Journal of Food Engineering 190 (2016) 54e60

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Journal of Food Engineering

journal homepage: www.elsevier.com/locate/jfoodeng

Valorisation of industrial cooked ham by-products as functional

ingredients
Alina-Violeta Ursu a, c, Alain Marcati b, c, *, Philippe Michaud a, c, Gholamreza Djelveh b, c
a
Universit
e Clermont Auvergne, Universit
e Blaise Pascal, Institut Pascal, BP 10448, F-63000, Clermont-Ferrand, France
b
Universit
e Clermont Auvergne, SIGMA Clermont, Institut Pascal, BP 10448, F-63000, Clermont-Ferrand, France
c
CNRS, UMR 6602, IP, F-63178, Aubiere, France

a r t i c l e i n f o a b s t r a c t

Article history: The production of cooked ham on an industrial scale generates two liquid by-products: pork exudate
Received 20 November 2015 (PE), collected before the salting, has 14% weight dry matter, mainly rich in proteins (90%); ham broth
Received in revised form (HB), released after cooking, has 8% dry matter including 50% proteins. The biochemical, rheological and
13 May 2016
functional properties of these by-products were studied and compared to reference ingredients. PE could
Accepted 20 June 2016
Available online 21 June 2016
form a gel by coagulation at 50
C and had a good emulsifying capacity (324 ± 8 mL of oil per gram of
protein) with high stability. Even after cooking, an altering process, HB had the ability to form a gel at low
temperature (8e18
C), a good emulsifying capacity (252 ± 7 mL of oil per gram of protein) and foaming
Keywords:
Cooked ham
ability (ratio of foam to initial volume: 177 ± 14). Both by-products could then be valorised as functional
By-products ingredients for delicatessen products.
Proteins © 2016 Elsevier Ltd. All rights reserved.
Gel
Emulsion
Foam

1. Introduction products generated after another meat processing step, such as

Dealing with by-products is a major concern in the food pro-
cessing industry (Mirabella et al., 2014). This is especially the case
in the meat-processing industry, as they can be a source of proteins
for food or feed purposes. These by-products can be found in solid
form (carcass, skin) or liquids form recovered in wastewaters that
require treatment because of their high chemical or biological
organic demands (Bull et al., 1982). Solid wastes could find a val-
orisation as energy vectors after digestion (Hejnfelt and Angelidaki,
2009) or can be hydrolyzed by chemicals (Selmane et al., 2008) or
enzymes (Rafieian et al., 2015) into valuable functional proteins.
Concerning liquid waste, proteins from red blood cells (Gomez-
Juarez et al., 1999) or plasma (Penteado et al., 1979) were also
found to have useful functional properties. Since slaughtering
represents the main source of waste products in the meat industry,
much interest has been raised concerning the ways of dealing with
these by-products (Arvanitoyannis and Ladas, 2008). However,
there is currently less research on the potential valorisation of by-
the cooking of hams in the delicatessen trade.
In Europe, France is the leader in the production of cooked ham,
with particular stress on high-quality products such as Paris or York
ham (Spencer, 2003). Each year, around 190,000 tons of cooked
hams are produced, but during the manufacturing process more
than 13,000 cubic meters of liquid by-products are generated.
These by-products, containing proteins, salts and water, are poorly
valorised and mainly rejected as effluents into wastewaters,
inducing a non-negligible cost of compulsory treatment due to
legal restrictions. In this paper, two different effluents from cooked
ham processing plants are investigated: ham broth (HB) and pork
exudate (PE) with the objective to characterize their biochemical
composition, to determine whether they can easily be processed
and if their proteins can be valorised as functional ingredients
when compared to reference ingredients.
2. Material and methods

2.1. Raw material collection and storage

* Corresponding author. Universite  Clermont Auvergne, SIGMA Clermont, Institut
Pascal, BP 10448, F-63000, Clermont-Ferrand, France. Effluents were collected in a plant with a 20,000 metric tonnes
E-mail address: alain.marcati@sigma-clermont.fr (A. Marcati). per year production capacity. A simplified flowchart of the ham

http://dx.doi.org/10.1016/j.jfoodeng.2016.06.013
0260-8774/© 2016 Elsevier Ltd. All rights reserved.
 A.-V. Ursu et al. / Journal of Food Engineering 190 (2016) 54e60
production process is given in Fig. 1 and detailed in Toldra  et al.
(2010). For each tonne of ham produced, around 70 kilos of HB
and 8 kilos of PE can be recovered. PE is a reddish-pink by-product
recovered from the pork chunk collecting tanks before salting and
tumbling. HB, the main effluent, is a light orange liquid which is
released during the opening of the moulds after the cooking and
maturing of hams. After collection, the effluents were stored at 4
C
or 16
C for respectively short or medium-term conservation. For
long-term conservation, effluents were converted into powders by
freeze-drying (PL6000, Thermo Electron Corp.) with nearly 100%
powder recovery or spray-drying (B290, Büchi) with 85 ± 5%
powder recovery. Water activity aw was measured post factum with
an aw-meter (Labmaster, Novasina Ag).
2.2. Raw material characterisation
Dry matter and biochemical composition of each effluent were
quantified using different assays. All measurements were done in
triplicate.
2.2.1. Biochemical characterisation
Protein content was obtained using a total nitrogen analyser
(TNM-1, Shimadzu); collagen was specifically quantified by the
Lollar method (Lollar, 1958). The quantities of fats and soluble
sugars were respectively measured using the Bligh and Dyer (Bligh
and Dyer, 1959) and Dubois (Dubois et al., 1956) methods. Sodium
chloride concentration was determined by Charpentier-Volhard
titration; other salts such as phosphates or nitrates were included
in the ash determination.
2.2.2. Protein qualitative analysis
The proteic fractions of the effluents were qualitatively analysed
for their molecular weight and amino acids compositions.
Size-exclusion chromatography (SEC) was implemented using
an Akta FPLC (Amersham Biosciences, UK) device equipped with a
UV/VIS detector. Samples (0.1 mL) filtered at 0.2 mm were loaded at
0.5 mL/min on a Superdex TM 200 column (GE Healthcare, Life
Sciences) eluted with a 50 mM phosphate buffer (pH 7) supple-
mented with 150 mM NaCl. A standard protein mixture (Bio-Rad
Laboratories), including thyroglobulin (670 kDa), g-globulin
Fig. 1. Flowchart of the ham production process with the potential recovery of effluents.
55
(158 kDa), ovalbumin (44 kDa), myoglobulin (17 kDa) and B12
vitamin (1.35 kDa), was used for calibration. Eluted proteins were
detected at 280 nm and quantitatively quantified in each elution
peak.
Sodium dodecyl sulphate-polyacrylamide gel electrophoresis
(SDS-PAGE) was carried out according to the method of Laemmli
(1970) in 12% acrylamide gels. The proteins were stained with a
Coomassie blue R-250.
Amino acids were quantified by ion-exchange chromatography
with post-column ninhydrin detection (Hitachi L 8900). Prior to
amino acids analysis, samples were submitted to basic or acid hy-
drolysis using NaOH 6 M for tryptophan quantification or HCl 5.5 M
for the other amino acids.
2.3. Functional properties
The functional properties of PE and HB proteins were compared
with commercial ingredients used in food formulations such as
sodium caseinate Na-Cas and whey protein isolate WPI (Armor
ines, France).
Prote
2.3.1. Rheological behaviour and gelling properties
A stress-controlled rheometer (AR-G2, TA Instruments, USA)
equipped with a double gap Couette or plate-plate system and a
Peltier circulator for temperature control was used to determine
two types of properties.
Measurements in flow conditions were applied with shear rates
in the range of 1e1000 s1 in order to determine PE and HB vis-
cosities in native solutions. Experiments were performed at 20
C.
Dynamic oscillatory shear tests were carried out to obtain the
gelling properties of the native solutions at low and high temper-
ature. A low-amplitude deformation (1% strain) was applied at an
oscillation frequency of 1 Hz. For low temperature gelation, the
temperature was decreased from 20 to 1
C with a ramp of
0.1
C$min1. The gelling temperature was detected at the cross-
over of the curves of storage modulus G0 and loss modulus G00 versus
temperature. For high temperature gelation, the temperature was
increased from 20 to 90
C with a ramp of 0.5
C$min1. The gelling
temperature was deduced from a rapid increase in the storage
modulus G0 versus temperature curve.
56 A.-V. Ursu et al. / Journal of Food Engineering 190 (2016) 54e60
2.3.2. Solubility of dried powders
After drying the effluents, the solubility of protein powders was
checked with respect to the pH. The pH was adjusted in a range of
3e11 using 1 M solution of NaOH or HCl.
2.3.3. Surface properties
Interfacial and surface tensions were measured using a K12
tensiometer (Krüss Gmbh, Germany) equipped with a Wilhelmy
plate. Experiments were conducted at 20
C with solutions con-
taining 2% proteins. Rapeseed oil was used as the organic phase for
interfacial tension measurements.
Protein surface hydrophobicity was evaluated according to a
protocol derived from Kato and Nakai (1980) using a magnesium
salt of 1-anilinonaphtalene-8-sulfonic acid (ANS) as an extrinsic
fluorescence probe. Relative fluorescence intensity (RFI) was
measured with a Flx spectrofluorimeter (Safas, Monaco). Excitation
and emission wavelengths of 390 and 470 nm and slit widths of
10 nm were used. Instrument standardisation was performed by
measuring the RFI values of a solution of ANS in methanol, as
described by Haskard and Li-Chan (1998).
5 mL of protein solutions in 20 mM phosphate buffer (pH 7)
were mixed with 25 mL of ANS and incubated in the dark for 10 min
at 20
C before measuring the RFI. Surface hydrophobicity corre-
sponded to the initial slope estimated by linear regression analysis
of the curve of RFI versus protein concentration.
2.3.4. Emulsifying and foaming properties
Two different emulsifying properties were investigated. Emul-
sion capacity EC (expressed in grams of oil per gram of protein)
represents the maximum amount of oil that can be emulsified by a
specific quantity of proteins. Solutions of 1% wt of proteins were
prepared for this measurement. Emulsion stability ES (expressed in
percentage) refers to the level of emulsion remaining stable after
24 h storage at room temperature. Solutions of 2% wt of proteins
with addition of 50% wt of oil were used. Rapeseed oil was again
used as an organic phase. Details on the applied protocols are
available in Ursu et al. (2014).
Following the protocols described by Selmane et al. (2008), two
foaming properties were studied. Foaming ability FA (expressed in
percentage) characterises the capacity of a protein solution to
produce foams and compares the volume of the foam to the initial
volume of the solution after agitation. Foaming stability FS
(expressed in minutes) is the time necessary to reduce the volume
of foam by half. All foaming experiments were conducted with the
protein solution at 2% wt using an Ultra-Turrax T25 device (Ika-
Werke GmbH, Germany).
3. Results
3.1. Biochemical characterisation of the effluents
The average chemical composition of the two effluents was
determined for the different batches; results are presented in
Table 1.
PE had the higher content in dry matter (14%), mainly consisting
of proteins (90%) and soluble minerals. Moisture was more present
in HB and the protein percentage was lower (50%). Among the
proteins, collagen residues were not detected in PE as its solubility
is poor in its native state. After salting and cooking, collagen could
be solubilised and represented around 12% wt of the proteins in HB.
Due to the salting of the meat before tumbling and cooking, the
NaCl percentage was quite high in HB (around 20% wt of the dry
matter). Soluble sugars were found in HB, and this effluent had a
higher quantity of minerals than PE.
Molecular weights of proteins from the two effluents (Fig. 2a)
Table 1
Average composition in dry matter of the collected effluents.
Ingredients (%) PE HB
Dry matter 14 ± 2 8.0 ± 0.5
Proteins 89 ± 3 48 ± 4
with collagen NDa 7±1
Fats 0.9 ± 0.1 10 ± 2
Soluble sugars ND 4±1
Sodium chloride 0.7 ± 0.1 20 ± 5
Residual ash 8±2 25 ± 2
The bold font is used to differentiate the composition in dry matter (or water: 100-%
of dry matter) of the sample and the detailed ingredients in the dry matter (normal
font). The subsequent items (proteins, fats,…) are a percentage of the dry matter.
The italics font is used to indicate the percentage in respect to dry matter of a
particular protein (collagen) among the total proteins analysed.
a
ND: non detected.
were strongly different. PE showed a majority (60% wt) of proteins
between 10 and 210 kDa, and the remaining (40%) had low mo-
lecular weights (<3 kDa). HB sample contained mainly (70% wt)
proteins with low molecular weights (<3 kDa), the 30% remaining
having molecular weights between 10 and 65 kDa. Collagen did not
appear on the chromatogram because filtration (0.2 mm) was used
before SEC. However, proteins with a molecular weight superior to
100 kDa detected on SDS-PAGE gels and absent on chromatograms
of SEC could be attributed to collagen (Fig. 2b). The SDS-PAGE
analysis denoted the presence of proteins fractions with a molec-
ular weight of 60, 35 and below 37 kDa as observed in the SEC
chromatrogram. The electrophoresis profile of PE displayed a large
variety of proteins with molecular weights between 20 and
100 kDa.
The amino acid compositions of the two effluents appeared as
not similar (Table 2). They were quite homogeneous for PE (only
glutamic acid is superior to 10%) whereas glutamic acid, glycine and
histidine represented 50% of total amino acids in HB. After basic
hydrolysis of proteins, only traces of tryptophan were detected, and
values are consequently not given in Table 2. Concerning the other
essential amino acids, their sum reached 50% of the content for PE,
which is in accordance with the value given for meat. In HB, total
amino acids were a little lower (45%) due to the high percentage of
histidine (23.2%). The value of methionine in this effluent was also
superior to PE.
3.2. Functional properties
The two effluents were liquid in their native form at room
temperature. Rheological measurements in flow conditions at 20
C
showed that both exhibited Newtonian behaviour with low vis-
cosity: PE viscosity was in the range of 3e10 cP according to the dry
matter content, and HB one in the range of 1.3e6.0 cP depending on
the dry matter. The effluents were nevertheless not always in a
liquid state: after short-term storage at 4
C, HB switched indeed to
a gel state. Oscillatory rheological measurements for a temperature
range between 20 and 4
C showed the crossover point of G0 and Gʺ.
The gelling point was sensitive to the amount of collagen between 8
and 18
C. Gel strength was rather low, as the storage modulus value
at 4
C was of a few tens. Gelling was reversible, as HB became liquid
when the temperature rised beyond the gel point. PE did not follow
the same tendency, remaining liquid at 4
C (storage temperature),
but was much more sensitive to higher temperatures (Fig. 3). Pro-
teins from PE had indeed the capacity to coagulate when the
temperature was raised beyond 45
C. There was a sharp increase in
the storage modulus between 45
C and 75
C before reaching a
plateau. After the temperature ramp, PE formed a solid and elastic
 A.-V. Ursu et al. / Journal of Food Engineering 190 (2016) 54e60 57

Fig. 2. a) Size-exclusion chromatographs of PE and HB; b) Electrophoresis of the two effluents.

Table 2 paste. This state transformation was irreversible because when the
Average composition in amino acids (% of total amino acids) from proteins of the temperature decreased to 20
C PE was still solid. The same phe-
by-products.
nomenon was observed with dairy proteins but temperatures of
Amino acids PE HB coagulation were higher: respectively 70 and 85
C for WPI and Na-
Asp 9.5 4.4 Cas. Coagulation with an increase in temperature was not observed
Thra 5.2 2.2 for HB and heat treatment (up to 90
C) had a negative impact on HB
Ser 3.7 2.7 properties, since it could no longer form a gel at storage tempera-
Glu 10.6 13.3
ture (data not shown). In order to preserve the effluents from the
Gly 5.4 13.5
Ala 6.2 6.6 development of bacteria such as Listeria, drying must be applied if
Vala 7.1 3.6 they are not used quickly after collection. Considering the above
Ileua 4.8 1.5 rheological results, a long high temperature treatment must be
Leua 7.4 3.0 avoided. In this case, freeze and spray-drying were used. With both
Tyr 3.1 1.0
Phea 7.8 1.8
methods, aw values were measured in the range of 0.15e0.25,
Hisa 6.6 23.2 which was sufficiently low for long-term preservation. Whatever
Lysa 8.6 4.3 the method, the proteins properties described below were not
Arg 5.0 4.3 affected by the drying process. In order to test the functional
Pro 4.7 6.8
properties of proteins from effluents, high solubility must be ach-
Cys 1.8 2.4
Meta 2.3 5.5 ieved. Solubility is expressed as a percentage of soluble proteins
a
versus total proteins, (Fig. 4).
Essential amino acids.

Fig. 3. Variation of storage modulus of HB (black dots), PE (grey dots), WPI (black circle) and Na-Cas (grey circle) with temerature increase.
58 A.-V. Ursu et al. / Journal of Food Engineering 190 (2016) 54e60

Table 3
Functional properties of proteins from PE and HB compared to commercial proteins.

Functional properties PE HB Na-Cas WPI

Surface hydrophobicity 66 ± 3 6±2 56 ± 3 44 ± 1

EC (mL oil/g of protein) 324 ± 8 252 ± 7 408 ± 19 356 ± 4

ES (%) 94 ± 6 77 ± 3 63 ± 1 61 ± 1

FA (%) 98 ± 3 177 ± 14 238 ± 3 217 ± 7

FS (min) 16 ± 1 4±1 10 ± 1 29 ± 3

low because the solutions were a mixture of proteins interacting

Fig. 4. Solubility of proteins fromf HB (black dots) and PE (grey dots) versus pH.
In native conditions, pH was measured close to 6.0 for HB and
5.0 for PE. The solubility of proteins from HB was constant between
85 and 90%, whatever the pH. This can be explained by the presence
of salts that induced a high ionic force. As a consequence, acid or
base could not interact with charged groups of proteins. PE
exhibited different behaviours: nearly half of the proteins were not
soluble for pH values between 6.0 and 9.0. In this pH range, the
colour of the solution also changed from dark reddish to white.
Proteins of both effluents were then used at native pH.
Solutions containing 2% wt of proteins from HB and PE were
tested for surface and interfacial tension and compared with Na-
Cas and WPI. Concerning surface tension (Fig. 5a), equilibrium
values were similar for HB and PE (between 49 and 50 mN/m).
Proteins from both effluents had less ability to lower surface ten-
sion than Na-Cas and WPI, which had equilibrium values respec-
tively of 45 and 42 mN/m. The presence of other compounds (salts,
sugars) in the solution containing effluent proteins negatively
affected the behaviour of these proteins at the water-air interface.
Equilibrium value was reached in a short time for PE, whereas the
surface tension decreased more progressively for HB. Interfacial
measurements (Fig. 5b) revealed similar behaviour for all the pro-
teins: their kinetics had the same tendency and their equilibrium
values were in the same range, between 13 and 15 mN/m.
Results of other surface properties are presented in Table 3.
Surface hydrophobicity was in the same range for PE, Na-Cas and
WPI. Typical values for surface hydrophobicity were of several
hundreds for isolated proteins. In this case, the values were rather
with each other, and solubility was not complete (Fig. 4). This
phenomenon contributed to the decrease of fluorescence. It was
even lower for HB due to the presence of salts, which also attenu-
ated the fluorescence of the solution. Proteins of PE and HB had
good emulsifying properties. Even if emulsion capacity values were
lower than those of Na-Cas and WPI, they were of the same order of
magnitude and sufficient for future applications, as oil represented
nearly 80% of the volume of the emulsion when it was destabilised.
Stability of emulsions with HB and especially PE were even higher
than the commercial ingredients. Concerning the foaming proper-
ties, HB had good foaming ability as it was just below those of Na-
Cas and WPI. However, if the amount of produced foam was large
its stability was poor, since 4 min were necessary to reduce the
foam volume by half. In this case, the presence of salt in the solution
explained this behaviour, as salt is known to reduce the stability of
foams. On the other hand, PE had a rather low foaming ability, less
than the half of that of Na-Cas and WPI, but the stability of the
generated foam appeared to be quite competitive with the com-
mercial proteins.
4. Discussions
PE had nearly the protein concentration of an isolate (92%) and
could thus be reused as a “pork meat protein isolate” if slightly
concentrated. The nutritional value of PE proteins was found as
high as for meat, and matches with dairy products. In pork muscle,
soluble proteins in the absence of salt are sarcoplasmic proteins and
proteins from plasma or remaining blood. The SEC profile of the PE
was indeed representative of these proteins with, for example, al-
bumin and/or haemoglobin at 66 kDa and myoglobin around
15 kDa, which gave the reddish-pink colour to the solution. SDS-
PAGE showed a very large variety of proteins between 20 and
100 kDa. An explanation may be that some myofibrillar proteins,

Fig. 5. Variation in surface tension (a) and interfacial tension (b) of solutions at 2% wt proteins from HB, PE, Na-Cas and WPI versus time at 20
C.
 A.-V. Ursu et al. / Journal of Food Engineering 190 (2016) 54e60
normally insoluble in native conditions, have been subject to pro-
teolysis. Hwang et al. (2005) have indeed detected a decrease in
some myofibrillar proteins or subunits in pig meat during the days
following slaughter. Bauchart et al. (2006) also discovered this
tendency in beef meet and noticed the presence of peptides with a
molecular weight below 5 kDa, which was also the case in PE for
30e40% of the proteins detected by SEC.
PE relatively low initial pH value (5.0) tends to confirm this
hypothesis, as meat pH values are usually close to 6.0 and decrease
over time (Toldra  et al., 2010). Ph-shifting could be used to recover
sarcoplasmic proteins, as shown in Fig. 4. The change of colour of
the solution was due to myoglobin and/or haemoglobin, which are
known to be insoluble close to a pH value equal to 7.0, but other
sarcoplasmic proteins also precipitate around neutral pH. However,
precipitation is much more delicate at the high initial concentration
(14% wt) than at the 2% of the solubility curves. PE is quite similar to
WPI and Na-Cas (high protein content and presence of native
proteins); it is therefore not surprising for PE to have comparable
functional properties, the main difference residing in the coagula-
tion temperature. It first occured between 40 and 50
C for PE,
which is in the range for sarcoplasmic proteins (Tornberg, 2005)
while for dairy products, a temperature of 80
C is necessary. This
explains the high emulsion stability value observed in Table 3. In
this case, the emulsion was stabilised by the partial or nearly total
coagulation of PE proteins, whereas this was barely the case for Na-
Cas and WPI.
HB was very different from PE: its protein content was only 50%
of dry matter. Consequently additional purification would be
necessary to make a protein isolate from HB. Salts and sugars
detected in HB are current additives used during salting in the
production of standard quality hams. Fats are not totally insoluble
in HB, and some may have been hydrolysed during the cooking
process. Collagen is also liberated during the salting and cooking
process (Tornberg, 2005), as it is not soluble in water in its native
form in the muscle. Proteins recovered in HB have undergone a long
heat treatment at between 70
C and 80
C. So, it is not surprising to
find small proteins or subunits of myofibrillar proteins and con-
nective tissue (collagen) that have not coagulated to form ham.
Bauchart et al. (2006) have detected fragments of troponin T at
30 kDa and a large quantity of peptides of less than 5 kDa with a
high histidine content after cooking beef meat. The results from
that study seem to be in agreement for pig meat, as 70% of HB
proteins were below 5 kDa and histidine was the major amino acid.
As the solubility of HB remained high whatever the pH, separation
by pH-shifting was not achievable in this case. Among the func-
tional properties, the low-temperature gelation of HB was probably
due to collagen. Gel forces were weak, due to the presence of the
small proteic chains and low collagen concentrations. However, this
result could be changed by concentrating HB. Collagen also in-
fluences the other properties, as it is known to have surface prop-
erties (Go mez-Guillen et al., 2011). However, HB still had surface
properties after microfiltration at 0.2 mm demonstrating that others
proteins were also surface agents.
According to these results, both effluents are good candidates
for functional ingredients. Valorisation of HB is more crucial than
PE, due to the relative amounts recoverable in the ham production
process. HB could be a source of collagen, but concentrations are
low and supplementary purification steps are required and finding
sources of collagen which are alternative to pork collagen raises
mez-Guille n et al., 2011). The re-use of HB as a
large interest (Go
substrate for energy vector production or fertilizers due to high
nitrogen content could be an alternative, but high salt content can
be a drawback. The best valorisation seems then to be as a food
ingredient. HB, but also PE, could replace dairy proteins in meat
formulations. In this case, the content of carbonyl compounds in PE
59
should be evaluated in future to validate their use as food in-
gredients. The presence of hydroperoxides, lipidic peroxides,
deaminated or decarboxylated side-products should be checked as
they can appear during heat treatments of solutions with proteins,
fat and sugars. The cooking process at low temperature 70
C with
anti-oxidative agents added during the salting and under vacuum
should nonetheless prevent or limit their formation.
5. Conclusion
In this work, two effluents of ham production at industrial scale
were collected and characterised: ham broth and pork exudate.
Both by-products are a source of proteins with good nutritional
properties. Furthermore, their proteins have intrinsic functional
properties such as emulsifying, foaming or gelling. In order to
prevent bacteria development and contamination, ham broth and
pork exudate, having low viscosity can easily be processed into
powders by spray-drying without losing their functional proper-
ties. These proteins could not be used as widely as dairy proteins
but could find valorisation as functional ingredient for delicatessen
products such as mousse or sausage or for domestic animal prep-
arations with a smell and taste of ham.
Acknowledgements
The authors gratefully acknowledge the European Regional
Development Fund (FEDER) and Oseo for their financial support.
Nouredinne Hafnaoui is gratefully acknowledged for his help dur-
ing this study.
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