FOOD TECHNOLOGY

FOOD CHEMISTRY AND NUTRITION

Food chemistry is the study of chemical processes and interactions of all biological and non-
biological components of foods. The biological substances include such items as meat, poultry,
lettuce, beer, and milk as examples. It is similar to biochemistry in its main components such as
carbohydrates, lipids, and protein, but it also includes areas such as water, vitamins, minerals,
enzymes, food additives, flavors, and colors. This discipline also encompasses how products
change under certain food processing techniques and ways either to enhance or to prevent them
from happening. An example of enhancing a process would be to encourage fermentation of dairy
products with microorganisms that convert lactose to lactic acid; an example of preventing a
process would be stopping the browning on the surface of freshly cut Red Delicious apples using
lemon juice or other acidulated water.

Food chemistry's history dates back as far as the late 18th century when many famous chemists
were involved in discovering chemicals important in foods, including Carl Wilhelm Scheele
(isolated malic acid from apples in 1785), and Sir Humphry Davy published the first book on
agricultural and food chemistry in 1813 titled Elements of Agricultural Chemistry, in a Course of
Lectures for the Board of Agriculture in the United Kingdom which would serve as a foundation
for the profession worldwide, going into a fifth edition.
Nutrition (also called nourishment or aliment) is the provision, to cells and organisms, of the
materials necessary (in the form of food) to support life. Many common health problems can be
prevented or alleviated with a healthy diet.
The diet of an organism is what it eats, which is largely determined by the perceived palatability
of foods.[citation needed] Dietitians are health professionals who specialize in human nutrition, meal
planning, economics, and preparation. They are trained to provide safe, evidence-based dietary
advice and management to individuals (in health and disease), as well as to institutions. Clinical
nutritionists are health professionals who focus more specifically on the role of nutrition in
chronic disease, including possible prevention or remediation by addressing nutritional
deficiencies before resorting to drugs. While government regulation of the use of this professional
title is less universal than for "dietician", the field is supported by many high-level academic
programs, up to and including the Doctoral level, and has its own voluntary certification board,[1]

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professional associations, and peer-reviewed journals, e.g. the American Society for Nutrition and
the American Journal of Clinical Nutrition.
A poor diet can have an injurious impact on health, causing deficiency diseases such as scurvy[2]
and kwashiorkor;[3] health-threatening conditions like obesity[4][5] and metabolic syndrome;[6] and
such common chronic systemic diseases as cardiovascular disease,[7][8] diabetes,[9][10] and
osteoporosis.
Carbohydrates: A carbohydrate is an organic compound with the empirical formula Cm(H2O)n;
that is, consists only of carbon, hydrogen, and oxygen, with a hydrogen:oxygen atom ratio of 2:1
(as in water). Carbohydrates can be viewed as hydrates of carbon, hence their name. Structurally
however, it is more accurate to view them as polyhydroxy aldehydes and ketones.
The term is most common in biochemistry, where it is a synonym of saccharide. The
carbohydrates (saccharides) are divided into four chemical groupings: monosaccharides,
disaccharides, oligosaccharides, and polysaccharides. In general, the monosaccharides and
disaccharides, which are smaller (lower molecular weight) carbohydrates, are commonly referred
to as sugars.
Monosaccharides - are the simplest carbohydrates in that they cannot be hydrolyzed to smaller
carbohydrates. They are aldehydes or ketones with two or more hydroxyl groups. The general
chemical formula of an unmodified monosaccharide is C•(H2O)n, literally a "carbon hydrate."
Monosaccharides are important fuel molecules as well as building blocks for nucleic acids. The
smallest monosaccharides, for which n = 3, are dihydroxyacetone and D- and L-glyceraldehyde.

D-Glucose with its α and β anomers

Disaccharides - Two joined monosaccharides are called a disaccharide and these are the
simplest polysaccharides. Examples include sucrose and lactose. They are composed of two
monosaccharide units bound together by a covalent bond known as a glycosidic linkage formed
via a dehydration reaction, resulting in the loss of a hydrogen atom from one monosaccharide and

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a hydroxyl group from the other. The formula of unmodified disaccharides is C12H22O11. Although
there are numerous kinds of disaccharides, a handful of disaccharides are particularly notable.

Sucrose: D-Glucose (left) + D-Fructose (right)

Sucrose, is the most abundant disaccharide, and the main form in which carbohydrates are
transported in plants. It is composed of one D-glucose molecule and one D-fructose molecule.
The systematic name for sucrose, O-α-D-glucopyranosyl-(1→2)-D-fructofuranoside, indicates
four things:
• Its monosaccharides: glucose and fructose
• Their ring types: glucose is a pyranose, and fructose is a furanose
• How they are linked together: the oxygen on carbon number 1 (C1) of α-D-glucose is
linked to the C2 of D-fructose.
• The -oside suffix indicates that the anomeric carbon of both monosaccharides participates
in the glycosidic bond.
Lactose, a disaccharide composed of one D-galactose molecule and one D-glucose molecule,
occurs naturally in mammalian milk. The systematic name for lactose is O-β-D-galactopyranosyl-
(1→4)-D-glucopyranose. Other notable disaccharides include maltose (two D-glucoses linked α-
1,4) and cellulobiose (two D-glucoses linked β-1,4). disaccharides can be classified into two
types.They are reducing and non-reducing disaccahrides if the functional group is present in
bonding with another sugar unit it is called as reducing disaccharide.

Oligosaccharides and polysaccharides - are composed of longer chains of monosaccharide units

bound together by glycosidic bonds. The distinction between the two is based upon the number of
monosaccharide units present in the chain. Oligosaccharides typically contain between three and
ten monosaccharide units, and polysaccharides contain greater than ten monosaccharide units.
Definitions of how large a carbohydrate must be to fall into each category vary according to
personal opinion. Examples of oligosaccharides include the disaccharides mentioned above, the
trisaccharide raffinose and the tetrasaccharide stachyose.

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Oligosaccharides are found as a common form of protein posttranslational modification. Such
posttranslational modifications include the Lewis and ABO oligosaccharides responsible for
blood group classifications and so of tissue incompatibilities, the alpha-Gal epitope responsible
for hyperacute rejection in xenotransplantation, and O-GlcNAc modifications.
Polysaccharides represent an important class of biological polymers. Their function in living
organisms is usually either structure- or storage-related. Starch (a polymer of glucose) is used as a
storage polysaccharide in plants, being found in the form of both amylose and the branched
amylopectin. In animals, the structurally similar glucose polymer is the more densely branched
glycogen, sometimes called 'animal starch'. Glycogen's properties allow it to be metabolized more
quickly, which suits the active lives of moving animals.
Cellulose and chitin are examples of structural polysaccharides. Cellulose is used in the cell walls
of plants and other organisms, and is claimed to be the most abundant organic molecule on earth.
[9]
It has many uses such as a significant role in the paper and textile industries, and is used as a
feedstock for the production of rayon (via the viscose process), cellulose acetate, celluloid, and
nitrocellulose. Chitin has a similar structure, but has nitrogen-containing side branches,
increasing its strength. It is found in arthropod exoskeletons and in the cell walls of some fungi. It
also has multiple uses, including surgical threads.

Amylose: a linear polymer of glucose with α-(1→4) bonds

Pectin - is a structural heteropolysaccharide contained in the primary cell walls of terrestrial
plants. It was first isolated and described in 1825 by Henri Braconnot.[2] It is produced
commercially as a white to light brown powder, mainly extracted from citrus fruits, and is used in
food as a gelling agent particularly in jams and jellies. It is also used in fillings, sweets, as a
stabilizer in fruit juices and milk drinks and as a source of dietary fiber. The main use for pectin
(vegetable agglutinate) is as a gelling agent, thickening agent and stabilizer in food. The classical
application is giving the jelly-like consistency to jams or marmalades, which would otherwise be

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sweet juices. For household use, pectin is an ingredient in gelling sugar (also known as "Jam
Sugar") where it is diluted to the right concentration with sugar and some citric acid to adjust pH.
In some countries, pectin is also available as a solution or an extract, or as a blended powder, for
home jam making. For conventional jams and marmalades that contain above 60% sugar and
soluble fruit solids, high-ester pectins are used. With low-ester pectins and amidated pectins less
sugar is needed, so that diet products can be made. Pectin can also be used to stabilize acidic
protein drinks, such as drinking yogurt, and as a fat substitute in baked goods. Typical levels of
pectin used as a food additive are between 0.5 – 1.0% - this is about the same amount of pectin as
in fresh fruit. In medicine, pectin increases viscosity and volume of stool so that it is used against
constipation and diarrhea.
Dietary fiber - or sometimes roughage is the indigestible portion of plant foods having two main
components:
• soluble (prebiotic, viscous) fiber that is readily fermented in the colon into gases and
physiologically active byproducts, and
• insoluble fiber that is metabolically inert, absorbing water as it moves through the
digestive system, easing defecation.
It acts by changing the nature of the contents of the gastrointestinal tract, and by changing how
other nutrients and chemicals are absorbed. Soluble fiber absorbs water to become a gelatinous,
viscous substance and is fermented by bacteria in the digestive tract. Insoluble fiber has bulking
action and is not fermented. Although a major dietary insoluble fiber source, lignin may alter the
fate and metabolism of soluble fibers.
Chemically, dietary fiber consists of non-starch polysaccharides such as arabinoxylans, cellulose
and many other plant components such as resistant dextrins, inulin, lignin, waxes, chitins, pectins,
beta-glucans and oligosaccharides. A novel position has been adopted by the US Department of
Agriculture to include functional fibers as isolated fiber sources that may be included in the diet.
The term "fiber" is something of a misnomer, since many types of so-called dietary fiber are not
fibers at all.
Food sources of dietary fiber are often divided according to whether they provide
(predominantly) soluble or insoluble fiber. Plant foods contain both types of fiber in varying
degrees, according to the plant's characteristics.
Advantages of consuming fiber are the production of healthful compounds during the
fermentation of soluble fiber, and insoluble fiber's ability (via its passive hygroscopic properties)
to increase bulk, soften stool and shorten transit time through the intestinal tract.

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A disadvantage of a diet high in fiber is the potential for significant intestinal gas production and
bloating. Constipation can occur if insufficient fluid is consumed with a high-fiber diet.
Dietary fiber functions and benefits
Functions Benefits
Increases food volume without increasing
May reduce appetite
caloric content, providing satiety
Attracts water and turns to gel during
Lowers variance in blood sugar
digestion, trapping carbohydrates and
levels
slowing absorption of glucose
Lowers total and LDL cholesterol Reduces risk of heart disease
May reduce onset risk or
Regulates blood sugar symptoms of metabolic
syndrome and diabetes
Speeds the passage of foods through the
Facilitates regularity
digestive system
Adds bulk to the stool Alleviates constipation
Balances intestinal pH and stimulates
May reduce risk of colorectal
intestinal fermentation production of short-
cancer
chain fatty acids

Fiber does not bind to minerals and vitamins and therefore does not restrict their absorption, but
rather evidence exists that fermentable fiber sources improve absorption of minerals, especially
calcium.[30][31][32] Some plant foods can reduce the absorption of minerals and vitamins like
calcium, zinc, vitamin C, and magnesium, but this is caused by the presence of phytate (which is
also thought to have important health benefits), not by fiber.

Proteins in Food
Classification: Proteins compose over 50% of the dry weight of an average living cell and are
very complex macromolecules. They also play a fundamental role in the structure and function of
cells. Consisting mainly of carbon, nitrogen, hydrogen, oxygen, and some sulfur, they also may
contain iron, copper, phosphorus, or zinc.In food, proteins are essential for growth and survival
and vary depending upon a person's age and physiology (e.g., pregnancy). Proteins in food are
commonly found in peanuts, meat, poultry, and seafood.
Proteins are polymer chains made of amino acids linked together by peptide bonds. Amino acids
can be divided into either essential amino acids or non-essential amino acids. Proteins and

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carbohydrates contain 4 kcal per gram as opposed to lipids which contain 9 kcal per gram. The
essential amino acids, which must be obtained from food sources, are leucine, isoleucine, valine,
lysine, threonine, tryptophan, methionine, phenylalanine and histidine. On the other hand, non-
essential amino acids can be made by the body from other amino acids. The non-essential amino
acids are arginine, alanine, asparagine, aspartic acid, cysteine, glutamine, glutamic acid, glycine,
proline, serine, and tyrosine.
In nutrition, proteins are broken down in the stomach during digestion by enzymes known as
proteases into smaller polypeptides to provide amino acids for the body, including the essential
amino acids that the organism cannot be biosynthesized by the body itself. Thus, protein from
one's diet should provide both essential and non-essential amino acids for protein synthesis.[1]
Most animal and certain vegetable proteins are considered complete proteins with a full
complement of essential amino acids in adequate proportions. People who avoid animal products
for religious and health reasons may practice protein combining to get the essential amino acids
in their diet.

Amino acid
Functions: Protein is a nutrient needed by the human body for growth and maintenance. Aside
from water, protein is the most abundant molecule in the body. Protein is found in all cells of the
body and is the major structural component of all cells in the body, especially muscle.[2][3] This
also includes body organs, hair and skin. Proteins also are utilized in membranes, such as
glycoproteins. When broken down into amino acids, they are used as precursors to nucleic acid
and vitamins. Hormones and enzymes are also formed from amino acids in which they help
regulate metabolism, support the immune system and other body functions. Finally, protein is
needed to form blood cells.
Structure
Most proteins fold into unique 3-dimensional structures. The shape into which a protein
naturally folds is known as its native conformation. Although many proteins can fold unassisted,

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simply through the chemical properties of their amino acids, others require the aid of molecular
chaperones to fold into their native states. Biochemists often refer to four distinct aspects of a
protein's structure:
• Primary structure: the amino acid sequence.
• Secondary structure: regularly repeating local structures stabilized by hydrogen bonds.
The most common examples are the alpha helix, beta sheet and turns. Because secondary
structures are local, many regions of different secondary structure can be present in the
same protein molecule.
• Tertiary structure: the overall shape of a single protein molecule; the spatial relationship
of the secondary structures to one another. Tertiary structure is generally stabilized by
nonlocal interactions, most commonly the formation of a hydrophobic core, but also
through salt bridges, hydrogen bonds, disulfide bonds, and even posttranslational
modifications. The term "tertiary structure" is often used as synonymous with the term
fold. The tertiary structure is what controls the basic function of the protein.
• Quaternary structure: the structure formed by several protein molecules (polypeptide
chains), usually called protein subunits in this context, which function as a single protein
complex.
Proteins are not entirely rigid molecules. In addition to these levels of structure, proteins may
shift between several related structures while they perform their functions. In the context of these
functional rearrangements, these tertiary or quaternary structures are usually referred to as
"conformations", and transitions between them are called conformational changes. Such changes
are often induced by the binding of a substrate molecule to an enzyme's active site, or the
physical region of the protein that participates in chemical catalysis. In solution proteins also
undergo variation in structure through thermal vibration and the collision with other molecules.[19]

Molecular surface of several proteins showing their comparative sizes. From left to right are: immunoglobulin G
(IgG, an antibody), hemoglobin, insulin (a hormone), adenylate kinase (an enzyme), and glutamine synthetase
(an enzyme).
Proteins can be informally divided into three main classes, which correlate with typical tertiary
structures: globular proteins, fibrous proteins, and membrane proteins. Almost all globular

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proteins are soluble and many are enzymes. Fibrous proteins are often structural, such as
collagen, the major component of connective tissue, or keratin, the protein component of hair and
nails. Membrane proteins often serve as receptors or provide channels for polar or charged
molecules to pass through the cell membrane.[20] A special case of intramolecular hydrogen bonds
within proteins, poorly shielded from water attack and hence promoting their own dehydration,
are called dehydrons.
Structure determination
Discovering the tertiary structure of a protein, or the quaternary structure of its complexes, can
provide important clues about how the protein performs its function. Common experimental
methods of structure determination include X-ray crystallography and NMR spectroscopy, both
of which can produce information at atomic resolution. However, NMR experiments are able to
provide information from which a subset of distances between pairs of atoms can be estimated,
and the final possible conformations for a protein are determined by solving a distance geometry
problem. Dual polarisation interferometry is a quantitative analytical method for measuring the
overall protein conformation and conformational changes due to interactions or other stimulus.
Circular dichroism is another laboratory technique for determining internal beta sheet/ helical
composition of proteins. Cryoelectron microscopy is used to produce lower-resolution structural
information about very large protein complexes, including assembled viruses;[22] a variant known
as electron crystallography can also produce high-resolution information in some cases ,
especially for two-dimensional crystals of membrane proteins.[23] Solved structures are usually
deposited in the Protein Data Bank (PDB), a freely available resource from which structural data
about thousands of proteins can be obtained in the form of Cartesian coordinates for each atom in
the protein. Many more gene sequences are known than protein structures. Further, the set of
solved structures is biased toward proteins that can be easily subjected to the conditions required
in X-ray crystallography, one of the major structure determination methods. In particular,
globular proteins are comparatively easy to crystallize in preparation for X-ray crystallography.
Membrane proteins, by contrast, are difficult to crystallize and are underrepresented in the PDB.
Structural genomics initiatives have attempted to remedy these deficiencies by systematically
solving representative structures of major fold classes. Protein structure prediction methods
attempt to provide a means of generating a plausible structure for proteins whose structures have
not been experimentally determined.