoglyceride and hydrogenated fats can improve the
quality of fats, for example, margarine characterized with small temperature changes and
wide plasticizing range, can be produced with them. It is a liquid characterized by being less
oily even at low temperatures and available as a solvent, lubricant, etc. Although it has no
function as a good emulsifier, it is usable for foaming fats and oils by itself or in combination
with other emulsifiers because of its stable alpha-crystal structure. Practically, it is used as
powdered foaming agents, solvents, plasticizers for gums and coating agents for food.
Table 9-3. HLB values of some emulsifiers [7]
Emulsifier
Acetylated monoglycerides
Sorbitan trioleate
Glycerol dioleate
Sorbitan tristearate
Propylene glycol monostearate
Glycerol Monoleate
Glycerol monostearate
Acetylated monoglycerides (stearate)
Sorbitan monooleate
Propylene glycol monolaurate
Sorbitan monostearate
Calcium stearoxyl-2-lactylate
Glycerol monolaurate
Sorbitan monopalmitate
Soy lecithin
Diacetylated tartaric acid esters of monoglycerides
Sodium Stearoyl lactylate
Sorbitan monolaurate
Polyoxyethylene (20) sorbitan tristearate
Polyoxyethylene (20) sorbitan trioleate
Polyoxyethylene (20) sorbitan monostearate
Sucrose monolaurate
Polyoxyethylene (20) sorbitan monooleate
Polyoxyethylene (20) sorbitan monopalmitate
HLB value
1.5
1.8
1.8
2.1
3.4
3.4
3.8
3.8
4.3
4.5
4.7
5.1
5.2
6.7
8.0
8.0
8.3
8.6
10.5
11.0
14.9
15.0
15.0
15.6
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290
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7.2. Classification
Raw material origin has been used to classify hydrocolloids, for example as seaweed
extracts, seed gums, fermentation products, plant exudates, animal gelatin or microorganic
gums. Their general functional properties may also be used to classify them as thickeners,
stabilizers or gelling agents. The resourceful plant polysaccharoses, like starch and cellulose,
are derived by some chemical methods are classified modify polysaccharoses. Natural
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stabilizers, thickeners and gelling agents coming from plants can be classified based on their
sources shown in Table 9-4.
Compounds examples
Guar gum, Locust bean gum, Tara gum
Acacia gum, Tragacanth gum
Pectin
Cellulose, Starches
Agar, Alginates, Carrageenan
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this and xanthan gum is the typical hydrocolloid to supply this functionality. For beverage
with pulp suspended, like orange juice with pulp particle, precipitation can be prevented by
adding suitable amount agar to crate a small yield point which is big enough to stop the pulp
settling during the shelf-life and small enough to keep the beverage's flow property like
normal drink.
7.3.4. Gelation
One of the key texturising aspects of hydrocolloids is the ability to gel and solidify fluid
products. For example, in gelled milk desserts, even low levels of carrageenan will form a
solid milk gel. Other classic gelling agents are pectin, gelatin and agar. However, others will
form a gel under specific conditions. Certain grades of alginates form gels with calcium ions.
Xanthan and locust bean gum alone do not gel, but their combination display synergy and
form a strong cohesive gel. Methyl cellulose and hydroxypropylmethyl cellulose are unusual
in forming solutions that reversibly thicken or gel when heated. The food industry has a
myriad of gelling applications ranging from soft, elastic gels to hard and brittle gels.
7.3.5. Nutritional and Nutraceutical Function
There is already a wide use of some hydrocolloids. For example, Arabic and guar gum
are sources of soluble dietary fiber. Much research has been conducted in the nutraceutical
benefits of hydrocolloids. Potential benefits range from cholesterol reduction to cancer risk
prevention.
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dessert gels, aspics, confectionery jellies, canned meats gels, a vegetarian gelatin substitute, a
thickener for soups, and as a clarifying agent in brewing.
7.4.3. Alginates
Alginates are derived from various species of brown seaweed found off the coasts of the
North Atlantic, South America and Asia. They are produced as a range of salts, but sodium
and potassium alginate are predominantly used in foods. It is a polysaccharide, consisting
primarily of D- and L-galactose units. About every tenth D-galactopyranose unit contains a
sulphate ester group. Calcium, magnesium, potassium or sodium cations are also associated
with the polysaccharide. It is insoluble in cold water and soluble in boiling water. Sodium or
potassium alginate hydrates in cold or hot water to give viscous solutions. The controlled
interaction between sodium or potassium alginate and calcium salts gives cold-setting gels
that are shear irreversible and heat stable. Control is affected using citrate or phosphate
sequestrants, or by processing at temperatures above about 70 C and cooling. Typical food
applications include reformed foods such as onion rings and olive fillings, cold-setting bakery
cream fillings and heat-stable bakery and fruit fillings.
7.4.4. Carrageenan
Carrageenan is obtained from red seaweeds. Different species provide a number of
carrageenan extracts. Carrageenan is a hydrocolloid consisting mainly of the ammonium,
calcium, magnesium, potassium and sodium sulphate esters of galactose and 3, 6anhydrogalactose polysaccharides. These hexoses are alternatively linked -1, 3 and -1, 4 in
the copolymer. The relative proportions of cations existing in carrageenan may be changed
during processing to the extent that may become predominant. Depending on the source of
seaweed, the functional components are kappa-carrageenan, iota-carrageenan or lambdacarrageenan, each of which is characterized by the content of sulphate groups and gelling
properties. Carrageenan is soluble in water of about 80 C, forming a viscous, clear or slightly
opalescent solution that flows readily. It is insoluble in ethanol.
Kappa carrageenan and furcellaran form thermally reversible firm, brittle gels. Iota
carrageenan gives soft, elastic gels. Kappa carrageenan interacts synergistically with
polymannans, such as locust bean gum and konjac, to give strong cohesive gels. Blends of
kappa with iota carrageenan or polymannans are used to give a range of gel textures used in
injected meats, canned meats and water dessert gels..
Hybrid (kappa/iota) carrageenan is particularly suitable for firm, creamy textures in dairy
desserts. Lambda carrageenan is non-gelling but thickens in drinks and dairy desserts. A
specific interaction between kappa carrageenan and kappa casein is widely used to stabilise
dairy products including milk beverages, ice cream mixes and processed cheese products.
7.4.5. Microcrystalline Cellulose
Microcrystalline cellulose is produced by converting fibrous cellulose to a fine-particle
form crystalline cellulose using acid hydrolysis. This material can be readily dispersed in
water using high shear. This dispersion will reconstitute to deliver a colloidal form which is
unique when compared to other soluble food hydrocolloids. It exhibits a variety of desirable
characteristics including suspension of solids, heat stability, ice crystal control, emulsion
stabilization, foam stability, texture modification and fat replacement. Food applications
include frozen desserts and ice cream, whipped toppings, low-fat mayonnaise and salad
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7.4.10. Pectin
Pectin is a polysaccharide that is naturally present in most land plants, although
commercial pectin is primarily extracted from citrus peel and apple pomace. Two forms of
commercial pectin are available: high methyl- and low methyl-esterified pectin; and two
versions of the latter exist: a conventional and an amidated form. High methyl-esterified
pectin forms gels in high soluble solids and acidic systems, whereas low methyl-esterified
pectin forms gels in a much broader pH and soluble-solids range, but requires the presence of
divalent cations for gelling. As a consequence, each type has its own particular function.
Nevertheless, general attractive features include excellent flavor release, good processing
characteristics and stability at low pH. Its traditional and major function is to act as a gelling
agent in foods, but, nowadays, it also serves as a thickening and stabilizing agent. The
application of pectin is diverse and covers fruit-based products, dairy products, acidified milk
drinks and other beverages, confectionery, bakery products, various fine foods and spreads.
Additionally, pectin is used in the pharmaceutical industry. Finally, increasing consumer
awareness of healthy life-style habits and the emerging trend to produce functional foods
increases the significance of the status of pectin as a water-soluble dietary fiber.
7.4.11. Xanthan Gum
Xanthan gum is a high-molecular-weight polysaccharide of which D-glucose and Dmannose are the dominant hexose units, along with D-glocuronic acid and pyruvic acid,
secreted by the microorganism Xanthomonas campestris and produced commercially in a
batch fermentation process. It exists as the sodium, potassium or calcium salts. Its solutions
are neutral. It is soluble in water, and insoluble in cold water. The solution is a neutral and
viscous one with pseudoplastic flow behaviour. This gives excellent suspension and cling at
low shear and excellent mouthfeel and pouring properties at high shear. The xanthan gum
molecule has a cellulosic backbone with side chains that wrap around the backbone protecting
it and conferring excellent stability across a wide pH range and tolerance of high salt
concentrations and ingredients, such as glycerol and alcohol. The rigid backbone helps to
maintain viscosity during heating. Xanthan gum shows synergistic thickening with guar gum
and forms very elastic cohesive gels with locust bean gum and konjac mannan. Typical
applications include sauces and dressings, baked goods, beverages, desserts and ice creams.
7.4.12. Gellan Gun
Gellan gum is a fermentation polysaccharide produced by the microorganism
Sphingomonas elodea. It has a straight chain structure based on repeating glucose, rhamnose
and glucuronic acid units with side groups of acryl groups. Gellan gum hydrates in hot water
and the low-acyl form also hydrates in cold water with sequestrants. On cooling, native highacyl gellan gum gives gels that are soft and elastic. Low-acyl gellan gum gels at very low
concentrations using both monovalent and divalent cations gives firm, brittle textures with
excellent thermal stability. Combinations of the two kinds of gellan gum can be used to
control syneresis and form a range of textures from soft and elastic to firm and brittle. A
major food application is water dessert gels, particularly for Asian desserts. Other significant
applications include confectionery, dairy desserts and bakery fillings. At levels too low to
form a demoldable gel, gellan gum can form fluid gels that can suspend particulates in sauces
and dressings and fruit pulp in beverages.
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9. COLORANTS
Dyes and pigments used in the food are known collectively as food colours, or more
tersely, simply as colours. They are added to foods to make it more attractive to the purchaser
or consumers or to replace natural colours lost during the food processing. Canned
strawberries, for example, would be grayish-brown if colours are not added and canned peas
would be brownish green without colouring with green colorant.
In China, only 56 colorants are permitted for use as FDs. Most of them are natural, and
include saffron, cochineal, carotenes (and the closely related xanthophylls) and anthocyanins.
Other permitted colorants include synthetic or semi-synthytic coumpound, such as carotene
structure identical, sodium copper chlorophyllin and erythrosin, and inorganic substances,
such as the white pigment titanium dioxide and finely divided aluminum, silver and gold
which are used in cake decoration.
The list of permitted colours includes 9 synthesis dyes and 47 natural pigments or
extracts. Most of them are used in foods with strictly limits. For example, colouring matter
must not be added to raw meat, fish, poultry, fruit, cream, milk, honey, vegetables, wine,
coffee, tea and condensed or dried milk in most countries. Also, by agreement with the
manufacturers, colours are not used in foods made for babies and infants. The 9 synthesis
colours use in China are amaranth, ponceau 4R, erythrosin, new red, lemon yellow, indigo
blue, sunset yellow, brilliant blue and crimson. Sodium copper chlorophyllin is a semisynthesis colour which is also permitted in China. The 47 natural colours are -carotene
(zymotechnics), bect-root red, turmeric yellow, curcumin, safflower yellow,
http://www.chinaadditives.com/Carthamus-Red.htm lac dye, cowberry red, papika extract
include capsorubin and capsanthin, chilli orange, caramel, carthamus yellow, gardenia
yellow, coreopsis yellow extract, wild groundnut red, broomcorn red, maize yellow include
zeaxanthin and crtotixabthin, radish red, cacao husk pigment, ang-kak, monascorubin,
vinespinach red, black currant red, neutral mustard red, gardenia blue, hippophae
rhamnoides(sea backthern) yellow, hibiscus sabaariffa(roselle) red, acorn husk brown, NP red
(NP), tanoak brown, mulberry red, natural amaranth, cherokee rose brown, wide jujube skin
extract, peanut underwear red, grape skin red, uguisukagnra color, spirulina blue, vegetable
carbon black, pale butterflybush flower yellow, gromwell red, theaflavin, tea green pigment,
citrus yellow, bixin, cochineal red and iron oxide red or black.
All of the 9 synthesis colours and most of natural colours used in China are water soluble
and purchased in a powder format that exhibits coloring solutions when they are dissolved.
Therefore, their using are very easy.
Aluminum lake pigments, made of aluminum and colorants, are water insoluble material
but oil dispersible (but generally not oil soluble) and thus can be mixed with oils and fats.
They can also be dispersed in other carriers such as propylene glycol, glycerin and sucrose
(water and sugar). Aluminum lake pigments are used in a variety of applications: (1) To color
a fat based product, such as chocolate or compound coatings. For these, we produce a
concentrated dispersion in a high quality and very stable vegetable oil. The dispersion is
added directly to the chocolate to dye it accordingly. (2) For "hard panning" (to dye the
outside of a product such as a gum ball or a pill). In this case, we produce a dispersion usually
using sucrose (sugar and water) that is applied to the candy or food as it is being tumbled and
dried. Multiple layers are applied to produce the desired shade.(3) Lakes tend to resist
bleeding. Dyes have a tendency to "bleed", or migrate from one part of the product to another.
This can be a problem in candy canes or any product where there are defined borders such as
Food Additives
301
the food with desired stripes. While Dyes are normally used in hard candy, lakes are
sometimes substituted if bleeding is a problem.
Chemical substances
Isothiocyantaes (except for those generally recognized as toxic).
3
4
5
Ethers.
Esters.
Ketones.
6
7
8
9
Fatty Acids.
Aliphatic Higher Alcohols.
Aliphatic Higher Aldehydes (except for those generally recognized as toxic)
Aliphatic Higher Hydrocarbons (except for those generally recognized as toxic)
10
11
12
13
14
15
16
17
18
302
REFERENCES
[1]
[2]
[3]
[4]
[5]
[6]
[7]
Food Additives
[8]
303
Ren, P; R, YW; Wang, LD. Properties of Plant Gum and Its Application in Food
Industry. Food Research and Development, 2004, 39-44.
ISBN: 978-1-61942-125-7
2012 Nova Science Publishers, Inc.
Chapter 10
TOXICANTS IN FOODS
Wang Dongfeng1, Guoqing Huang2 and Shuhui Wang3
1
ABSTRACT
Microorganisms, plants and animals have evolved multiple defense systems against
predators. Among the systems, the chemical defense system is of special interest for the
food industry. Some of these compounds are toxic to specific microorganisms, insects,
birds, and mammals, but most of those are toxic to humans and can give rise to chronic or
acute symptoms of poisoning. Though some of the compounds occur in very low
concentrations, the compounds have a cumulative harmful effect if they constitute a part
of the normal diet over a prolonged period. Besides, food materials might be
contaminated by exogenous toxins. Intrinsic toxins and contaminants have been
recognized as the major components that affect food safety. This chapter introduces the
occurrence and properties of the most important toxicants in foods, including allergens,
toxic glycosides, toxic amino acids, lectins, saponins, toxins in aquatic organisms,
various antinutrients, heavy metals, pesticide residues, dioxins, veterinary and fish drug
residues, benzopyrenes as well as heterocyclic amines. Besides, measures for preventing
the generation of some toxicants are proposed.
1. INTRODUCTION
According to structure and biological effects on human body, toxicants in foods are
divided into toxic substances, harmful substances, and antinutrients. A toxic compound shows
its toxicity even in a very low dose, and a harmful substance is toxic only when its content
exceeds a certain threshold. An antinutrient may interfere in or inhibit the absorption of other
nutrients in foods. The definitions of these terms, however, are subject to changes due to the
306
improvement of analysis techniques and the availability of more data on their biological
effects. It has been found that some toxicants are beneficial in certain contents and some
substances are toxic or hazardous only in certain cases. For example, phenols in foods are
often recognized as antinutrients since they inhibit the adsorption of proteins. However,
phenols have the anti-oxidation and free radical scavenging capabilities and can be used as
natural antioxidants in foods. In addition, some well-known nutrients may be risky to certain
individuals, such as lactose, which may be deleterious to lactose-intolerant individuals.
According to origin, hazards in foods can be divided into inherent toxicants (or
endogenous toxicants) and contaminants (or exogenous toxicants). Endogenous toxicants are
metabolites produced via biosynthesis by food organisms under normal growth or metabolites
produced via biosynthesis by food organisms that are stressed. Contaminants refer to
toxicants that directly contaminate foods, toxicants that are absorbed from the environment by
food-producing organisms, toxic metabolites produced by food organisms from substances
that are absorbed from the environment, and toxicants that are formed during food preparation
[1].
Table 10-1. Endogenous toxicants in foods
Toxicants
Glucosinolates
(goitrogens)
Cyanogenic
glycosides
Lectins
Source
Cruciferae seeds, oilseeds,
mustard seed, kale, radish,
cabbage, peanut, soybean,
cassava, onion, et al.
Cassava, sweet potato, nuts,
kidney bean, limabean, millet,
broomcorn millet, et al
Papilionaceae, cereals, soybean,
and other beans
Glycoalkaloids
Gossypol
Cottonseed
Tetrodotoxin
Globefish
Shellfish
toxins
Histamine
Mycotoxins
307
Toxicants in Foods
Table 10-2. Endogenous antinutrients in foods
Antinutrient
Source
Oxalic acid
Phenols
Phytates
Protease
inhibitors
Saponins
Tannins
Non-protein
amino acids
Legume, seaweed
Source
Heavy metals
Veterinary drugs
Microbial toxins
Microorganism-polluted
foods and materials
Organophosphoru
s pesticides
It should be noted that all chemicals are potentially toxic, and that the dose alone
determines whether or not a toxic effect occurs. Indeed, toxicant (or toxin) is recently defined
as a substance that has been shown to present some significant degree of possible risk when
consumed in sufficient quantity by humans or animals [2]. For example, pure water drunk to
excessive can induce an electrolyte imbalance and lead to death, which is called the water
toxicity that is due in part to decreased renal capacity to excrete water [3]. The innumerable
308
naturally occurring chemicals in food are potentially capable of inducing toxic effects, but
few are ordinarily present in sufficient concentrations to actually show toxic effect [2, 4].
Hence, we should distinguish between toxic substance and toxic effect. The most
frequently occurring toxicants in foods are listed in Table 10-1~10-3.
A substantial number of toxic substances have been isolated and identified This chapter
concerns only the most important toxicants that have been identified in foods.
2. ENDOGENEOUS TOXICANTS
Endogeneous toxicants include any substances produced by food materials (either plants
or animals) that are harmful to human beings. Lectins, saponins, and toxic peptides mentioned
above are endogenous toxicants.
2.1. Allergen
An allergen refers to any substance that can cause an allergy. Most immune responses of
caused by food components are IgE-mediated immediate allergic reactions. Upon exposure to
allergens, the lymphatic system of human body acts to avoid or alleviate the adverse effects.
Most antigens can be metabolized to monosaccharides, amino acids and lower fatty acids
after antigen-antibody reactions. However, complete-antigens, which are characteristic of
both immunogenicity and immunoreactivity, can cause immune reactions.
The intake of allergen-containing foods can cause allergic symptoms, such as pruritus,
functional gastrointestinal disorder and fever. Many foods have been found to contain
allergens, but the sensitivity to these foods varies with local diet, environmental factors and
possibly genetics. Epidemiological investigations reveal that the incidence of food-induced
allergy in infants and children is higher than that in adults and the incidence decreases as age
increases.
Food allergens share the following characteristics:
1. Allergens are present in most foods, such as milk, eggs, and soybean, of which, milk
and egg are the most important source of allergens. Though allergens occur widely in foods,
90% of food allergies are induced by only a small number of foods.
2. Only few food components are allergenic. For example, up to 23 types of
glycoproteins have been identified in white egg, but only ovalbumin, conalbumin, and
ovomucin are allergic.
3. The allergenicity of foods is subject to change after processing. For example, heat
treatment inactivates most allergens and the increase of acidity or the presence of digestive
enzymes reduces the allergenicity of foods.
4. Sensitive consumers could suffer allergic cross reactions. Some proteins contain the
same antigenic determinant and these proteins can cause allergic cross reactions. For instance,
at least 50% of patients allergic to cows milk also react to goats milk and patients allergic to
chicken eggs might be allergic to the eggs of other birds.
Toxicants in Foods
309
Source
Almond, cherry, peach, plums,
apples
Sorghums
Linseed, clovers, cassava, lima beans
Linseed, cloves, cassava, lima beans
Cherry, almond
Vetches
Hydrolytic products
HCN, gentobiose, and benzaldehyde
HCN, glucose, and hydroxybenzaldehyde
HCN, glucose, and acetone
HCN, glucose, and 2-butanone
HCN, glucose, and benzaldehyde
HCN, vicianose, and benzaldehyde
Content
3~6
18~31
10
4~10
<1
2~3
2.5
9
<1
310
2.2.2. Glucosinolates
Structure and main species
Glcosinolates, also known as -thioglucoside N-hydroxysulfates, contain one branch and
one glucopyranose residue bound via a sulfur atom, as shown in Figure 10-1.
The side group R may be sulfur-containing groups, straight-chain alkanes, side-chain
alkanes, olefins, saturated alcohols, ketones, aromatic groups, benzoates, indole, polyglucose
groups, or others. Among the glucosinolates that have been identified, one third of the
compounds possess sulfur-containing R groups and the sulfur atoms are present in multiple
forms, such as methyl sulfanes, methyl thionyl alkanes, and methyl sulfuryl alkanes. Plants of
the Cruciferae family have high levels of glucosinolates and the side chain R may be alkanes,
-methyl sulfanes, aromatic groups, or heterocyclic groups.
Glucosinolates that act as progoitrins are the source of organic nitriles, isothiocyanates,
and SCN ions. Some of these compounds have been shown to be quite harmful if consumed
in sufficient amounts by humans and animals.
Enzymatic hydrolysis and changes in processing
Glucosinolates are quite stable. They are the precursors of isothiocyanates and are present
in much higher levels than their hydrolyzates in fresh plants. Glucosinolates can produce a
large variety of products when exposed to myrosinase as shown in Figure 10-2. In the case of
fresh plants chewing or tissue injury during cultivation, harvest, transport, and processing due
to scratching or freezing-thawing, glucosinolates get contact with myrosinase (EC 3.2.3.1)
and are hydrolyzed to toxic isothiocyanates.
Glucosinolates and their enzymatic hydrolyzates are water soluble. During cooking, more
than a half of the compounds are released to water, but the specific loss caused by processing
varies with vegetable species.
Myrosinase can be activated by Vc. Many facts have proved that myrosinase is inactive
in the absence of Vc. The activation is not due to the reducing property of Vc, instead due to a
nucleophilic group provided by Vc. Vc improves the Vmax and Km of myrosinase on its
substrates [6].
Toxicants in Foods
311
2.3.1. Classification
Up to hundreds of non-proteinic amino acids have been identified in animals and plants
and most of them are the intermediate or final products of certain metabolisms in animals and
plants. Toxic amino acids can be divided into two categories according to their toxicity:
Table 10-6. Some toxic amino acids commonly occurring in plant foods and forages [7,8]
Amino acid
N-(3-hydroxypyridone-4)-2-aminopropionic acid
(mimosine)
2-Amino-4-(guanidinooxy)butyric acid
(canavanine)
L-2-Amino-6-amidinohexanoic acid (indospicine)
5-Hydroxy-L-tryptophan (5-HTP)
2-Amino-3-methylaminopropionic acid
L-3,4-dihydroxyphenylalanine (L-DOPA)
3-Methylenecyclopropylpropionic acid
(hypoglycin A)
Seleno-amino acids (methylselenocysteine,
selenocystathionine, selenocystine)
3-Cyanoalanine and 4-Glutamylcyanoalanine
-Acetyl ornithine
Homoserine and o-oxalylhomoserine
Lathyrine, -methyl glutamic acid, hydroxynorvaline, and -hydroxyhomoarginine
Homoarginine and pipecolic acid
Source
Many species of Mimosoidae (a subfamily
of Leguminosae)
Many species of Papilionoidae (a
subfamily of Leguminosae
Tropical legume Indigofera spicata
Griffonia simplicifolia
Cycas spp.
Vicia and some other legumes
Plants of Sapindaeceae family
Plants grown on selenium-rich soils
Vicia spp.
Lathyrus spp.
Lathyrus spp.
Lathyrus spp.
Lathyrus and Vicia spp.
312
The representatives are , -diaminobutyric acid, -cyano-L-alanine, -N-oxalyl-, diamino-propionic acid and L-homoarginine.
2.3.2. Toxicity
Toxic amino acids are not essential for human body and can interfere with the normal
amino acid metabolism. Djenko sickness is a disorder of the urinary tract and most cases are
caused by the intake of djenko bean, which contains the toxic djenkolic acid. In some legume
species, the contents of djenkolic acid can reach 1~2% and its content in black varieties is as
high as 3~4%. Djenkolic acid shares a similar structure with cysteine and thus can interfere in
the metabolism of this essential amino acid.
2.4. Lectins
2.4.1. Classification
Lectins occur widely in plants, animals, and microorganisms. Exogenous lectins are also
known as vegetable haemagglutinin. They are sugar-binding proteins or glycoproteins of nonimmune origin and can lead to selective red blood cell agglutination in human blood. Lectins
can reversibly bind to specific monosaccharides or oligosaccharides. Most lectins contain
more than one sugar-binding site for cross connection with oligosaccharides. The molecular
weight of lectins ranges from 91 kDal to 130 kDal. Lectins are natural antigen of red blood
cells and are heat stable. Some lectins are highly toxic to experimental animals. For example,
when mouse are orally fed with 80 mg/kg garlic lectin for consecutively 7 days, both the
appetite and body weight are significantly reduced.
Vegetable hemagglutinin is firstly discovered in castor seeds. To present, a large number
of lectins with different properties have been identified. According to structure, lectins are
divided into merolectin, hololectin, chemerolectin, and superlectin. Based on the specificity to
sugars, lectins can be of the fucose type, the galactose/N-acetyl galactosamine type, the Naceytl glucosamine type, the mannose type, the sialic acid type, or the glycoconjugate type.
According to the origin, lectins can be divided into legume-derived lectins, mannose-binding
lectins, chitin-binding lectins, type-2 ribosome-inactivating proteins (RIP), and lectins derived
from other crops. According to the agglutination to red blood cells, lectins can be categorized
as specific and non-specific lectins. Based on evolution and structure correlation, lections can
be divided into 7 families. Table 10-7 lists the structure, sugar specificity, and distribution of
the 7 families in crops.
Based on reported researches, Peumans W J divided the lectins that have been identified
in crops into 5 categories: (1) legume lectins. Legume lectins are a family of structurally
related lectins that occur exclusively within the legume family. In Spite of their structural and
evolutionary relationships, legume lectins exhibit a wide range of carbohydrate-binding
specificities. (2) Monocot mannose-binding lectins. Monocot mannose-binding lectins occur
in at least five different families (Amaryllidaceae, Alliaceae, Araceae, Liliaceae and
Orchidaceae). They all have a similar molecular structure and sugar-binding specificity. (3)
chitin-binding lectins.
313
Toxicants in Foods
Table 10-7. Properties of the 7 families and their distribution in crops
Family
Structure
Leguminous
lectin
-sandwich
Monocot
mannose-binding
lectin
Specificity
Man/Glc Gal/Gal NAc
(GlcNAc)n Fuc
Sia2,3 Gal/GalNAc
complex
-barrel
Man
Family
Hevein domaincontaining chitinbinding lectin
Type-2 ribosomeinactivating
proteins
Structure
Hevein
domain
Specificity
(GlcNac)n
-trefoil
Gal/GalNac
Sia2,6 Gal/GalNAc
Cucurbitaceae
Phloem Lectins
Breadfruit lectin
Unknown
(GlcNac)n
-prism
Gal/T-antigen
Man
Amaranthaceae
lectin
-trefoil
GalNAc/T-antigen
Distribution
Leguminosae
Orchidaceae, Liliaceae,
Amaryllidaceae, Araceae,
Alliaceae, Bromeliaceae,
Iridaceae
Distribution
Gramineae, Solanaceae,
Urticaceae, Loranthaceae
Euphorbiaceae,
Caprifoliaceae, Loranthaceae,
Iridaceae, Ranunculaceae,
Lauraceae, Passifloraceae,
Liliaceae, Leguminosae
Cucurbitaceae
Moraceae, Convolvulaceae,
Compositae, Musaceae,
Gramineae, Cruciferae
Amaranthaceae
Tissue
Oral
toxicity
Heat
stability a
Seed
Content in
raw material
(g/kg)
0.2-2
Arachis hypogaea
(peanut)
Glycine max
(soybean)
Lens culinaris
(lentil)
Phaseolus
coccineus (scarlet
runner bean)
Phaseolus lunatus
(lima bean)
Phaseolus
acutifolius (tepary
bean)
Slight
Unstable
Yes
Yes
Seed
0.2-2
Slight
Low
Yes
No
Seed
0.1-1
Slight
Unstable
Yes
No
Seed
1-10
High
Moderate
Yes
Possibly
Seed
1-10
High
Moderate
Yes
Possibly
Seed
1-10
High
Moderate
Yes
Possibly
314
Species (common
name)
Tissue
Content in
raw material
(g/kg)
1-10
Oral
toxicity
Heat
stability a
Harmful lectin in
food
Phaseolus
Seed
High
Moderate
Yes
Possibly
vulgaris (kidney
bean)
Pisum sativum
Seed
0.2-2
Minor
Unstable
Possible No
(garden pea)
Vicia faba (fava
Seed
0.1-1
Minor
Unstable
Possible No
bean)
Note: a Heat stability (of purified lectin in aqueous solution); very high: withstands 90C; high:
withstands 80C; moderate: withstands 70C; low: withstands 6OT; unstable: denatured at 60C.
The definitions also apply to Table 10-6.
Tissue
Content in raw
material (g/kg)
Oral toxicity
Heat stability
Bulb
0.01-0.1
Nontoxic
Moderate
No
No
Bulb
<0.01
Nontoxic
Moderate
No
No
Leaf
<0.01
Nontoxic
Moderate
No
No
Bulb
0.5-2
Nontoxic
Moderate
No
No
Bulb
1-5
Nontoxic
Moderate
No
No
Tuber
1-5
ND
Moderate
No
No
Tuber
1-5
ND
Moderate
No
No
315
Toxicants in Foods
to lectin poisoning. Experiments have proved that when mouse are fed lectin-containing crude
soybean powder, the mouse will suffer either enterocyte breakdown, leading to intestine
malfunction, or reduced activity of hydrolytic enzymes in stomach and intestine, leading to
decreased nutrient adsorption and inhibited growth.
Table 10-10. Chitin-binding lectin [10]
Species (common
name)
Tissue
Oral
toxicity
Heat
stability
Seed
Content in
raw material
(g/kg)
<0.01
Hordeum vulgare
(barley)
Oryza sativa (rice)
Secale cereale
(rye)
Triticum vulgare
(wheat)
Triticum vulgare
(wheat)
Amaranthus
caudatus
(amaranth seeds)
antifungal protein
Cyphomandra
betacea (tamarillo)
Lycopersicon
esculentum
(tomato)
Solanum
tuberosum (potato)
ND
High
Yes
Possible
Seed
Seed
<0.01
<0.01
ND
ND
High
High
Yes
Yes
Possible
Possible
Seed
<0.01
Moderate
High
Yes
Yes
Germ
0.1-0.5
Moderate
High
Yes
Yes
Seed
0.1
Nontoxic
Very high
Unkown
Unkown
Seed
<0.01
ND
Unkown
Unkown
Unkown
Fruit
<0.01
Nontoxic
High
Possibly
Possibly
Tuber
0.01-0.05
No
High
Possibly
Tissue
Content in
raw material
(g/kg)
Oral
toxicity
Heat
stability
Processed
None
Possibly
Ricinus communis
(castor seeds)
Seed
1-5
Lethal
Unstable
Not for
direct
consumpti
on
Sambucus nigra
(elderberry)
Fruit
0.01
ND
Moderate
Yes
2.5. Saponins
Saponins are a complex group of compounds and consist of saponin, sugar, uronic acid or
other organic acids. Most saponins are white and amorphous powders and tastes bitter and
spicy. Saponins are insoluble in nonpolar solvents but are soluble in water-containing polar
solvents. Saponins can irritate the mucous coat of digestive tract and lead to local hyperemia,
316
Tissue
Content in
raw
material
(g/kg)
Oral
toxicity
Heat
stability
Processed
Seed
0.1-0.5
Nontoxic
Unstable
No
No
Seed
0.5-2
ND
ND
Unknown
Unknown
Fruit
<0.01
ND
ND
Possibly
Unknown
Fruit
<0.01
ND
ND
Unknown
Unknown
Saponins are widely distributed in plants as well as in some marine animals. The reports
on saponins-induced food poisoning are emerging in recent years. For example, poisoning
caused by the ingestion of improperly cooked kidney bean is quite common in China and
saponins have been confirmed as a cause of the poisoning. One of the most intensively
studied saponins is tea saponins and their structure, composition, and physiologicalbiochemical properties have been well elucidated. The following describes the structure,
properties, and toxicity of saponins by taking tea saponins as an example.
R1-barrigenol
Theasapogenol B
Theasapogenol D
A1-barrigenol
303~308
284~288
285~286
285~287
Molecular
weight
506
490
474
490
Empirical formula
C30H50O6
C30H50O5
C30H50O4
C30H50O5
Toxicants in Foods
R1-barrigenol
Theasapogenol D
317
Theasapogenol B
A1-barrigenol
318
Toxicants in Foods
319
TTX is an extremely toxic natural toxin and is roughly 100 times more poisonous than
potassium cyanide. The LD50 (i.v.) to mice is 8.7g/kg.
320
2.6.5. Actinotoxins
Actinotoxins are toxin derived from extracts of the tentacles of sea anemones. To present,
more than 60 kinds of cytolysin toxins have been isolated from sea anemones. Cytolysins are
substances or antibodies raised by microorganisms, plants or animals that are specifically
toxic to individual cells. The molecular weights of sea anemone-derived cytolysins range
from 15000 to 20000 and can selectively bind to the lipids on cell membranes, causing pain,
inflammation, and muscular paralysis. The most intensively studied actinotoxin is the
cytolysin isolated from anthoplerin. The molecular weight of the cytolysin is 17000 and is
characterized by a long hydrophobic -sheet section and 5 short hydrophobic -hydrophobic
sections in the N terminal, in which, 60%-70% of amino acids are hydrogen bonded and form
a transmembrane structure. The C terminal is highly hydrophilic and locates on the outside
surface of membrane, which forms a transmembrane channel.
Figure 10-9. Structures of OA and DTX-1, and DTX-2. OA: R1=CH3, R2=H, R3=H, DTX-1: R1=CH3,
R2=CH3, R3=H, DTX-2: R1=H, R2=CH3, R3=H.
2.6.6. Conotoxins
Conotoxins (CTXs) are a group of neurotoxic peptides isolated from the venom of the
marine cone snail, genus Conus. CTXs are highly poisonous to human body and the
selectivity varies with the living habits of cone snails. Among the CTXs identified, that
isolated from Conus gegraphus Linnaeus is the most poisonous.
The structures of more than 100 CTXs have been elucidated. A majority of CTXs
characterized from venoms so far are 1230 amino acids (AA) in length and contain one or
more disulfide bonds. CTXs are initially translated as propeptide precursors, approximately
80100 AA and the biologically active toxins are produced by proteolytic cleavage from the
precursors. Conotoxins can act on a wide range of targets and are highly tissue specific. CTXs
have been used as probes in the classification and identification of ion channels and receptors.
CTXs are potential drugs or leading compounds for new drug development.
Toxicants in Foods
321
2.6.7. Cyanotoxins
Cyanotoxins are produced by cyanobacteria (also known as blue-green algae). The
mechanisms of cyanobacterial toxicity currently described and understood are very diverse
and range from hepatotoxic, neurotoxic and dermatotoxic effects to general inhibition of
protein synthesis. Cyanotoxins fall into three broad groups of chemical structure: cyclic
peptides (including microcystins and nodularins), alkaloids (including neurotoxic anatoxins
and saxitoxins, cytotoxic cylindrospermopsin and demethoxy-cylindrospermopsin, and
dermatotoxic aplysiatoxins and lyngbyatoxin) and lipopolysaccharides.
322
Living bodies do not show deficiency for non-essential metals, such as Be, Hg, Pb, and
Sb. However, once the contents of these metals exceed certain thresholds, toxicity symptoms
appear.
Toxicants in Foods
323
324
Figure 10-5. Substitution reactions between phosphoryl compounds and nucleophilic agents.
Alkylation
As mentioned above, when a nucleophilic agent attacks the -C of the phosphate group,
the alkyl group is detached from the phosphate and the phosphate anion and alkylated
compound are generated. Many nucleophilic reagents can react with phosphoryl compounds
for alkylation. For example, amine compounds and sodium iodide have been used in the
production of demethylated derivatives of organophosphorous pesticides. Many sulfide
compounds, such as dithiophosphates, dithiocar-bamates, thiol, thioether, thiocyanates, and
thiourea are dealkylation agent of phosphates.
Oxidation and reduction
Oxidation of P=S to P=O is an important reaction for organophosphorous pesticides.
Oxidation increases the activity of pesticides, because the resultant products are strong
cholesterase inhibitors. Hydrogen nitrate, hydroxides, bromine water, peroxides, and many
peroxides catalyze the oxidation of organophosphorous pesticides. It should be noted other
groups on ester groups and side chains are also easily oxidized during P=S oxidation.
Reduction often leads to activity loss. For example, the S atom of the P=S bond can be
reduced to hydrogen sulfide when boiled in 48% bromic acid. The resultant hydrogen sulfide
can react with dimethyl-p-phenylenediamine and ferric chloride to produce methylene blue.
This reaction has been used to detect the presence of diazinon, rogor, and azinphos methyl.
Toxicants in Foods
325
The nitro group in the benzene ring of parathion, fenitrothion, and ethyl-p-nitrophenyl
can be easily reduced to amine and the reducing products are no longer effective.
Photo and thermal degradation
3.2.3. Pyrethroids
Pyrethroids are high-efficay and low-toxicity insecticides and acaricides. Pesticides of
this category include deltamethrin, prallethrin, cyphenothrin, and cyhalothrin. The effective
doses of pyrethroids are less than 10 gram per hectare. In environment, pyrethroids are
destroyed mainly by photo degradation (leading to isomerization, ester linkage breakdown,
and dehalogenation), followed by hydrolysis and oxidation. However, insects can evolve
resistance to pyrethroids in a short time. Hence, pyrethroids are often used together with other
pesticides to reduce the resistance issue.
Pyrethroids are divided into two groups based on their chemical structure and action
mechanism. Group I pyrethroids do not contain the cyano group. Commonly used group I
pyrethroids include allethrin, bifenthrin, tetramethrin, ethofenprox, and permethrin. Group I
326
3.2.4. Carbamates
Pesticides of this category include tricarnam, aldicarb, bufencarb, carbofuran, methomyl,
and propoxur. Carbamates are characterized by quick action, high selectivity, low toxicity to
homothermal animals, fishes, and human, easy degradation by soil microorganisms, and less
accumulation in organisms. Carbamates exert their toxicity as cholinesterase inhibitors, which
is similar to that of organophosphorous pesticides. After carbamates are hydrolyzed, the
activity of cholinesterase can be partially restored.
3.3.1. Dioxins
Dioxins are a group of planar aromatic hydrocarbons that are substituted by multiple
chlorides and share similar structure and physic-chemical properties. Dioxins are oxygen
containing chlorinated tricyclic aromatics. Seventy five PCDDs and 135 PCDFs have been
defined as dioxins. The most intensively studied toxic dioxins are 17 congeners, whose H
atoms in positions 2, 3, 7, and 8 are substituted by chloride. 2,3,7,8-Tetrachlorodibenzo-p-
Toxicants in Foods
327
dioxin (TCDD) is the most toxic dioxin among all known congeners (oral LD50 1g/kg bw).
TCCD is highly carcinogenic and can interfere in endocrine in extremely low concentrations.
Dioxins are the by-product of combustion and various industrial processes. The sources of
environmental dioxins include chlorphenols used in wood preservation and blood fluke
prevention, combustion, defoliant, insecticides preparation, paper bleaching, and automobile
exhaust.
328
PCDD/Fs are resistant to physical, chemical, and biochemical degradations and can
persist in environment. UV light can rapidly destroy PCDD/Fs. However, PCDD/Fs in air are
absorbed on gasoloid particles and hence quite resistant to UV degradation. In soil, PCDD/Fs
are stable against physical, chemical, and biological degradation and the average half life
reaches 9 years.
3.3.4. Toxicity
PCDD/Fs are extremely toxic. In contrast to common acute toxicants, death occurs
several weeks post PCDD/Fs intake. After ingestion, the body weight of animals decrease
sharply in the early phase, accompanied by emaciation syndromes, including significant
muscle and fat tissue reduction. The uptake of sublethal dose leads to body weight loss and
the effect is dose dependent.
In experimental animals, sublethal dioxin induces thymic atrophy by reducing the number
of lymphocytes in thymic cortex. According to published researches, human thymus is also
sensitive to dioxins. A characteristic symptom of dioxin poisoning is chloracne [12].
Chloracne can cause skin accretion or hyperkeratosis [13] and pigmentation [14].
Dioxins are hepatoxic. Dioxins in high levels cause liver enlargement and subsequent
degeneration and necrosis in experimental animals. Besides, dioxins have reproductive
toxicity and carcinogenicity. It is reported that dioxins stimulate the hydroxylation of
dihydrotheelin and decrease the dihydrotheelin concentration in blood. Dioxins can change
the morphology of testis and affect the formation of sperm. The strong carcinogenicity of
2,3,7,8-TCDD has been evidenced in rodents and the minimum dosage for liver cancer in
mice is as low as 10 pg/kg body weight.
329
Toxicants in Foods
The antibacterial potency of penicillins is related to the stability of the lactan ring, in
which, the peptide bond can be broken by acids, bases, heavy metals or penicillin enzymes,
causing activity loss. Figure 10-8 and Figure 10-9 illustrate the hydrolysis of penicillins under
acidic and alkali conditions.
Chemical name
Side chain R
Molecular
weight of
sodium salt
Melting
point (C)
Penicillin F
2-pentene penicillin
CH3-CH2CH=CH-CH2-
334.2
204~205
Penicillin G
benzylpenicillin
356.4
215
Penicillin X
p-hydroxybenzylpenicillin
372.4
228~235
Penicillin K
n-heptylpenicillin
CH3-(CH2)5CH2-
364.3
Dihydropenicillin F
n-Amyl penicillin
CH3-(CH2)3CH2-
336.3
Penicillin V
phenoxymethylpenicillin
372.4
120~128
330
Toxicants in Foods
331
Tetracyclines are amphoteric. Tetracyclines and their salts are yellow or light yellow
crystals and are extremely stable in dried state. They are soluble in diluted acid and alkaline
solutions, slightly soluble in water and lower alcohols, and insoluble in ethers or petroleum
ether.
332
Although female and male hormones have different functions in human body, they share
quite similar structure. Both female and male hormones are derived from cholesterol and can
be converted to each other.
Toxicants in Foods
333
metabolic enhancers (hormones), Chinese herbal medicines, biological products, and others.
According to preparation methods, fishery drugs are divided into chemical drugs, biological
drugs, biochemical drugs, and feed additives.
4. ANTI-NUTRIENTS IN FOODS
The nutritional values of animal- and plant-derived foods are determined by the
nutritional composition of their edible parts. However, to meet the requirements for growth,
propagation, and protection against invasions of microbes and predators, animals and plants
have evolved effective protection systems, such as morphology change and chemical
secretion. Besides, the accumulation of proteins or protein complexes in seeds or other edible
parts is another measure against external attacks, such as enzyme inhibitor, amylase inhibitor,
and sugar-binding proteins. These compounds are collectively termed anti-nutrients. If antinutrients are present in high levels, the adsorption and utilization of nutrients in foods will be
affected.
Phytic acid is contained mainly in the seed, stem, and root trunk of plants and the highest
content is found in the seed of legumes and the bran and embryo bud of cereals. Phytic acid
can react with Ca, Fe, Mg, Zn, and other elements to form insoluble products and reduce their
bioavailability. In addition, phytates also form complexes with proteins. Phytic acid occurs
widely in plant-derived foods and is a main anti-nutrient that affects mineral absorption.
Each phytic acid molecule has 12 dissociable protons, of which, 6 protons are highly
acidic (pKa=1.84) and are completely dissociated in water, 2 protons are weak acidic groups
334
(pKa=6.3) and the rest 4 protons are extremely weak acidic groups (pKa=9.7). Phytic acid can
complex with most metals and the stability of the complexes is closely associated with the
acidity of foods and the properties of metals. For example, the stability of some essential
metal-phytic acid complexes in pH 7.4 is Cu2+ > Zn2+ > Co2+ > Mn2+ > Fe3+ > Ca2+. The
complexes of phytic acid with proteins, Ca2+, and Mg2+ are water-soluble, whereas those with
most heavy metals are only slightly water soluble.
Due to the high contents in plant-derived foods, phytic acid can bind to endogenous Zn,
Cu, and other metals in pancreatic juice and bile that are secreted by organs to small intestine.
Hence, phytic acid not only affects the bioavailability of food-derived trace elements, but also
hinders the re-adsorption of endogenous trace elements.
Phytic acid has strong chelating capability. Each phytic acid molecule contains six
negatively-charged phosphate groups and can complex with proteins as well. When the
medium pH is lower than the pI of a protein, the protein carries positive charges. Due to
strong electrostatic interaction, the protein binds to negatively-charged phytic acid and
insoluble complex is formed. When the medium pH is higher than the pI of a protein, the free
carboxyl groups and the unprotonated imidazolyl in histines are negatively charged. In this
case, the protein forms a ternary complex with phytic acid by using Ca2+, Mg2+, or Zn2+ as the
bridge. The formation of the ternary complex reduces the solubility of proteins and
consequently decreases protein digestibility. For example, casein completely dissolves in pH
2 medium. If phytic acid is added, casein is nearly completely precipitated. The same effect
also applies to proteins extracted from corn, sunflower seed, soybean meal, and rice bran.
However, after phytic acid is degraded by phytase, the solubility of the proteins increase
tremendously and some even exceed the original values, such as the proteins derived from
fine rice bran and rapeseed.
3C2O4
20
[Fe(C2O4 )3 ]3 ( Kf=1.0610 )
Toxicity
Intake of excessive oxalic acid leads to urethral calculus and reduces the bioavailability
of essential minerals.
Toxicants in Foods
335
4.2. Polyphenols
Polyphenols are widely distributed in plant-derived foods, but their species and contents
vary significantly. Due to the presence of multiple hydroxyl groups, polyphenols are
susceptible to oxidization and are natural antioxidants in foods. Besides, polyphenols have
free radical scavenging, bacterostasis, and cancer prevention functions. Hence, polyphenols
are known as functional components in foods. However, polyphenols can complex with some
essential trace elements, precipitate proteins, and inhibit the activities of certain enzymes. In
this sense, polyphenols are natural anti-nutrients.
336
the most chemically active among polyphenols. Polyphenols are unstable and are easily
destroyed by high pH, high temperature, and high oxygen concentrations. Besides, oxidases,
oxidants, and metal ions also affect polyphenol stability.
Toxicants in Foods
337
Figure 10-17. Relationship between catechin content and protein adsorption in fermented sorghum
products [16].
When positions 3 and 4 in ring B of flavones are connected with OH, the flavones can
easily form quinoid oxidates by enzymatic and automatic oxidation. The quinoid oxidates can
complex with GSH, as shown in Figure 10-19.
338
4.3.1. Properties
Protease inhibitors are widely present in microbes and the tissues of plants and animals.
Legume seeds have higher protease inhibitor contents than other sources. Protease inhibitors
derived from legume seeds are divided into the Kunitz type and the Bowman-Birk type.
Kunitz protease inhibitors have relatively higher molecule weights of about 20000 Dal and
specifically bind to trypins. Bowman-Birk protein inhibitors have lower molecule weight of
about 9000 Dal and two binding sites. Hence, Bowman-Birk protease inhibitors can bind two
serine proteases, trypins, or chymotrypsins at the same time. Kunitz protein inhibitors are
sensitive to heat treatment, but Bowman-Birk protein inhibitors are quite heat resistant.
Protein inhibitors of difference sources are quite similar in amino acid composition. That
is, cystine has the highest content, followed by aspartic acid, arginine, lysine, and glutamic
acid in sequence. The high content of cystine facilitates the formation of intra-molecular
disulfide bonds, which make the inhibitors heat and acid resistant.
4.3.2. Action Mechanism
Digestive enzyme inhibitors inactivate proteases by forming complexes with enzymes.
The action mechanism of digestive enzyme inhibitors is elucidated by taking trpsin inhibitor
(LTI) as an example. LTI is mainly found in legume Leucaena leucocephala and belongs to
the Kunitz family.
Toxicants in Foods
339
340
"TO
"TO
b)
Figure 10-21. (a) Stereoview of the Ca-atom backbone of STI (a) and LTI (b). Only the positions of
Arg63 and Asn11 are indicated in the structures.
(b)
Interaction between Arg62 (P1) of LTI and S1 residues of trypsin (shown in pink color) [18].
Associated type: Inhibitors do not occupy the recognition sites of target enzymes. Instead,
the inhibitors associate with target enzymes for hydrogen bonding with the active groups of
target enzymes and block the substrate binding site. The interactions between thrombin
inhibitors, such as hirudin, and their substrates are of this type.
Covered type: Inhibitors cover the areas close to the active center of target enzymes as
linear molecules to prevent the contact between active center and substrate. For example,
papain inhibitor is of this type.
Toxicants in Foods
341
significantly affect the flavor, color, shelf life, and safety of lipid-containing foods. Many
diseases have been associated with lipid oxidation and their thermal products.
342
()P has the most significant effect on food safety among PAHs. To date, a total of more than
two hundred kinds of PAHs and PAH derivates have been identified and many of them are
extremely carcinogenic and mutagenic. Figure 10-24 shows the structures of some common
PAHs. Of the PAHs, 3,4-benzo()pyrene is the most widely distributed and is highly
carcinogenic. 3,4-Benzo()pyrene is often regarded as the representative of PAHs.
Figure 10-23. Structure of PCBs. (left) PCB; (right) chlorinated dibenzofuran (X can be substituted
by chlorine).
Phenanthrene
Bezo()anthracene
Pyrene
Triphenylene
Diabenzo(a,i) pyrene
Bezo()pyrene
Toxicants in Foods
343
incidence of cancer and shortened incubation period. In the case of mice, injection of 4-12 g
benzo()pyrene induces cancer and the half carcinogenic dosage is 80 g.
The carcinogenicity of PAHs is associated their chemical structures. Carcinogenicity is
only observed in PAHs with four to seven benzene rings. PAHs with less than four or more
than seven rings are not carcinogenic. Population and epidemiological investigations indicate
that benzo()pyrenes and other PAHs can be absorbed through respiratory tract, digestive
tract, and skin. B-()P can cause gastric cancer, lung cancer, or skin cancer in human. Iceland
has the third highest incidence of gastric cancer and the reason has been associated with
smoked foods in the diet of Iceland residents. Besides, the incidences of gastrointestinal tract
and respiratory tract cancers are three times higher than those of inland populations. The
carcinogenic incubation period of benzo()pyrene in human beings ranges from 20 to 25
years.
344
Molecular weight
198.2
212.3
213.2
213.2
227.3
224.3
183.2
197.2
211.3
197.2
198.2
184.2
170.2
Formula
C11H10N4
C12H12N4
C11H11N5
C11H11N5
C12H13N5
C13H12N4
C11H9N3
C12H11N3
C13H13N3
C12H11N3
C11H10N4
C10H8N4
C11H10N2
UVmax (nm)
264
257
264
264
266
315
339
345
263
265
364
367
264
pKa
3.8, 6.6
3.9, 6.4
<2, 6.3
<2, 6.3
<2, 6.3
5.7
4.6
4.9
8.6
8.5
6.0
5.9
6.5
Content in foods
According to published reports, nearly all foods contain acrylamide. The acrylamide limit
of WHO in tape water is 0.5 g/kg (1993). However, investigations reveal that the acrylamide
contents in foods that are rich in carbohydrates and processed by frying or roasting are much
higher than the allowed value in tap water. For example, the average content of acrylamide in
fried potato chip (slice) is 1000 g/kg and that in infant biscuit is 600-800 g/kg.
Acrylamide is mainly found in foods that are processed in temperatures higher than 120
C. High contents of acrylamide have been detected in most fried potato chips, part bread,
cocoa powder, apricot kernel, coffee, and biscuits.
Generation pathway
The mechanism of acrylamide formation in heat-processed foods is still not well
understood. It is recognized that acrylamide is generated through the Maillard reaction and
the compounds involved include carbohydrates, proteins, amino acids, lipids, and other minor
components in foods [21]. The possible mechanism is as follows: amino acids react with
reducing sugars to produce dicarbonyl compounds and the products then react with amino
acids to yield acrylaldehyde. Acrylaldehyde is oxidized to acrylic acid and acrylic acid is
finally converted to acrylamide in the presence of amine or amino acids. Figure 10-27
illustrates the general pathway of acrylamide formation. It is reported that acrylamide can be
directly converted from amino acids. In addition, many organic acids, such as malic acid,
lactic acid, and citric acid, also participate in the formation of acrylamide.
According to current data, the following conclusions can be drawn:
(1) Amino acids are degraded in high temperatures and the degradation products react
with reducing sugars to produce acrylamide;
(2) The primary reaction product N-glucoside of the Maillard reaction plays important
role in acrylamide formation;
(3) -Dicarbonyl compounds react with amino acids to release acrylamide;
Toxicants in Foods
345
346
(4) Strecker degradation facilitates the formation of acrylamide, because aldehydes are
generated during the degradation;
(5) Free radicals might also involve in acrylamide formation;
(6) More than one pathway might contribute to acrylamide formation.
In addition to intrinsic formation during food processing, acrylamide might come from
other sources. Acrylamide can immigrate from polyacrylamide-based packaging materials to
foods or from flocculating agent.
Toxicants in Foods
347
348
In N-nitroso compounds, if groups R1 and R2 are the same, the compounds are
symmetric; otherwise, the compounds are asymmetric. R1 and R2 can be alkyl groups, such as
N-nitrosodimethylamine (NDMA) and N-nitrosodiethylamine (NDEA), aromatic
hydrocarbons, such as N-nitrosodiphenylamine (NDPhA), naphthenic bases, such as Nnitrosopyrolidine (NPRY), N-nitrosomorpholine (NMOR), N-nitrosopiperidine, and Nnitrosopiperazine, and amino acids, such as N-nitrosoproline (NPRO) and N-nitrososarcosine
(NSAR).
Low-molecular weight nitrosamines are yellow liquid in room temperature, and most
high-molecular weight nitrosamines are solid. Most nitrosamines are insoluble in water,
except some N-nitrosamines, such as NDMA, NDEA, and some N-nitroso amino acids. All
N-nitrosamines are soluble in organic solvents and are stable against spontaneous hydrolysis.
N-nitrosamines can be converted to carcinogenic compounds after being metabolized in
human body.
R1
N
5.3. Chloropropanols
With the increase of demand on flavorings, the soy sauce processing technique undergoes
large evolutions during recent years. Hydrolyzed vegetable proteins have been used in soy
sauce production to improve quality and reduce cost. If the hydrolysis condition is not well
controlled, toxic chloropropanols may be generated. Chloroproanols can cause cancers in
liver, kidney, and thyroid and affect fertility. Chloropropanols have turned to be another
hotspot in the food pollutant area in addition to dioxins.
Toxicants in Foods
349
350
5.4.1. Plastics
Plastics are made from synthetic resins and supplementary materials. Plastics and
synthetic resins are polymerized from small blocks and the higher polymerization degree, the
more stability and the less possibility of block migration into foods. If a polymer is
synthesized from only one block, this polymer is a homopolyer; if two or more blocks are
used, the polymer is a copolymer.
Plastics that are currently allowed for food packaging include polyethylene (PE),
polypropylene, polystyrene, urea formaldehyde, and melamino-formaldehyde. These
materials are potential pollutants for foods. For example, polyvinyl chloride (PVC) is
nontoxic, but the monomer vinyl chloride and its degradation products are toxic. PVC can be
degraded by high temperature and UV light and the decomposition product can cause hepatic
hemangioma. Free formaldehyde may exist in urea formaldehyde and melaminoformaldehyde plastics in case of incomplete reaction during production. Besides, urea
formaldehyde and melamino-formaldehyde can be degraded by high temperature and acidic
solutions to release formaldehyde and phenols. Formaldehyde is a protoplasmic poison and
can cause focal necrosis of liver cells and lymphocytic infiltration if orally ingested by
animals.
5.4.2. Other Packaging Materials
Ceramic glazes or porcelain glazes that are coated on chinas and ceramics contain high
levels of metallic salts, such as lead salts and cadmium salts. If the salts get in contact with
foods for long periods, the salts dissolve in foods and poisoning occurs. The salts are readily
soluble in acidic foods such as vinegar, fruit juices, and wines.
Packaging paper used in food packaging cannot contain fluorescent brightener.
Regenerated paper can cause potential microbial pollution in foods and recycled paper can
lead to toxic substance contamination in foods. Paraffin used in paraffin paper must be pure
and the contents of polycyclic aromatic hydrocarbons cannot exceed allowed values.
Tinplate cans are widely used for packaging foods and beverages. Metal pollutions
caused by food packaging materials and food containers are attracting more and more
attentions in recent years. Ai et al [22] measured the contents of toxic metals in tinplate alloys
by using ICP-AES and found that the alloys have high toxic metal contents, especially Pb,
Cd, Cr, and Sn. Hence, how to control the contents of toxic elements in foods and reduce their
potential damages deserves more attention.
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the safety of foods produced by genetic modification. Regulatory Toxicology and
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[3] Chernoff, R. Thirst and fluid requirements. Nutrition Reviews, 1994, 52, S3S5.
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[5] Tewe, OO; Lyayi, EA. 1989. Cyanogenic glycosides. In: Cheeke PR. Toxicants of Plant
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[6] Fenwick, G.R, et al., Glucosinolates and their breakdown products in food and food
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[13] Geusau, A; Khorchide, M; Mildner, M; Pammer, J; Eckhart, L; Tschachler, E. 2,3,7,8Tetrachlorodibenzo-p-Dioxin Impairs Differentiation of Normal Human Epidermal
Keratinocytes in a Skin Equivalent Model. Journal of Investigative Dermatology, 2005,
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309-316.
[15] Heim, KE; Tagliaferro, AR; Bobilya, DJ. Flavonoid antioxidants: chemistry,
metabolism and structure-activity relationships. The Journal of Nutritional
Biochemistry, 2002, 13, 572-584.
[16] Osman, MA. Changes in sorghum enzyme inhibitors, phytic acid, tannins and in vitro
protein digestibility occurring during Khamir (local bread) fermentation. Food
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[17] Han, X; Shen, T; Lou, H. Dietary Polyphenols and Their Biological Significance.
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INDEX
A
Abraham, 268, 349
accounting, 76
acetaldehyde, 255, 261, 266
acetic acid, 62, 66, 83, 206, 251, 261, 273, 286, 315
acetone, 47, 62, 67, 91, 201, 255, 261, 307, 317, 340,
341, 347
acetonitrile, 317
acetophenone, 258
acidic, 46, 48, 56, 59, 61, 66, 69, 70, 72, 74, 81, 82,
83, 95, 98, 138, 140, 145, 152, 165, 178, 184,
186, 205, 207, 208, 209, 211, 230, 232, 251, 260,
273, 279, 293, 294, 295, 296, 315, 316, 318, 321,
322, 323, 327, 328, 332, 340, 341, 348
acidity, 28, 47, 66, 98, 207, 273, 296, 306, 332
acrylic acid, 342
action potential, 324
activation energy, 31, 121, 179
active compound, 128, 258
active oxygen, 67
active radicals, 281
active site, 46
adaptability, 188
adaptation, 194, 247
additives, 158, 172, 184, 251, 271, 272, 273, 278,
279, 283, 289, 299, 319, 334
adenine, 227, 228, 261
adhesion, 159, 165, 284
adiposity, 100, 102
ADP, 227
adsorption, 50, 101, 102, 153, 159, 160, 162, 164,
165, 212, 250, 296, 304, 305, 313, 319, 331, 332,
334, 335, 340
adults, 103, 174, 176, 178, 306
advancement, 3, 40
adverse effects, 167, 305, 306, 324, 339
aflatoxin, 130, 131
agar, 88, 90, 91, 96, 100, 291, 293
354
Index
antagonism, 224
antibiotic, 328
antibody, 306
antigen, 306, 310, 311
antimony, 194
antioxidant, 61, 66, 67, 71, 126, 128, 131, 185, 189,
197, 199, 213, 215, 220, 272, 274, 279, 281, 282,
283, 296, 297, 333, 334
antitumor, 74
appetite, 251, 252, 310
apples, 71, 264, 307
aquaculture, 316
aqueous solutions, 34, 36, 51, 59, 85, 207, 210, 212,
213, 236, 279, 315, 316, 326
aqueous suspension, 84, 280
arabinogalactan, 291
arginine, 67, 68, 140, 149, 177, 336
aromatic compounds, 254, 256, 257, 258, 264, 265,
266
aromatic hydrocarbons, 194, 260, 324, 346
aromatic rings, 184
aromatics, 324
ARS, 135
arsenic, 222, 225, 239
ascorbic acid, 38, 61, 62, 63, 70, 211, 213, 219, 281,
282
aseptic, 179
Asia, 292, 295
asparagines, 345
asparagus, 74, 218, 257
Aspartame, 187, 276
aspartate, 147
aspartic acid, 140, 187, 320, 324, 336
assessment, 34, 249, 339
asthenia, 339
astringent, 46, 246, 254
atmosphere, 4, 194, 280
atmospheric pressure, 71
atomic emission spectrometry, 349
atoms, 11, 13, 41, 45, 108, 109, 126, 210, 225, 229,
230, 231, 233, 237, 308, 320, 321, 324
ATP, 202, 208, 224, 227, 228, 229, 252, 282
atrophy, 326
autolysis, 185
autooxidation, 55
awareness, 283, 294
B
bacteria, 24, 74, 93, 94, 102, 173, 181, 185, 189,
200, 206, 209, 210, 212, 230, 231, 278, 279, 280
bacterial fermentation, 276
barriers, 320
base, 31, 55, 72, 151, 209, 220, 225, 227, 272, 300,
321
beef, 108, 156, 157, 174, 179, 188, 199, 208, 210,
238, 240, 260, 261, 266, 268, 269
beer, 5, 92, 158, 162, 249, 250, 266, 295, 296
Beijing, 7, 188, 189, 243
beneficial effect, 102
benefits, 7, 28, 272, 291
benzene, 62, 201, 206, 260, 266, 315, 317, 323, 328,
333, 339, 340, 341, 347
benzoyl peroxide, 184
beriberi, 192, 202
beryllium, 222
beta-carotene, 193, 194, 196, 219
beverages, 51, 74, 75, 91, 100, 169, 247, 251, 266,
276, 277, 279, 292, 293, 294, 296, 348
bile, 94, 101, 103, 249, 250, 332
bile acids, 103
bioavailability, 9, 68, 103, 178, 179, 180, 182, 207,
212, 224, 225, 227, 236, 237, 238, 239, 305, 331,
332, 333, 334
biochemical processes, 221
biochemistry, xi, xii, 2, 3, 324
biological activity, 191, 237, 349
biological stability, 5
biomass, 5, 173
biomolecules, 26, 32, 225, 239, 320, 334
biopolymer, 9
biopolymers, 34
biosynthesis, 44, 95, 212, 234, 255, 304, 333
biotechnology, xii
biotic, 174
biotin, 209, 210
birds, 169, 303, 306
bladder cancer, 276
bleaching, 184, 241, 272, 325
bleeding, 298
blindness, 192, 194
blood, 40, 55, 94, 100, 101, 102, 149, 150, 192, 196,
198, 199, 201, 202, 210, 236, 261, 262, 275, 276,
305, 310, 316, 325, 326
blood plasma, 149
blood pressure, 102, 305
blood stream, 55, 236
body fluid, 192, 233
body weight, 310, 326
boils, 341
bonding, 10, 11, 12, 15, 16, 17, 18, 23, 27, 50, 52,
76, 79, 87, 91, 92, 101, 116, 145, 146, 153, 154,
156, 160, 165, 166, 168, 172, 248, 249, 288, 334,
337, 338
bonds, 10, 11, 13, 14, 15, 40, 42, 43, 46, 58, 76, 77,
85, 88, 98, 108, 109, 116, 124, 126, 127, 146,
147, 148, 151, 153, 155, 156, 159, 160, 166, 169,
172, 186, 230, 231, 237, 318, 336, 337
Index
bone, 150, 170, 221, 223, 224, 233, 240, 305
bone growth, 223
bone marrow, 170, 233
bones, 296
botanists, 2
bounds, 17
brain, 300
brain damage, 300
branching, 77
breakdown, 58, 86, 124, 166, 184, 300, 313, 321,
323, 349
breast milk, 134, 180
bromine, 222, 322, 340
buns, 173, 296
burn, 116, 277
by-products, 272
C
Ca2+, 14, 39, 41, 81, 87, 90, 92, 98, 102, 164, 167,
178, 227, 235, 237, 332, 334
cabbage, 10, 200, 215, 218, 240, 304
cacao, 249, 298
cadmium, 222, 348
caffeine, 68, 249, 250
calcification, 196
calcium, 39, 74, 91, 92, 95, 170, 188, 192, 196, 207,
221, 222, 278, 279, 288, 291, 292, 294, 296, 297,
304, 307, 326, 332
calculus, 239, 333
calorie, 85, 86, 100, 277, 290
cancer, 100, 276, 291, 320, 333, 339, 340, 341
cane sugar, 24
capillary, 51, 168
carbohydrate, xi, 40, 54, 55, 76, 84, 170, 181, 184,
207, 225, 226, 289, 310, 312, 333, 341, 345
carbohydrates, vii, xii, 1, 3, 5, 7, 32, 35, 36, 37, 46,
50, 51, 54, 58, 63, 66, 73, 100, 102, 103, 172,
184, 202, 217, 225, 226, 229, 236, 243, 260, 268,
342, 345
carbon, 28, 36, 37, 46, 49, 62, 63, 90, 92, 94, 102,
108, 109, 110, 111, 115, 116, 121, 122, 130, 131,
132, 143, 145, 163, 203, 210, 215, 222, 229, 253,
261, 298, 315, 323, 328, 333, 340, 347
carbon atoms, 36, 37, 90, 108, 109, 143, 229, 328
carbon dioxide, 28, 36, 102, 163, 261, 323
carbon tetrachloride, 92, 347
carbon-centered radicals, 215
carbonyl groups, 49, 72, 181, 345
carboxyl, 36, 37, 44, 48, 52, 53, 84, 102, 138, 141,
165, 211, 225, 231, 232, 234, 235, 332
carboxylic acid, 108, 138, 143, 214, 225, 227, 260,
264, 282
carboxylic acids, 138, 214, 260, 282
355
356
Index
Index
cysteine, 71, 140, 144, 166, 179, 184, 232, 256, 257,
266, 267, 310, 320, 328
cystine, 165, 166, 179, 182, 184, 233, 320, 336
cytochrome, 223, 230, 324
cytoplasm, 316
D
damages, 348
D-amino acids, 248
danger, 278, 282
DDT, 321
deacetylation, 93, 295
decay, 93, 274, 275
decomposition, 5, 6, 102, 116, 124, 125, 194, 203,
205, 207, 254, 259, 260, 261, 262, 268, 272, 281,
348
defecation, 101
defects, 13
deficiency, 173, 191, 192, 194, 196, 197, 198, 201,
202, 205, 208, 209, 210, 212, 213, 214, 222, 224,
238, 273, 319, 320
deformation, 29, 51, 118, 165, 284
degradation, 5, 6, 56, 57, 65, 66, 68, 71, 129, 181,
182, 184, 194, 195, 196, 199, 202, 203, 204, 205,
207, 208, 209, 210, 212, 214, 216, 219, 252, 262,
266, 268, 269, 284, 320, 323, 324, 325, 326, 342,
344, 348
degradation rate, 203
degumming, 131
dehydration, 9, 21, 22, 36, 58, 59, 60, 61, 66, 86,
143, 168, 179, 199, 241, 242, 253, 296
denaturation, 5, 6, 7, 137, 148, 151, 152, 153, 154,
156, 157, 159, 167, 168, 169, 172, 178, 180, 183,
184, 187, 338
dendrites, 13
dental caries, 73
Department of Agriculture, 243
dephosphorylation, 217
depolarization, 324
depression, 34, 83
derivatives, 36, 37, 49, 76, 82, 86, 107, 110, 111,
120, 138, 187, 197, 200, 208, 211, 220, 225, 226,
229, 243, 249, 269, 293, 299, 317, 322, 328, 333
dermatitis, 205, 208, 210
desorption, 22, 23, 29
destruction, 68, 151, 152, 183, 194, 205, 212, 215,
216
detectable, 152
detection, xii, 104
detergents, 285
detoxification, 71, 213, 220
developing countries, vii
deviation, 113
357
358
Index
221, 232, 239, 256, 258, 259, 262, 264, 275, 305,
307, 313, 320, 327, 333, 336, 337, 338, 339, 346
EPA, 5, 109, 112
epidemiological investigations, 341
epidermis, 316
epinephrine, 107
epithelial cells, 194, 304
equilibrium, 19, 29, 30, 138, 168, 262, 296
equipment, 3, 162, 241
essential fatty acids, 107
ester, 49, 52, 54, 90, 111, 120, 139, 140, 150, 187,
194, 256, 264, 287, 288, 292, 322, 323, 333
ester bonds, 150
ethanol, 59, 62, 64, 91, 92, 93, 100, 142, 149, 165,
171, 172, 194, 207, 209, 212, 213, 255, 266, 283,
288, 292, 293, 315, 317, 328, 333, 341, 347
ethers, 49, 254, 260, 266, 324, 326, 329
ethyl acetate, 62, 255, 259, 266, 283, 315, 328
ethylene, 93, 281, 283
eukaryotic cell, 222
evacuation, 101
evaporation, 183
evidence, 16, 276, 277
evolution, 271, 310
EXAFS, 226
excretion, 95
experimental design, 6
exploitation, 4
exposure, 17, 118, 121, 126, 153, 183, 194, 213, 234,
279, 306, 323
extraction, 7, 88, 101, 130, 168, 169, 172, 293
extracts, 289, 292, 298, 300, 318
extrusion, 7, 83, 172
exudate, 96, 98, 291
F
families, 310, 311, 312
fast food, 349
fat, 3, 5, 86, 91, 94, 100, 103, 107, 108, 111, 112,
113, 114, 118, 119, 131, 133, 134, 156, 158, 159,
161, 172, 191, 192, 193, 194, 196, 197, 199, 239,
240, 250, 260, 261, 282, 283, 284, 288, 289, 290,
292, 293, 295, 298, 317, 326
fat soluble, 191, 194, 196, 197, 317
fatty acids, xii, 16, 78, 83, 94, 102, 107, 108, 109,
110, 111, 112, 113, 114, 115, 116, 117, 120, 121,
122, 124, 126, 127, 129, 130, 131, 132, 133, 134,
182, 256, 259, 260, 261, 262, 285, 287, 288, 306
FDA, 100, 103, 187
feed additives, 331
fermentation, 5, 90, 100, 165, 173, 184, 185, 189,
254, 258, 259, 266, 267, 274, 277, 289, 294, 295,
334, 349
359
Index
ferritin, 237
fertility, 346
fever, 306
fiber, 35, 91, 100, 150, 170, 173, 291
fibers, 40, 100
films, 159, 163, 164, 165, 188
filtration, 4, 117, 131
fish, 24, 68, 92, 108, 148, 157, 169, 173, 174, 177,
178, 179, 180, 184, 185, 196, 204, 208, 212, 233,
234, 238, 261, 262, 269, 279, 283, 296, 297, 298,
300, 303, 316
fish oil, 196, 262
fission, 58
fixation, 210
flame, 179
flatulence, 73, 172
flavonoids, 45, 46, 283, 333, 334
flavour, 54, 103, 187, 293, 299, 300
flaws, 58
flexibility, 42, 52, 159, 160
flocculation, 120, 164
flora, 37, 75
flour, 10, 24, 86, 96, 165, 166, 167, 171, 172, 173,
177, 180, 184, 202, 216, 218, 219, 272, 288, 295,
296, 297, 300
fluid, 51, 85, 113, 157, 164, 169, 250, 291, 294, 348
fluorescence, 67, 104, 202, 205, 340
fluorine, 222
foals, 105
foams, 154, 158, 159, 162, 163, 164, 188, 289, 293
folate, 210
folic acid, 210, 211, 212, 215, 219
follicle, 329
food additive, vii, 5, 91, 241, 271, 272, 273, 284,
300, 346
food additives, vii, 5, 91, 241, 271, 272, 273, 284,
300, 346
Food and Drug Administration, 73
food chain, 319, 325
food industry, 1, 3, 4, 5, 6, 7, 39, 46, 48, 49, 73, 82,
85, 86, 87, 90, 91, 92, 93, 94, 97, 120, 132, 137,
168, 171, 178, 180, 184, 187, 213, 251, 271, 278,
280, 289, 291, 295, 300, 303, 347
food poisoning, 314
food production, 287, 289
food products, 297, 300
food safety, xi, xii, 2, 46, 271, 272, 296, 303, 319,
340, 347
food security, 3
food spoilage, 272
food web, 324
foodborne illness, 317
force, 17, 95, 101, 146, 147, 163, 168, 169
formaldehyde, 182, 210, 261, 262, 348
formula, 19, 37, 40, 41, 59, 75, 93, 141, 234, 314,
316, 317, 340
free energy, 119, 120, 141, 159, 284
free radicals, 26, 103, 121, 126, 128, 130, 182, 199,
205, 233, 281, 334
free rotation, 42
free volume, 31, 32
freezing, 2, 6, 13, 20, 28, 34, 45, 83, 84, 117, 240,
308
freshwater, 261, 316
friction, 152, 169
fructose, 4, 36, 47, 48, 49, 50, 55, 57, 59, 60, 74, 75,
82, 181, 225, 248, 274, 275, 276, 345
fruits, 4, 7, 18, 21, 24, 36, 55, 74, 87, 93, 95, 108,
195, 213, 219, 237, 245, 249, 254, 255, 263, 264,
265, 273, 275, 279, 280, 290, 297, 304, 305
functional food, 73, 86, 94, 294, 296
fungi, 74, 193, 233, 278
furan, 124, 203, 214, 258, 259, 260, 261, 266, 268,
324
G
gallbladder, 251
gastroenteritis, 305
gastrointestinal tract, 194, 341
gel, 44, 51, 52, 53, 81, 82, 83, 84, 86, 87, 90, 91, 92,
98, 100, 167, 168, 171, 291, 292, 294, 295, 296
gel formation, 296
gelatinization temperature, 76, 80, 81, 82, 83, 84
gelation, 81, 87, 88, 98, 151, 158, 159, 160, 167,
168, 293, 297
genes, 145
genetic code, 145
genetic information, 320
genetics, 306
genitals, 198
genomics, 7
genus, 96, 98, 275, 318
geometry, 40, 41, 42, 43, 44
germination, 273
gill, 316
ginger, 253
gland, 233
glass transition, 23, 30, 32
glossitis, 210
glucoamylase, 48, 82
glucose, 36, 39, 40, 47, 48, 49, 50, 55, 59, 65, 66, 67,
68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 82, 84, 86,
97, 98, 100, 101, 181, 224, 225, 239, 248, 249,
266, 267, 274, 275, 276, 281, 282, 294, 295, 307,
328, 333, 345
glucose oxidase, 48, 72, 281, 282
glucoside, 45, 342
360
Index
361
Index
hydroxyl, 36, 37, 39, 45, 46, 48, 49, 61, 62, 63, 67,
79, 83, 88, 90, 95, 102, 110, 111, 115, 116, 129,
139, 165, 225, 231, 248, 253, 260, 264, 275, 320,
333, 334, 347
hydroxyl groups, 36, 39, 45, 46, 49, 62, 63, 79, 83,
88, 95, 102, 225, 333, 347
hygiene, 220, 272
hyperemia, 194, 313
hypersensitivity, 210
hypertension, 100, 101, 277
hypothesis, 58
hysteresis, 23
hysteresis loop, 23
I
Iceland, 341
ID, 268
ideal, 19, 94, 159, 176
identification, 5, 6, 115, 139, 318
illumination, 216
images, 3
immune reaction, 306
immune response, 306
immunity, 181
immunogenicity, 306
immunoglobulin, 180
immunoglobulins, 149
immunomodulatory, 185
immunoreactivity, 306
immunostimulatory, 74
impurities, 115, 116, 130, 131, 132, 133
in vitro, 349
in vivo, 72, 113, 148, 208, 240, 326
incidence, 73, 102, 210, 276, 306, 330, 341
incubation period, 341
India, ix, 107, 246
individual differences, 103
individuals, 102, 245, 246, 284, 304, 330
induction, 67, 121
induction period, 67, 121
industrial processing, 179
industries, 74, 87, 95, 133, 325
industry, 4, 5, 7, 90, 173, 179, 188, 251, 271, 294,
295, 297, 316, 347
infants, 155, 178, 180, 298, 300, 306
infertility, 198
inflammation, 192, 194, 208, 214, 314, 318
infrared spectroscopy, 225
ingestion, 75, 101, 102, 186, 247, 304, 305, 314,
316, 320, 326
ingredients, 5, 7, 37, 53, 73, 82, 94, 158, 265, 283,
288, 289, 290, 294, 296, 300
inhibition, 5, 67, 68, 91, 93, 304, 305, 319, 322, 347,
349
inhibitor, 67, 177, 183, 331, 335, 336, 337, 338, 349
initiation, 46, 116, 121, 124, 126
injury, 304, 308, 316
inositol, 38, 39, 111, 283, 328, 331
insecticide, 241
insects, 73, 174, 303, 321, 323
insertion, 44
insomnia, 305
instant noodles, 173
insulin, 147, 224
integrity, 194, 221
intercellular adhesion molecule, 213
interface, 119, 120, 125, 153, 154, 159, 160, 162,
163, 164, 169, 185, 284
interference, 44, 304
international law, 272
interphase, 160
intervention, 58
intestinal tract, 192
intestine, 37, 55, 94, 102, 103, 185, 313
invasions, 331
inversion, 161
investment, 173
iodine, 5, 129, 194, 222, 304
ion channels, 318
ionization, 153, 154, 168
ionizing radiation, 153
ions, 11, 14, 26, 70, 81, 87, 88, 91, 94, 98, 99, 102,
138, 158, 164, 178, 188, 216, 225, 230, 233, 234,
237, 281, 291, 308, 326
Iran, 96
iron, 60, 93, 150, 180, 212, 224, 230, 233, 237, 238,
281, 282, 298, 304
irradiation, 184
irreversible aggregation, 155
irritability, 178, 254
isoflavone, 333
isoleucine, 140
isomerization, 7, 48, 58, 66, 75, 122, 194, 250, 253,
323
isomers, 37, 39, 49, 113, 122, 124, 133, 135, 141,
195, 219, 248, 253, 287, 324, 328
isoprene, 265
isotherms, 22
isotope, 13
K
K+, 14, 81, 90, 91, 98, 102
kaempferol, 333
keratin, 32
362
Index
ketones, 37, 58, 60, 66, 69, 124, 129, 181, 184, 187,
214, 256, 258, 259, 260, 261, 263, 264, 266, 280,
308
kidney, 177, 196, 206, 210, 218, 233, 236, 304, 307,
312, 314, 330, 346, 347
kidney failure, 196
kinetic model, 104
kinetics, 34
L
labeling, 139, 300
lactase, 73
lactase deficiency, 73
lactic acid, 3, 66, 143, 173, 181, 185, 189, 202, 251,
280, 287, 288, 342
lactobacillus, 74, 295
Lactobacillus, 24, 74, 104
lactoferrin, 180
lactose, 50, 66, 67, 70, 73, 75, 304, 345
lactose intolerance, 73
lakes, 299
lamella, 164
lanthanum, 225
large intestine, 100, 102
lead, 70, 121, 129, 164, 167, 168, 177, 178, 179,
183, 217, 218, 236, 275, 305, 307, 310, 313, 316,
319, 321, 324, 345, 348
leakage, 93, 316
leaks, 251
lecithin, 110, 111, 283, 286, 289
legs, 317
legume, 76, 309, 310, 312, 336
lesions, 212
leucine, 67, 68, 140, 255, 264
Lewis acids, 225
ligand, 39, 46, 225, 237, 314, 320
light, 63, 88, 91, 92, 94, 121, 126, 141, 161, 192,
193, 194, 196, 197, 205, 206, 207, 209, 210, 211,
253, 261, 279, 323, 329
light scattering, 161
lignin, 85, 100, 269
linear molecules, 53, 338
linear polymers, 166
linoleic acid, 67, 108, 109, 110, 111, 112, 113, 114,
124, 126, 127, 133, 258, 259, 263, 264
lipases, 121
lipid metabolism, 192
lipid oxidation, 6, 26, 67, 103, 115, 121, 126, 128,
131, 184, 186, 199, 217, 260, 268, 273, 282, 339,
345
lipid peroxidation, 320
lipoid, 182
lipoproteins, 17, 150
363
Index
MCP, 296
measurement, 67, 119, 246
meat, 5, 10, 24, 49, 53, 66, 68, 72, 91, 92, 93, 98,
142, 143, 148, 158, 162, 169, 178, 179, 182, 184,
186, 208, 212, 260, 268, 274, 279, 283, 288, 293,
296, 297, 298, 300, 305, 346
mechanical stress, 163
media, 60, 71
medical, 220, 277
medication, 180
melt, 20, 117, 119, 212, 293
melting, 12, 30, 59, 111, 112, 116, 117, 118, 119,
132, 134, 162, 167, 201, 207, 209, 293, 325, 341
melting temperature, 341
melts, 59, 118, 119, 194, 201, 205, 207, 213, 328,
341
membranes, 93, 120, 246, 320, 324
mercury, 222
metabisulfite, 279
metabolism, 101, 177, 192, 196, 200, 202, 205, 207,
209, 223, 236, 239, 269, 275, 304, 305, 310, 329,
349
metabolites, 102, 107, 304, 326, 330
metabolized, 101, 187, 224, 306, 329, 330, 346
metal complexes, 243, 282
metal ion, 68, 92, 103, 128, 129, 150, 213, 214, 225,
237, 273, 281, 296, 320, 334
metal ions, 68, 92, 103, 128, 129, 213, 214, 225,
237, 273, 281, 296, 320, 334
metal salts, 155, 239
metalloenzymes, 223, 232, 237, 239, 320
metals, 70, 126, 133, 155, 184, 225, 233, 234, 235,
237, 239, 305, 319, 320, 325, 332, 334, 347
methanol, 12, 62, 91, 315, 317, 328, 333, 341
methodology, 22
methyl cellulose, 295
methylation, 333, 334
methylcellulose, 86
methylene blue, 322
Mexico, 277
Mg2+, 14, 39, 98, 164, 227, 230, 237, 251, 332, 334
mice, 240, 300, 317, 326, 339, 341
microbial cells, 95
microcrystalline, 80, 85
microcrystalline cellulose, 85
micrograms, 192
microorganism, 23, 101, 278, 294, 323
microorganisms, 1, 9, 18, 20, 24, 26, 31, 35, 72, 101,
102, 173, 181, 184, 185, 207, 210, 212, 213, 251,
273, 278, 303, 310, 318, 324
microscope, 79
microscopy, 78
microstructures, 18
migration, 6, 21, 29, 153, 348
milligrams, 192
Ministry of Education, xi
mixing, 16, 165, 280, 289
model system, 63, 64, 66, 70, 71, 104, 184, 349
modelling, 349
models, 6, 78, 220, 229
modifications, 76, 82, 182, 187, 239
modified Clausius-Clapeyron equation, 19
moisture, 9, 18, 19, 21, 22, 23, 24, 25, 26, 29, 30, 31,
32, 50, 61, 172, 178, 180, 181, 184, 293, 296
moisture content, 21, 23, 31, 32, 180, 184
moisture sorption, 9, 21, 22, 25
molasses, 24, 274
mold, 173, 279
molds, 24, 26, 95, 279, 280
mole, 15
molecular biology, 2
molecular mass, 285
molecular mobility, 9, 23, 28, 29
molecular oxygen, 334
molecular structure, 169, 225, 310, 312
molecular weight, 32, 33, 39, 40, 46, 51, 52, 54, 58,
63, 68, 77, 85, 90, 92, 93, 94, 95, 96, 98, 129,
141, 159, 161, 166, 170, 171, 172, 178, 184, 185,
186, 187, 229, 233, 245, 266, 268, 280, 293, 295,
310, 316, 318, 340, 341, 346
mollusks, 252
molybdenum, 222
monolayer, 17, 18, 23, 27
monomers, 30, 40, 42, 43, 86, 95, 97, 147, 183
monosaccharide, 36, 37, 38, 39, 40, 43, 45, 69
monosodium glutamate, 142
morphology, 326, 331
mortality, 316
mosaic, 150
MR, 269
mRNA, 95
mucosa, 246, 254
mucus, 261
multiple factors, 153, 237, 241
muscle contraction, 202
muscles, 156, 252
mussels, 317, 318
mustard oil, 254
mutation, 339
myoglobin, 31, 146, 147, 170, 223, 230, 231
myosin, 156
N
Na+, 14, 81, 90, 102, 324
NaCl, 14, 86, 162, 164, 165, 171, 172, 251
NAD, 208
naphthalene, 324
National Academy of Sciences, 348
364
Index
native starches, 76
natural compound, 187
natural food, 73
natural polymers, 156
natural resources, 274
nausea, 73, 177, 196, 314, 317, 318, 335
NCS, 254
necrosis, 326, 348
negative consequences, 68
negative effects, 283
nerve, 202, 246, 247, 248, 304, 305, 317, 324, 341
nervous system, 60, 202, 212
Netherlands, 269
neurotransmitters, 324
neutral, 46, 69, 90, 95, 98, 138, 150, 172, 186, 187,
205, 206, 207, 211, 251, 260, 280, 294, 295, 298,
316, 321, 322
New Zealand, 277
NH2, 72, 138, 144, 187, 226, 248, 320
nickel, 132, 222
nicotinamide, 206, 207, 208
nicotinic acid, 206, 207, 208
niobium, 222
nitrates, 345, 346
nitrides, 257
nitrite, 278, 341, 345, 346
nitrogen, 3, 17, 58, 138, 139, 168, 172, 176, 222,
225, 231, 233, 320
nitrogen fixation, 233
nitrogen gas, 139
nitrosamines, 345, 346
nitroso compounds, 345, 346
NMR, 64, 227, 233, 234
non-diffusion-limited properties, 33
nonequilibrium, 29
non-polar, 165
NPR, 346
nuclear magnetic resonance, 119
nucleic acid, 17, 150, 174, 210, 223, 225, 236, 239,
320
nucleophiles, 71, 203
nucleoprotein, 150
nucleotides, 227, 236, 260
nucleus, 46
nuisance, 163
nutraceutical, 290, 291, 295
nutrient, 75, 100, 179, 216, 304, 313, 332
nutrients, vii, 1, 5, 6, 9, 37, 177, 179, 189, 191, 219,
243, 245, 271, 303, 331, 333, 335
nutrition, vii, xi, xii, 1, 2, 3, 4, 5, 6, 7, 37, 63, 73, 75,
76, 100, 102, 130, 137, 149, 167, 176, 180, 237,
239, 240, 245, 272, 319
nutritional status, 319
O
obesity, 101, 274, 277
octane, 325
OH, 11, 13, 14, 17, 31, 46, 63, 67, 152, 212, 226,
230, 248, 249, 321, 329, 333, 335
oil, 4, 5, 10, 67, 86, 100, 112, 117, 118, 119, 120,
125, 128, 131, 132, 159, 161, 162, 169, 172, 173,
176, 177, 182, 184, 185, 198, 258, 262, 265, 278,
282, 284, 286, 287, 288, 290, 291, 298
oilseed, 180
olefins, 308
oleic acid, 108, 110, 111, 112, 113, 115, 124, 127
oligomers, 74, 186
oligosaccharide, 4, 6, 36, 73, 74, 88
olive oil, 112, 117
optical activity, 152
oral cavity, 186, 246
organ, 209
organelle, 320
organic compounds, 36, 192, 325
organic food, 296
organic solvents, 92, 107, 156, 317, 328, 332, 333,
340, 346
organism, xii, 191, 223, 233, 234, 243
organs, 170, 330, 332, 339
ornithine, 140, 309
oscillation, 180
osmotic pressure, 102, 221
osteomalacia, 196
osteoporosis, 296
ovum, 329
oxalate, 251, 332
oxidation products, 61, 84, 103, 131, 211, 261, 262,
263, 339
oxidation rate, 26, 124, 125
oxidative reaction, 130
oxidizability, 205
oxygen, 6, 10, 11, 13, 26, 28, 31, 40, 41, 43, 45, 46,
61, 67, 93, 121, 122, 124, 125, 126, 127, 128,
129, 152, 182, 184, 194, 196, 197, 199, 200, 205,
209, 214, 215, 220, 222, 225, 236, 237, 268, 281,
282, 316, 320, 324, 334
oysters, 317, 318
P
pain, 73, 210, 246, 275, 300, 314, 317, 318
palm oil, 112, 117
palpitations, 300
pancreas, 22
pantothenic acid, 206, 207, 217
parallel, 46, 77, 78, 146
paralysis, 202, 304, 318
Index
pasta, 30, 220, 286
pasteurization, 178, 179, 209
patents, xii
pathogens, 153
pathways, 56, 107
PCBs, 325, 339, 340
PCDD/Fs, 325, 326
pellagra, 192, 207, 208
penetrability, 45
penicillin, 326, 327
pepsin, 150, 180, 184, 185, 316
peptide, 15, 137, 141, 145, 146, 148, 159, 168, 182,
184, 185, 186, 189, 225, 231, 327
peptide chain, 146, 148, 160, 168
peptides, 4, 36, 69, 141, 142, 177, 181, 182, 185,
186, 229, 234, 236, 260, 276, 282, 306, 318, 319
perchlorate, 239
peristalsis, 201
permeability, 316, 320, 324
permit, 282
permittivity, 14
pernicious anemia, 192, 210, 212
peroxidation, 320
peroxide, 124, 128, 184, 199, 217, 286, 336, 339
pesticide, 241, 303, 323
petroleum, 328, 329
PGE, 285
pH, 28, 31, 39, 49, 52, 53, 61, 66, 70, 71, 72, 81, 82,
84, 85, 87, 88, 92, 95, 99, 102, 104, 138, 143,
146, 153, 154, 159, 162, 163, 168, 171, 172, 178,
188, 202, 203, 204, 207, 211, 212, 214, 215, 236,
251, 273, 276, 277, 278, 279, 280, 294, 323, 332,
334
pharmaceutical, 74, 293, 294
pharmaceuticals, 82, 87, 295
phase diagram, 29
phase inversion, 161
phase transformation, 119
phenolic compounds, 61, 63, 281
phenylalanine, 140, 153, 187, 265
phosphate, 39, 49, 52, 84, 144, 170, 192, 203, 208,
209, 227, 228, 239, 292, 293, 295, 296, 297, 321,
322, 331, 332
phosphates, 38, 83, 84, 92, 236, 238, 296, 321, 322
phosphatidylcholine, 111
phosphoinositides, 39
phospholipids, 74, 107, 110, 111, 120, 128, 130, 131,
150, 167, 289, 320
phosphorous, 93
phosphorus, 49, 77, 81, 83, 196, 221, 222, 228, 296
phosphorylation, 208, 322
photochemical degradation, 205, 220
photosynthesis, 36, 233, 237
physical chemistry, 2
physical interaction, 9, 17
365
366
Index
367
Index
receptor sites, 11
receptors, 53, 140, 141, 186, 246, 247, 248, 249, 318
recognition, 337, 338
recombination, 31, 260
recommendations, 173, 174
recovery, 247
recrystallization, 29, 81
red blood cells, 177, 310, 316
red wine, 254
reducing sugars, 55, 60, 69, 73, 177, 181, 260, 342
refractive index, 115, 132, 339
regenerate, 215
regulations, 273, 319
rehydration, 168
reproduction, 74
repulsion, 16, 52, 53, 77, 82, 120, 145, 154, 160, 168
requirements, 1, 3, 37, 196, 272, 284, 289, 331, 348
researchers, 58, 66, 181, 188
residues, 5, 17, 39, 40, 41, 42, 43, 44, 46, 55, 58, 74,
76, 84, 87, 95, 96, 98, 145, 146, 148, 153, 165,
166, 177, 181, 183, 231, 233, 234, 239, 273, 303,
320, 323, 326, 330, 338, 339
resins, 348
resistance, 51, 84, 85, 92, 96, 166, 169, 182, 213,
287, 305, 323
resorcinol, 315
resources, 2, 4, 173, 174, 185, 272
respiration, 93, 205, 316
response, 75, 246
restrictions, 289
retail, 10, 290
retardation, 71, 304, 319
reticulum, 170
retina, 193, 194
retinol, 191, 192, 193, 194
RH, 50, 121, 269
rheology, 53, 85, 290
riboflavin, 150, 203, 205, 206, 217, 219
ribose, 69, 144, 300
ribosome, 150, 310, 311, 312, 313
rickets, 192, 196
rings, 53, 58, 62, 203, 229, 230, 292, 317, 339, 341
risk, 278, 291, 305, 319, 324, 339
risks, 319, 326, 330, 347
RNA, 320
rodents, 326
ROOH, 121, 281
room temperature, 49, 115, 118, 203, 212, 276, 279,
326, 340, 346, 347
root, 37, 74, 255, 298, 305, 331
roots, 36
rubber, 23
rubbers, 347
rubbery state, 33
rules, 109, 140, 141
S
saccharin, 247, 248, 274, 276, 277
safety, vii, xii, 2, 4, 5, 6, 19, 34, 35, 63, 68, 85, 107,
124, 130, 143, 224, 225, 275, 276, 277, 285, 339,
345, 348
salinity, 316
salmon, 240
Salmonella, 24
salt concentration, 149, 170, 294
salts, 9, 12, 16, 17, 39, 59, 60, 72, 81, 90, 91, 92, 98,
141, 142, 143, 163, 167, 168, 173, 184, 212, 251,
254, 273, 279, 283, 292, 294, 296, 316, 326, 328,
329, 348
saponin, 313, 314, 316
saturated fat, 108, 111, 112, 113, 114, 116, 129
saturated fatty acids, 108, 111, 112, 113, 114, 116,
129
saturation, 19
scanning calorimetry, 30, 156
scavengers, 71, 128, 281
scent, 258
school, 178
science, xi, xii, 1, 3, 4
sclerosis, 194
seafood, xii, 185, 196
secretion, 94, 201, 233, 252, 260, 331
security, 245
sedimentation, 91, 172
seed, 114, 176, 177, 184, 188, 198, 203, 289, 293,
295, 304, 314, 315, 331, 332
selectivity, 132, 133, 318, 324
selenium, 222, 309
sensation, 45, 54, 246, 247, 248, 249, 251, 252, 254,
265, 275
sensations, 252
senses, 245
sensitivity, 151, 153, 178, 246, 306
sequencing, 139
serine, 99, 111, 140, 170, 231, 320, 336
serum, 101, 153, 162, 163, 164, 171, 233
serum albumin, 153, 162, 163, 164, 171
sex, 107, 330
sex hormones, 330
SFI, 119
shade, 298
shape, 1, 2, 21, 22, 23, 46, 51, 52, 53, 79, 80, 91,
118, 145, 152, 153, 158, 159
shear, 51, 52, 98, 162, 165, 166, 169, 292, 294
shelf life, 30, 33, 82, 86, 95, 96, 120, 157, 277, 278,
281, 284, 289, 339
shellfish, 269, 317, 318
shortage, 319
showing, 249, 276
shrimp, 185, 316
368
Index
369
Index
sustainable development, 4
sweeteners, 55, 74, 94, 187, 248, 251, 274, 276, 277,
300
swelling, 23, 80, 81, 83, 84, 85, 90, 102, 159, 168,
169, 314
symptoms, 177, 191, 194, 196, 202, 205, 208, 210,
214, 240, 272, 303, 305, 306, 314, 318, 320, 335,
339
synergistic effect, 281, 295
synthesis, 37, 101, 196, 201, 210, 214, 233, 238,
264, 265, 269, 298, 304, 309, 320, 341, 347
Syria, 96
T
tachypnea, 304
tannins, 349
target, 337, 338
techniques, 3, 107, 137, 241, 245, 271, 304
technological advancement, 4
technologies, 3, 4, 6, 7, 173, 218
technology, 3, 71, 179, 196, 199, 272, 283, 290
teeth, 221, 284
tension, 28, 31, 120, 286
terminals, 141, 234
terpenes, 254, 258, 265
testicle, 329
testis, 326
testosterone, 329, 330
tetracyclines, 329
textbook, vii, 4
textbooks, vii, 4
texture, 1, 4, 5, 6, 7, 9, 18, 37, 46, 53, 85, 87, 88, 91,
97, 156, 157, 158, 162, 163, 165, 169, 188, 271,
273, 281, 289, 290, 292, 295, 296
thallium, 222
thermal analysis, 30
thermal decomposition, 107, 129, 268
thermal degradation, 129, 203, 266, 267, 268, 323,
341
thermal expansion, 119
thermal stability, 74, 159, 209, 294
thermal treatment, 157, 188, 205, 323
thermodynamic equilibrium, 29
thermodynamic parameters, 220
thermodynamic properties, 156
thermograms, 156
thermolysis, 58
thermostability, 94
thiamin, 201, 202, 219
thickening agents, 97, 293
thinning, 82, 98, 169
thiophenol, 203
threonine, 140, 231
thrombin, 338
thymine, 212
thymus, 326
thyroid, 346
tin, 317, 349
tissue, 84, 86, 108, 170, 194, 196, 269, 308, 318,
326, 329
titanium, 298
tobacco, 147, 150
tocopherols, 197, 219, 281, 282
tofu, 152, 251
tones, 93
tonic, 277
tooth, 274, 275
toxic effect, 183, 305
toxic metals, 102, 240, 348
toxic substances, vii, 178, 303, 306
toxicity, 7, 132, 183, 188, 222, 224, 227, 233, 238,
239, 240, 278, 303, 305, 309, 311, 312, 313, 314,
316, 317, 319, 320, 321, 322, 323, 324, 326, 339,
347
toxicology, 2
toxin, 305, 317, 318
trace elements, 222, 223, 241, 242, 243, 331, 332,
333
trade, 276
transesterification, 5
transferrin, 233
transformation, 3, 12, 44, 117, 194, 208, 231, 240,
323
transformations, 165, 166
transition elements, 237
transition metal, 36, 41, 332, 334
transition temperature, 30
transmission, 224
transparency, 82, 83, 84
transport, 4, 6, 11, 31, 36, 150, 152, 232, 237, 272,
308, 319
transportation, 283, 347
treatment, 5, 71, 101, 153, 155, 156, 157, 164, 168,
172, 174, 177, 178, 179, 180, 182, 183, 187, 204,
220, 236, 272, 281, 306, 317, 326, 336
treatment methods, 204
trigeminal nerve, 246
triglycerides, 74, 94, 107, 133, 134
trypsin, 152, 177, 180, 183, 185, 337, 338, 349
tryptophan, 67, 68, 145, 153, 248, 309
Turkey, 96
tyrosine, 140, 153, 184, 231, 320
U
ultraviolet irradiation, 151
United Nations, 324
370
Index