Journal of Food Composition and Analysis 41 (2015) 212220

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Journal of Food Composition and Analysis

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Original Research Article

Characterisation of the lipid and protein fraction of fresh camel meat

and the associated changes during refrigerated storage
Sajid Maqsood a,*, Aisha Abushelaibi a, Kusaimah Manheem a, Isam Tawk Kadim b
a
b

Department of Food Science, College of Food and Agriculture, United Arab Emirates University, Al Ain 15551, United Arab Emirates
Department of Animal and Veterinary Sciences, College of Agricultural and Marine Sciences, Sultan Qaboos University, Oman

A R T I C L E I N F O

A B S T R A C T

Article history:
Received 4 August 2014
Received in revised form 1 December 2014
Accepted 17 December 2014
Available online 21 February 2015

Characterisation of protein and lipid fractions of fresh camel meat and their associated changes were
investigated during 9 days of refrigerated storage. Camel meat lipids contained palmitic acid (C16:0) as
dominant fatty acid followed by stearic acid (C18:0) and oleic acid (C18:1 n-9). Content of total saturated
fatty acid (SFA) and unsaturated fatty acids were 58.46 and 41.5 mg/100 g, respectively. Total
unsaturated fatty acids were reduced at the end of storage. Lipids underwent rapid oxidation as
indicated by increase in peroxide value (PV) and thiobarbituric acid reactive substances (TBARS).
Decrease in total haem pigment, myoglobin and haemoglobin content with concomitant decrease in
redness (a* value) was noticed during the storage. Protein extractability, solubility, TCA-soluble peptides
and drip loss increased during storage indicating proteolysis and degradation of structural proteins,
which was also evident from SDS-PAGE pattern. This further corroborates with the decrease of textural
parameters like hardness, cohesiveness, springiness and gumminess. Thus, the protein and lipid fraction
of camel meat underwent considerable changes during refrigerated storage. Therefore, the behaviour of
protein and lipid fraction in camel meat during refrigerated storage could provide better understanding
of the processing and storage conditions.
2015 Elsevier Inc. All rights reserved.

Keywords:
Camel meat
Food composition
Proteolysis
Fatty acid analysis
Protein characterisation
Lipid oxidation
Food analysis
Food processing

1. Introduction
With increasing demand for the meat and meat products due to
increasing human population, there is an urgent need to look for
marginal and underutilised options for the supply of red meat, such
as those in semi-arid and arid lands, of which camel meat is
certainly the most suitable one. There are approximately 25
million camels in the world where the global market for camel
products has a potential of US$10 billion a year based of Food and
Agriculture Organisation (FAO) of United Nations. United Arab
Emirates is known to possess 412,000 camels (FAOSTAT, 2008).
Camels are used for many purposes such as meat and milk
production, and for physical labour as well as racing. Camel meat
is known to be more benecial for health because the meat
contains lower fat and cholesterol levels than other red meats
(Gheisari and Ranjbar, 2013). Camel meat is also relatively high in
polyunsaturated fatty acid (PUFA) in comparison to other red

* Corresponding author. Tel.: +971 37134519; fax: +971 37675336.

E-mail address: sajid.m@uaeu.ac.ae (S. Maqsood).
http://dx.doi.org/10.1016/j.jfca.2014.12.027
0889-1575/ 2015 Elsevier Inc. All rights reserved.

meat (Gheisari and Ranjbar, 2013), which contributes to its healthpromoting benets. Consumption of camel meat can therefore lead
to a reduction in total fat and cholesterol intake and an increase in
PUFA as compared with other conventional meat sources. Moreover,
camel meat is also used for medicinal purposes in diseases such as
hyperacidity, hypertension, pneumonia, and respiratory disease; it is
also known as an aphrodisiac (Kurtu, 2004). Such a diet can be
expected to reduce cardiovascular diseases and improve health
(Rawdah et al., 1994). Thus, camel as a meat source seems to present
a viable alternative to other red meats.
The compositional quality of fresh camel meat can be affected
by problems encountered during refrigerated storage, i.e. lipid
oxidation, discoloration, proteolysis and increase of drip loss, etc.
Camel meat is the least studied meat and is mistakenly believed to
be of lower nutritive value and quality than other types of red meat
(Abdelhadi et al., 2013). Although camel meat is not universally
consumed, it might be a potential alternative for meat, particularly
in arid/semi-arid regions where camels can thrive well and are
produced in a much more economical manner than cattle.
Low-temperature storage is one of the primary preservation
methods to maintain meat freshness, because the rates of

S. Maqsood et al. / Journal of Food Composition and Analysis 41 (2015) 212220

microbiological, chemical and biochemical changes are reduced at

lower temperatures. Therefore, it is important to study and
monitor the changes the meat undergoes during low-temperature
storage. For instance post-mortem refrigerated storage of meat,
often termed as maturation or ageing, permits desirable degradative structural changes in myobrillar and connective tissue
proteins which enhance its palatability (Takahashi, 1996). Meat
carcasses are held in refrigerated storage for varying periods to
improve tenderness, the most important meat quality. Furthermore, during the retail display, the colour of the meat is affected
signicantly. All these quality attributes are related with the postmortem changes in the protein and lipid fractions of the meat.
Overall, there is a lack of research on camel meat to attain the
better understanding of camel meat properties and their changes
during refrigerated display. Some scientically sound studies have
been conducted concerning the physical characteristics, chemical
composition and nutritive values of camel meat (El-Faer et al.,
1991; Elgasim and Alkanhal, 1992; Dawood and Alkanhal, 1995;
Dawood, 1995; Kadim et al., 2006, 2013). However, there is no
information available about the changes in protein and lipid
fraction during refrigerated storage, which is very important to
gain a better understanding of camel meat.
Therefore, the aim of this research was to characterise the
protein and lipid fractions and to study their associated changes in
fresh camel meat during refrigerated storage.
2. Materials and methods

213

characterisation of protein and lipids, and another portion was used

for studying the changes in protein and lipid fraction and assessing
quality parameters during storage at 4 8C. During storage, the samples
were taken and evaluated after every 3rd day up to 9 days.
2.3. Characterisation of lipid fraction of camel meat and its changes
2.3.1. Lipid extraction and analysis of fatty acids composition
Lipids from the fresh camel meat (day 0) and those stored for
9 days were extracted by the method of Bligh and Dyer (1959)
using chloroform:methanol:distilled water mixture (50:100:50) as
an extraction solvent. After extraction, the solvent was evaporated
at 25 8C, using an EYELA rotary evaporator N-100 (Tokyo, Japan),
and the residual solvent was removed by ushing with nitrogen.
Fatty acid prole of extracted camel meat lipids was determined as
fatty acid methyl esters (FAMEs) as described by Maqsood and
Benjakul (2010c). Supelco 37-Component FAME Mix (SigmaAldrich,
PA, USA, Cat No. 47885-U) was used for identication of different fatty
acids. Fatty acid concentration was calculated by using C23 internal
standards (purity >99%) (SigmaAldrich, PA, USA). Average from the
three runs was expressed as g fatty acid/100 g lipid.
2.3.2. Peroxide value (PV)
Peroxide value (PV) of the camel meat was determined as per
the method of Richards and Hultin (2002) with a slight
modication. A standard curve was prepared using cumene
hydroperoxide at the concentration range of 0.52 mg/kg. Peroxide
value was expressed as mg of hydroperoxide/kg of sample.

2.1. Chemicals
Chloroform, ethanol, acetone and anhydrous sodium sulfate
were obtained from BDH Prolabo (Briare, France). Methanol,
sodium chloride, hydrochloric acid and glacial acetic acid were
obtained from Scharlau Chemicals (Barcelona, Spain). Ammonium
thiocyanate and trichloroacetic acid were procured from Panreac
AppliChem (Barcelona, Spain). Iron (II) chloride and Coomassie
brilliant blue R-250 was procured from AppliChem (Darmstadt,
Germany). Cumene hydroperoxide (80% purity), thiobarbituric acid
(>98% purity), 1,1,3,3-tetramethoxypropane (MDA) (99% purity),
tyrosine (>98% purity), sodium phosphate dibasic, sodium dodecyl
sulfate (SDS) (>98.5% purity), b-mercaptoethanol (b-ME), wide
range molecular weight marker and bovine serum albumin (BSA)
(>98% purity), were procured from Sigma-Aldrich Chemical Co. (St.
Louis, MO, USA). All other chemicals used were of analytical grade.
2.2. Preparation of camel meat samples
Six female camels (Arabian dromedary one-humped camel,
Camelus dromedarius), which have been reared in a semi-intensive
management system and fed ad libitum on a Rhodes grass (Chloris
gayana) hay diet mixed with date seed powder, were slaughtered
at 35 years of age and when they had reached 410  25 kg, at an Al
Ain slaughterhouse in the United Arab Emirates (UAE). UAE-Standard
No. 993/2000 concerning animal slaughtering requirements according to Islamic law was followed to slaughter the camels. Semitendinosus (ST) muscle was carefully separated with a sharp knife from the
carcass of the camels within 24 h of slaughter. Separated meat
portions were packed in polyethylene bags and stored in insulated
box lled with ice during transportation to laboratory of Department
of Food Science, UAE University. Upon arrival, the meat was washed
with chilled deionised water, cut into similar-sized pieces
(3 cm  3 cm  3 cm), and the connective tissue and fat deposits
were removed manually. Meat samples obtained from the carcass of
the six female camels were divided into three batches (or replicates)
and placed on separate polystyrene trays wrapped with shrink lm.
One portion from each batch or replicate was subjected to

2.3.3. Thiobarbituric acid reactive substances (TBARS)

TBARS in the camel meat were determined as described by
Buege and Aust (1978). A standard curve was prepared using
1,1,3,3-tetramethoxypropane (MDA) at the concentration ranging
from 0 to 10 mg/kg and TBARS was expressed as mg of MDA
equivalents/kg sample.
2.4. Changes in haem pigment
2.4.1. Determination of total haem pigment
Total haem pigment in the camel meat was determined according to
the method of Hornsey (1956) with some modications. A ground
sample (10 g) was weighed into a 50-mL polypropylene centrifuge
tube. To this was added about half of an acidied acetone solution
containing 40 mL of acetone, 9 mL of water (taking into account the
amount of moisture in the meat) and 1 mL of HCl. Each sample was
homogenised at 13,500 rpm for 15 s using a Ultra-Turrax T25 high
speed homogeniser (Janke & Kunkel, Staufen, Germany), and remaining
acidied acetone solution was added. The samples were mixed
thoroughly, and the tubes were capped tightly and allowed to stand in
the dark for 1 h. The homogenate was centrifuged at 2200  g for
10 min at 4 8C using a Allegra X 30R refrigerated centrifuge (Beckman
Coulter, Brea, California, USA). The supernatant was ltered with
Whatman No.1 lter paper (Whatman International, Ltd, Maidstone,
UK) and the absorbance was measured at 640 nm against a reagent
blank using a UV-1601 spectrophotometer (Shimadzu Corporation,
Kyoto, Japan). The absorbance was multiplied by the factor 6800 and
then divided by the sample weight to give the concentration of total
pigments in the meat as mg haematin/g meat (Turhan et al., 2004).
2.4.2. Determination of haemoglobin content
To determine haemoglobin content in the camel meat,
haemolysate was prepared according to the method of Richards
and Hultin (2002) with slight modication. In brief, 5 g of meat
and 15 mL of 80 mM KCl were mixed with 50 mM TrisHCl buffer
(pH 8.0) in a polypropylene centrifuge tube. The sample was
homogenised for 2 min at 3500 rpm, rinsed with additional 5 mL

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S. Maqsood et al. / Journal of Food Composition and Analysis 41 (2015) 212220

of the buffer and centrifuged at 3500  g at 4 8C for 30 min. The

supernatant was referred to as haemolysate and used for
quantication of haemoglobin. Haemoglobin content in the
prepared haemolysate was determined following the method
described by Maqsood and Benjakul (2011). The haemoglobin
concentration was calculated by LambertBeers law using a
millimolar extinction coefcient of 125 for oxyhaemoglobin at
pH 8 (Antoni and Brunoni, 1971) and expressed in mM.
2.4.3. Determination of myoglobin content
Myoglobin content was determined by direct spectrophotometric
measurement. A ground sample (2 g) was weighed into a 50 mL
polypropylene centrifuge tube and 20 mL of cold 40 mM phosphate
buffer, pH 6.8, were added. The mixture was homogenised at
13,500 rpm for 10 s, followed by centrifuging at 3000  g for 30 min
at 4 8C, using a Allegra X 30R refrigerated centrifuge (Beckman
Coulter, Brea, California, USA). The supernatant was ltered with
Whatman No. 1 lter paper. The supernatant (2.5 mL) was treated
with 0.2 mL of 1% (w/v) sodium dithionite to reduce the myoglobin
and the absorbance was read at 555 nm. Myoglobin content was
calculated from the millimolar extinction coefcient of 7.6 and a
molecular weight of 16,110 Da (Gomez-Basauri and Regenstein,
1992). The myoglobin content was expressed as mg/g sample.

a portable digital pH metre attached with a probe (Model pH 510,

Eutech Instrument, Ayer Rajah Crescent, Singapore). Three readings were taken by dipping the pH metre probe in the homogenate
and mixing the homogenate on a magnet stirrer until the reading
was stable. The pH metre was calibrated after every three readings
using two buffers of pH 4.0 and 7.0.
2.6.2. Colour determination
Colour of the ground camel meat was measured using a Hunter
Lab colorimeter (Model colour Flex, Reston, VA, USA) with the port
size of 0.50 in. The determination of colour was done on six
different samples. Standardisation of the instrument was done
using a black and white Minolta calibration plate. The colour values
were calculated based on illuminant C and the 108 standard
observer (CIE). The values were reported in the CIE colour prole
system as L*-value (lightness), a*-value (redness/greenness), and
b* value (yellowness/blueness) on day 0, 3, 6 and 9 of storage.
2.6.3. Drip loss
The drip loss of the camel meat was calculated from differences
in the weight taken before and after storage at 4 8C and the results
were expressed as average proportion (Honikel, 1998). The percent
change in weight over the subsequent 48 h was taken as the drip
loss, as described by Honikel (1998).

2.5. Characterisation of protein fraction

2.5.1. Protein patterns by sodium dodecyl sulfate polyacrylamide gel
electrophoresis (SDS-PAGE)
Fresh camel meat (day 0) and those stored for 9 days were
subjected to SDS-PAGE according to the method of Laemmli (1970)
as described by Maqsood and Benjakul (2010c). Wide range
molecular weight markers ranging from 200 kDa to 20 kDa was
used for estimation of molecular weight of proteins.
2.5.2. Determination of protein extractability, total protein solubility
and
TCA-soluble peptides
To determine protein extractability in camel meat, 10 grams of
camel meat was mixed with 20 mL of 5% NaCl solution, homogenised for 5 min, incubated (4 8C) for 1 h, and centrifuged at
30,000  g (14,000 rpm) for 20 min (Gordon and Barbut, 1992).
Biuret protein assay was used to determine protein concentration in
the salt soluble protein extracts using bovine serum albumin
(SigmaAldrich Chemical Co., St. Louis, MO, USA) as a standard.
Protein extractability was expressed as mg of protein/g of sample.
Total protein solubility was determined by the method described by
Joo et al. (1999). Total proteins were extracted from 1 g camel meat
using 20 mL of ice-cold 1.1 M potassium iodide in 0.1 M phosphate
buffer (pH 7.2). The samples were minced, homogenised on ice, and
then left on a shaker at 4 8C overnight. Samples were then
centrifuged at 1500  g for 20 min, and protein concentration in
the supernatants was determined by the Biuret method. Total
protein solubility was expressed as mg of protein/g of sample.
TCA-soluble peptides in the camel meat were determined
according to the method of Morrissey et al. (1993). Meat samples
(3 g) were homogenised with 27 mL of 5% TCA (w/v) at speed of
19,000 rpm using a homogeniser. Homogenate was kept in ice for
1 h and centrifuged at 5000  g for 5 min. The soluble peptides in
supernatant were measured by the Lowry method and expressed
as mg of protein/g of sample (Lowry et al., 1951).
2.6. Changes in meat quality during refrigerated storage
2.6.1. Changes in pH of camel meat
To determine pH, 10 g of the sample was homogenised with
50 mL of chilled distilled water. The pH values were measured with

Drip loss %

"
#
weightsample before cooling  weightsample after cooling
weightsample before cooling
 100

2.6.4. Textural prole analysis (TPA)

TPA of the camel meat cubes (3 cm  3 cm  3 cm) were
performed using a texture analyser (CT3-4500, Brookeld Engineering Laboratories, Middleboro, MA, USA) with cylindrical
aluminium probe (50 mm diameter) as described by Maqsood
et al. (2012). Hardness, springiness, cohesiveness, gumminess and
chewiness were calculated from the forcetime curves generated
for each sample on day 0 and day 9 (Bourne, 1978).
2.7. Statistical analysis
Meat portion removed from the carcasses of six different female
camels were characterised and analysed for different parameters
in triplicate. The experimental data were subjected to Analysis of
Variance (ANOVA) and the signicant differences between mean
values obtained at different sampling days were evaluated by
Duncans Multiple Range Test/least signicant difference (Steel
and Torrie, 1980). Data analysis was performed using an SPSS
package (SPSS 14.0 for Windows, SPSS Inc, Chicago, IL, USA).
3. Result and discussion
3.1. Characterisation and changes in lipid fraction of camel meat
3.1.1. Changes in fatty acid prole of the camel meat lipids
Semitendinosus (ST) muscle of the camels contains
4.82  0.84% of total fat and 71.77  3.84% of moisture. Fatty acid
prole of lipids extracted from fresh camel meat and those stored for
9 days at 4 8C is displayed in Table 1. Camel meat lipids (day 0)
contained palmitic acid (C16:0) as dominant fatty acid followed by
stearic acid (C18:0) and oleic acid (C18:1 n-9). Kadim et al. (2013) also
reported that palmitic acid (C16:0) is the most abundant saturated
fatty acid in camel intramuscular fat followed by stearic acid (18:0),
and myristic acid (C14:0). The monounsaturated fatty acids (MUFA)

S. Maqsood et al. / Journal of Food Composition and Analysis 41 (2015) 212220

215

Table 1
Changes in fatty acid composition of lipids extracted from camel meat on day 0 and day 9 of refrigerated storage.
Fatty acids

Common name

0 day

9 day

Saturated FA
C10:0
C12:0
C13:0
C14:0
C15:0
C16:0
C17:0
C18:0
C20:0

Capric acid
Lauric acid
Tridecylic acid
Myristic acid
Pentadecylic acid
Palmitic acid
Margaric acid
Stearic acid
Arachidic acid

0.39  0.094a
0.16  0.069a
0.71  0.084a
5.88  1.98b
1.99  0.13a
29.64  2.74b
1.98  0.15a
16.56  2.15a
1.15  0.097a

0.36  0.090a
0.17  0.071a
0.68  0.088a
6.19  1.99a
1.94  0.12a
30.33  2.95a
1.97  0.14a
16.94  1.95a
1.53  0.099a

Mono-unsaturated FA
C14:1
C15:1
C16:1
C17:1
C18:1 n-9

Tetradecenoic acid
Ginkgolic acid
Palmitoleic acid
Ginkgolic acid
Oleic acid

0.43  0.079a
0.47  0.077a
3.15  1.51a
0.79  0.094b
24.48  2.45b

0.44  0.083a
0.56  0.82a
3.07  1.49a
0.92  0.099a
25.17  2.55a

Poly-unsaturated FA
C18:2n6t
C18:2n6c
C18:3n6
C18:3n3
C20:2
C20:3n3
C20:4n6
C22:2
C22:6n3

Linoleic acid (trans)

Linoleic acid (Cis)
Gamma linolenic acid
Alpha linolenic acid
Eicosadienoic acid
Eicosatreinoic acid
Arachidonic acid
Docosadienoic acid
Docosahexaenoic acid

2.23  0.25a
3.46  0.26a
2.03  0.198a
1.90  0.12a
0.08  0.006a
0.21  0.007b
1.87  0.118a
0.14  0.008a
0.31  0.009a

2.07  0.23b
3.01  0.25b
1.39  0.198b
1.34  0.106b
0.07  0.004a
0.29  0.009a
1.22  0.119b
0.15  0.009a
0.21  0.008a

Total saturated FA
Total unsaturated FA
Total mono-unsaturated FA
Poly-unsaturated FA
Ratio of n-6/n-3

58.46
41.54
29.32
12.23
3.96

60.11
39.89
30.16
9.75
4.17

Values are mean  SD from 3 determinations. Different letters in the same row for each fatty acid at different storage time denote the signicant difference (P < 0.05).

contributed to about 30% of total fatty acids and among them oleic
acid (C18:1n9c) followed by palmitoleic acid (C16:1) were the major
ones. Rawdah et al. (1994) also reported that MUFA in camel meat
account for almost one-third of the total fatty acids and are
dominated by oleic acid followed by palmitoleic acid. Content of
total saturated fatty acid (SFA) and unsaturated fatty acids were
58.46 and 41.5 mg/100 g, respectively, indicating that camel meat
lipids were dominated by saturated fatty acid with considerably high
amounts of unsaturated fatty acids. Among the unsaturated fatty acid,
camel meat lipid contain 29.23 mg/100 g of mono-unsaturated fatty
acids (MUFA) and 12.23 mg/100 g of poly-unsaturated fatty acids
(PUFA). High amount of unsaturated fatty acids (41.54 mg/100 g)
could play a major role in making the lipids more susceptible to lipid
oxidation. The dominant PUFA in the camel meat lipid was linoleic
acid (Cis) (C18:2n6c). Kadim et al. (2013) also reported that the main
polyunsaturated fatty acids in the muscles were linoleic acid
(C18:2n6c). This nding further corroborates with those reported
by Rawdah et al. (1994). These unsaturated fatty acids in camel meat
lipids underwent oxidation during the refrigerated storage for 9 days.
This was evidenced by the decrease in total unsaturated fatty acids
from 41.54 to 39.89 mg/100 g and PUFA from 12.23 to 9.75 mg/100 g
on day 9 of storage. This was in agreement with the high formation of
PV and TBARS in the camel meat on day 9 of storage (Fig.1). Decrease
in PUFA was coincidental with an increase in saturated fatty acids at
the end of refrigerated storage. When comparing fatty acids between
camel meat lipids at day 0 and day 9, there was a noticeable decrease
in some of the PUFA especially C18:2n6, C18:3n6, C18:3n3 and
C20:4n6. PUFA reduction was due to oxidative and hydrolytic
reactions that occurred during the storage. Yi-Chen et al. (2008)
showed that long hydrocarbon chains and high unsaturation of PUFA
made them more susceptible to hydrolytic reactions than the SFA.
Decrease in PUFA resulted in corresponding increase of SFA when
compared to the total fatty acid. Fatty acid composition of meat can

play an important role in determining the health benets of meat to

consumers. The ratio between n-6 and n-3 fatty acids have important
role to play in reducing the risk of coronary heart disease (American
Heart Association, 2008). Ratio of n-6/n-3 in the camel meat found in
the present study is 3.96, which is within the range of recommended
value of lower than 4 (British Department of Health, 1994). Enser et al.
(1996) reported that n-6/n-3 ratio of beef, lamb and pork meat was
2.11, 1.32 and 7.22, respectively. The low n-6/n-3 levels are desirable
for meat consumers health reasons (British Department of Health,
1994). Ratio of n-6/n-3 in camel meat lipids is very well in the
recommended range of less than 4. Consumption of food with high
proportion of MUFA and PUFA is related with lowering of serum
cholesterol levels (Rawdah et al., 1994). Camel meat is known to
contain higher percentage of MUFA and PUFA and lower cholesterol
than beef, therefore, can be considered as an alternative healthy red
meat.
3.1.2. Changes in lipid oxidation products
Changes in peroxide value (PV) and thiobarbituric acid reactive
substances (TBARS) values of camel meat during refrigerated
storage are shown in Fig. 1(a) and (b), respectively. A continuous
increase in PV was observed in the sample during the rst 6 days.
Thereafter, a sudden decreased in PV was noticed up to day 9 of
storage (P < 0.05). The results suggested that the camel meat
underwent lipid oxidation at a pronounced rate during the rst
3 days of storage. After 6 days of storage, the hydroperoxide
formed might undergo decomposition to form secondary lipid
oxidation products (Maqsood and Benjakul, 2010a). Therefore, a
decrease in the peroxide value on day 9 was related to
hydroperoxide degradation. Lee et al. (2010) reported that the
peroxide value of the raw ground pork meat increased until 7 days
and reached the maximum value at a certain storage time and
decreased thereafter during 14 days of refrigerated storage.

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S. Maqsood et al. / Journal of Food Composition and Analysis 41 (2015) 212220

b)
8

TBARS (mg MDA/kg sample)

c
4

a
3

1
0

0
0

c)

d)

Mb

Myoglobin (mg/g sample)

100

95

a
b

90

bc

Storage me (Days)

Storage me (Days)

Total haem pigment

(g haeman / g meat)

b
2

85

14
12

0.14

10
8

Hb

0.1

a
c

bc

3
6
Storage me (days)

0.08

0.06

0.04

0.02
0

80

0.12
Haemoglobin (mM)

PV (mg of hydroperoxide/kg
sample)

a)

3
6
Storage Time (Days)

Fig. 1. Changes in peroxide value (a); thiobarbituric acid reactive substances (b); total haem pigment (c) and myoglobin and haemoglobin content (d) in camel meat during
refrigerated storage. Values are mean  SD from 18 determinations. Different letter at different storage time indicates the signicant difference (P < 0.05).

Even though TBARS assay is widely used on the food

laboratories for monitoring lipid oxidation in the food matrix,
however, components like ketones, ketosteroids, acids, esters,
sugar, protein and vitamins can react with TBA and thus can
interfere with the assay (Devasagayan et al., 2003). In the present
study, TBAR assay might have overestimated the values. TBARS
values of the camel meat increased as the storage time increased
(P < 0.05) (Fig.1(b)). The initial value of TBARS was 0.25 mg/kg
meat, suggesting that lipid oxidation had occurred during postmortem handling to some extent. TBARS showed a marked
increased within the rst 3 days of storage indicating that camel
meat was highly susceptible to lipid oxidation and lipids
underwent oxidation rapidly during storage. TBARS showed a
slight increase from days 3 to days 6 of storage (P > 0.05).
Thereafter, it increased sharply until the end of storage (P < 0.05).
The increase in TBARS indicated formation of secondary lipid
oxidation products which contribute to the off-odour development
in the meat. The increases in TBARS were coincidental with the
decrease in PV from 6 to 9 days of storage. This was probably due to
the degradation of hydroperoxides into secondary oxidation
products, especially aldehydes, in the later stages of lipid oxidation
(Maqsood and Benjakul, 2010b). Fallah et al. (2010) also reported
that TBARS value of non-irradiated camel meat increases when
storage time increases for 15 day of refrigerated storage. Gheisari
(2011) reported that the camel meat showed the higher TBARS
than cattle and chicken and the values increased with an increase
in storage time. Camel meat is known to contain high amount of
myoglobin and other haem compounds which function as prooxidants to promote lipid oxidation (Maqsood and Benjakul, 2011).
Therefore, the presence of high amount of PUFA and pro-oxidants
like haem pigment (myoglobin and haemoglobin) makes camel
meat highly prone to lipid oxidation.

3.2. Changes in haem pigments in camel meat during storage

3.2.1. Changes in total haem pigment
Changes in total haem pigment of camel meat during 9 days of
refrigerated storage are shown in Fig. 1(c). Total haem pigment is a
measure of haematin, which is related to haem containing proteins
such as myoglobin, haemoglobin and cytochrome. Total haem
content of the fresh camel meat in this study was found to be
92.3 mg haematin/g of sample which is higher than what was
found in beef (76.16 mg haematin/g of sample) (Maqsood and
Benjakul, 2010b). Presence of high haem content in the fresh
camel meat might contribute to its susceptibility to lipid
oxidation. Total haem pigment gradually decreased as the storage
time increased from day 0 to day 9 (P < 0.05). At day 0, total
pigment of camel meat was 92.38 mg haematin/g meat and it
decreased to 86.4 mg haematin/g meat on day 9 of refrigerated
storage. The decrease could be due to the denaturation and
oxidation of haem pigment during storage. It was postulated that
the haem pigment can display lower extraction efciency with
increasing storage time which might have resulted in the decrease
of haem content of the meat (Chaijan et al., 2005). Decrease in total
haem pigment during storage has been reported in different red
meats like lamb, beef and pork (Luciano et al., 2009; Maqsood and
Benjakul, 2010b). Total haem plays an important role in the colour
of fresh meat. Pigments in red meats like camel meat are
especially vulnerable to oxidation, which causes deep yellow or
brown discoloration during handling, chilling, and frozen storage.
The decrease in haem pigment during storage in the camel meat
corroborates well with the decrease in redness (a*) values (Table
2). The decrease of haem pigment during storage can also play an
important role in the lipid oxidation of the meat. Damage and
denaturation of the haem pigment with increasing storage time

S. Maqsood et al. / Journal of Food Composition and Analysis 41 (2015) 212220

217

Table 2
Changes in textural properties and colour values of camel meat during 9 days of refrigerated storage.
Storage time (days)

Hardness (g)

Cohesiveness

Springiness (mm)

Gumminess (g)

Chewiness (mJ)

Textural properties
0
9

3228  39.60a
927.5  23.03b

0.61  0.01b
0.73  0.02a

6.4  0.1a
5.30  0.22b

2235  17.07a
774.1  27.98b

146.39  5.01a
40.13  4.98b

Storage time (days)

L*

a*

b*

Colour values
0
3
6
9

34.44  0.42c
35.46  1.23c
37.59  1.14a
38.83  0.11b

19.98  1.48a
16.73  0.66b
12.81  0.46c
11.58  0.72d

17.78  1.05a
15.72  0.91b
15.03  0.66cb
14.75  0.04c

For textural properties and for colour, values are mean  SD (n = 18). Different letters in the same column for each parameter at different storage time denote the signicant
difference (P < 0.05).

results in the release of iron which can accelerate lipid oxidation

(Maqsood and Benjakul, 2010b).
3.2.2. Changes in myoglobin and haemoglobin
Myoglobin and haemoglobin content of camel meat during
9 days of refrigerated storage are shown in Fig. 1(d). Haemoglobin
and myoglobin are known to be potent catalysts of lipid oxidation
in muscle foods (Maqsood and Benjakul, 2011). In the present
study, average myoglobin content of the camel meat was 7.16 mg/
g of sample. Gheisari (2011) reported that camel meat contain
myoglobin content of 3.64 mg/g of sample. The lower myoglobin
content in the study of Gheisari (2011) might be due to the
different extraction solvent and extraction conditions used.
Moreover, the portion of the camel carcass used in the study of
Gheisari (2011) was different than ours. In the present study, an
increase in myoglobin and haemoglobin content were observed in
the camel meat on the day 3 of storage. Thereafter, a continuous
decrease in myoglobin and haemoglobin content was noticed up to
day 9 of storage (P < 0.05). It was reported that the lower tendency
of the haem proteins (haemoglobin and myoglobin) towards
extraction when the storage time is increased might have resulted
in their lower content in the meat (Chaijan et al., 2005). With the
increase of storage time, high degree of haem destruction might
have taken place, which could resulted in lower extraction of
haemoglobin and myoglobin from the camel meat. This could have
ultimately resulted in release of more iron from the prophyrin ring
of haemoglobin and myoglobin, thus acting as pro-oxidants in the
camel meat during the storage. Until now no study has reported
the haemoglobin content in the camel meat. Knowledge regarding
amount of haemoglobin present in the camel meat is important, as
it plays an important role as a pro-oxidant in the meat. After the
animal is being slaughtered, the iron atom in the haem ring of the
haemoglobin or myoglobin is primarily in the ferrous (+2) state.
Conversion of ferrous haemoglobin or myoglobin to met (+3)
haemoglobin or myoglobin is a process known as autoxidation.
Autoxidation appears to be a critical step to enhance lipid
oxidation since met haemoglobin or met myoglobin reacts with
peroxides to stimulate the formation of compounds capable of
initiating and propagating lipid oxidation (Maqsood and Benjakul,
2011). Therefore, the presence of myoglobin and haemoglobin in
the camel meat can be a decisive factor in making the lipids more
prone to lipid oxidation.
3.3. Characterisation and changes in protein fraction of camel meat
3.3.1. Changes in protein pattern by SDS PAGE
Changes in protein pattern of camel meat during 9 days of
refrigerated storage are presented in Fig. 2. Camel meat protein
contains myosin heavy chain (200 kilodaltons; kDa), C-protein

(140 kDa), Alpha actinin (110 kDa), tropomysin (70 kDa), and actin
(55 kDa). C-protein is a thick lament of a single polypeptide chain
having a molecular mass of 140 kDa. a-Actinin is located
exclusively in the Z disc and has a molecular mass of 130 kDa.
Tropomyosin is a protein with two-stranded coiled-coil of an ahelix having a molecular mass of 6570 kDa. Actin is a major
protein of the thin laments in the meat, which comprises 1530%
of myobrillar protein of muscle and had a molecular mass of 43
48 kDa (Abdelhadi et al., 2013). During the storage at refrigerated
temperature for 9 days, different proteins in the camel meat
underwent degradation to some extent as depicted in Fig. 2. MHC,
C-protein, alpha actinin as well as tropomyosin bands showed a
noticeable degradation on day 9 of storage. Proteolytic degradation
of myobrillar proteins, especially myosin, might result in the loss
of structural domains of the meat (Takahashi, 1996), which is
reected by the lower hardness values obtained in the camel meat
on day 9 of storage (Table 2). Ageing or storage of meat at
refrigerated temperature is the period during which an increase
in tenderness and specic degradation of structural proteins
occurs (Kadim et al., 2006). Degradation of different protein
bands in the camel meat during the refrigerated storage might
also be due to the oxidation of proteins as well as due to the
production of endoproteinases by microorganisms. Oxidation of
proteins is believed to cause fragmentation and degradation of
structural protein (Maqsood and Benjakul, 2010b). Proteolysis
by endogenous proteases in the meat during storage might be
associated with the pronounced microbial growth (Maqsood and
Benjakul, 2010b,c). It is well established that the proteolysis of
myobrillar proteins by endogenous proteases during postmortem ageing is primarily responsible for the tenderisation of
meat. The principal degradative change in proteins that occurred
over 9 days of storage, as detected by SDS-PAGE, was the
appearance of troponin T (30KDa) band. Loss of troponin T has
been related to protein degradation and could play a role in
tenderness (Gheisari et al., 2009). Therefore, the camel meat
proteins underwent degradation to some extent during the
refrigerated storage of 9 days.
3.3.2. Changes in protein extractability, protein solubility and TCAsoluble peptides
Extractability of camel meat protein during refrigerated storage
is shown in Fig. 3. Extraction of proteins was carried out in 5% NaCl
as an extraction solvent. Extraction of myobrillar proteins,
commonly called salt-soluble proteins, is crucial in manufacturing
of further processed meat products such as frankfurters and
bologna. Once extracted, these proteins serve as emulsifying
agents in meat batter and contribute to emulsion stability and play
an important role during processing of restructured meat products
(Hultin et al., 1995).

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S. Maqsood et al. / Journal of Food Composition and Analysis 41 (2015) 212220

Fig. 2. Proteolysis in the camel meat proteins as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).

Extractability of camel meat proteins did not changed

signicantly during the rst 6 day of storage (P > 0.05). Thereafter,
an increase in protein extractability was noticed up to day 9 of
storage (P < 0.05). During the early period of storage, myobrillar
protein could apparently form an insoluble fraction due to
denaturation that accounts for the lower protein solubility and
thus extractability (Leelapongwattana et al., 2005). Degradation of
myobrillar proteins, commonly called salt-soluble proteins,
during the extended storage period might have resulted in high
extraction of total protein. Extractability behaviour of proteins
from camel meat has not been reported before. The amount of
protein extracted will play an important role in the performance of
its functional properties.
Solubility of protein is one of the most important physicochemical property through which protein performs its different
functional properties like emulsifying, foaming, gelling (Kristinsson and Rasco, 2000). In the present study, solubility of camel meat
protein on day 0 was 9.4 mg/g of sample and it increased to
12.6 mg/g on 9 days of storage (P < 0.05) (Fig.3(a)). The increase in
protein solubility with increase in storage time might have
resulted in higher values for protein extractability. The protein
solubility changes were due to myobrillar protein degradation.
Protein solubility is used as an indicator of protein denaturation,
and low protein solubility indicated a high extent of protein
denaturation (Joo et al., 1999).
Changes in TCA-soluble peptides in camel meat sample during
9 days of refrigerated storage are shown in Fig. 3(b). TCA-soluble
peptides showed a sharp increase throughout 9 days of refrigerated storage (P < 0.05), suggesting the autolytic degradation of meat
protein resulting in the release of peptides. This indicates that
endogenous enzymes were active enough during the refrigerated
storage to cause the breakdown of proteins to peptides. The action
of proteolytic enzymes such as calpains and cathepsins on the
myobrillar protein fraction results in the production of protein
fragments like that of TCA-soluble peptides. TCA-soluble peptide

has been used as the index for the protein degradation of muscle
food (Benjakul et al., 1997).
3.4. Changes in quality parameters of camel meat during refrigerated
storage
3.4.1. Changes in pH
Changes in pH of fresh camel meat during 9 days of refrigerated
storage is shown in Fig. 4(a). Initial pH value of fresh camel meat
was 6.2. Soltanizadeh et al. (2008) also reported that the pH of
camel meat was 6.15 after 12 h post-mortem. The range of pH in
the camel meat during the refrigerated storage was from 6.2 to 5.4,
which were within the range for camel meat (6.165.83) reported
by Eskandari et al. (2013). There was an abrupt decrease in pH on
day 3 of storage (P < 0.05), after which the decrease was gradual
until the end of storage period (P > 0.05). This is usually due to the
fact that camels possess high gluconeogenesis capacity because of
the presence of camel hump, which cause rapid drop of pH
(Soltanizadeh et al., 2008). The decline of pH in meat depends on
the amount of glycogen in the muscle at the time of slaughter.
Lower glycogen contents result in decreased rates of anaerobic
glycolysis; therefore, a slower production of lactic acid and hence a
lower rate of post-mortem pH decline (Soltanizadeh et al., 2008).
Camel meat reached to an ultimate pH of 5.4 after 9 days of storage.
The range of the ultimate pH values of dromedary camel meat
ranged between 5.7 and 6.0 (Kadim et al., 2006). The rate and
extent of post-mortem pH decline may induce protein denaturation, affecting tenderness, WHC, juiciness and colour, thus plays
an important role in quality of camel meat.
3.4.2. Changes in textural properties of camel meat
Texture prole analysis of the camel meat at day 0 and 9 of
refrigerated storage is shown in Table 2. Hardness, springiness,
gumminess and chewiness values of camel meat samples sharply
decreased from day 0 to 9 of refrigerated storage, while there was

S. Maqsood et al. / Journal of Food Composition and Analysis 41 (2015) 212220

a)

219

a)
6.5

6.25

pH

b
c

bc

5.75
5.5
5.25
5

b)

3
6
Storage me (Days)

16

14

b)

Drip loss (%)

12
10

8
c
6

4
2
0
0

Storage me (days)

Fig. 3. Protein solubility (a) and protein extractability and TCA-soluble peptides (b)
in camel meat proteins as affected by refrigerated storage. Values are mean  SD
from 18 determinations. Different letter at different storage time indicates the
signicant difference (P < 0.05).

no signicant change in cohesiveness. There was an increase in

cohesiveness of camel when stored for 9 days under refrigeration
(P < 0.05). The major eating qualities of meat are developed during
muscle ageing, and it is well established that ageing or storage
improves meat tenderness and thus the eating quality. Normally,
increasing the ageing time will also increase tenderness, and
water-holding capacity is closely related to meat tenderness
during ageing. In this study, decrease in hardness, gumminess,
chewiness, and springiness in the camel meat during the storage
was supported by the increased drip loss and decreased waterholding capacity. Softening of camel meat occurred after storage of
9 days, which could probably be due to the proteolytic action
promoted by muscle endopeptidases (calpain I and II and cathepsin
B, D, H and L).
3.4.3. Changes in colour parameters
Changes in L* (lightness), a* (redness) and b* (yellowness) of
camel meat kept under refrigerated storage for 9 days are
presented in Table 2. Results showed that L* value increased as
storage time increased, while a* and b* values showed a gradual
decrease throughout 9 days of storage (P < 00.5). Redness (a*)
value of camel meat decreased drastically during rst 6 days of
storage from an initial value of 19.9811.58 (P < 0.05). Red colour
of the meat is due to the presence of myoglobin pigment. Decrease
in redness (a*) values in the camel meat with an increase in storage
period was in agreement with decrease in total haem pigment and
myoglobin content during storage (Fig.2). Decrease in redness
occurs in all types of meat, which is mainly due to oxidation of oxymyoglobin to metmyoglobin (Maqsood and Benjakul, 2010b).

Fig. 4. Changes in pH (a) and drip loss (b) in the camel meat during refrigerated
storage. Values are mean  SD from 18 determinations. Different letter at different
storage time indicates the signicant difference (P < 0.05).

During the post-mortem storage of meat, myoglobin in the ferrous

state is oxidised to ferric metmyoglobin, resulting in a brownishred meat (Maqsood and Benjakul, 2010b). Guidera et al. (1997)
reported that redness (a*) values in lamb meat tended to decrease
during chilled storage. High oxygen packing with added natural
antioxidants can be used as a strategy to retain the redness of
camel meat during storage.
3.4.4. Drip loss
Drip loss of camel meat kept under refrigerated storage for
9 days is shown in Fig. 4(b). The ability of meat to retain inherent
water, dened as water-holding capacity (WHC), is an essential
quality parameter for both the industry and the consumer. Drip
loss is considered to be inversely proportional to WHC. For the
meat processing, the WHC of fresh meat is known to inuence its
technological quality, i.e. processing yield. In the present study, a
continuous increase in drip loss was observed in the camel meat
when the storage time increased (P < 0.05). This might be due to a
greater loss of water holding property of the muscle protein. The
increase in drip loss with storage time is explained by water loss
from the muscle due to degradation of muscle proteins caused by
the spoilage mechanisms. WHC or drip loss is affected by
degradation of myobrillar proteins (Traore et al., 2012).
Abdelhadi et al. (2013) also reported that the drip loss in the
camel meat continuously increased during refrigerated storage for
7 days. As the camel meat aged, protein might have undergone
denaturation, which might have resulted in its loss of water
holding capacity. Severe denaturation affects the proteins ability
to bind water and thus results in high drip loss (Traore et al., 2012).
The high drip loss is considered to be a serious quality problem
because it contributes to the lower acceptability due to the fewer
taste constituents remained as well as the shrinkage of the meat.

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S. Maqsood et al. / Journal of Food Composition and Analysis 41 (2015) 212220

4. Conclusions
The present study showed that the camel meat contains high
quantities of unsaturated fatty acid with signicant amount of
health-promoting PUFA. However, the presence of PUFA along
with high haem proteins (Hb and Mb) could make camel meat
more prone to lipid oxidation as reected by high PV and TBARS
formation. There was a considerable change in the protein fraction
of camel meat during storage. Degradation of protein bands with
concomitant increase in TCA-soluble peptides and protein
extractability and solubility was evident after 9 days of storage.
Camel meat showed a gradual deterioration of composition quality
attributes, which includes a continuous drip loss and drastic
changes in texture prole and colour. Nevertheless, developing
diverse products from camel meat through optimum processing,
proper preservation and consumer acceptance can be a future
research focus in order to popularise camel meat among the
consumers.
Acknowledgement
Authors are thankful to United Arab Emirates University for the
funding this research through a research grant (No. 31F024).
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