Food Chemistry 268 (2018) 257–263

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Food Chemistry
journal homepage: www.elsevier.com/locate/foodchem

Characteristics and properties of goat meat gels as affected by setting T

temperatures
⁎
Sulaiman Mad-Alia, Payap Masniyoma, Soottawat Benjakulb,
a
Halal Institute, Prince of Songkla University, Hat Yai, Songkhla 90112, Thailand
b
Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla 90112, Thailand

A R T I C LE I N FO A B S T R A C T

Keywords: Effects of different setting temperatures (40–70 °C) on properties of goat meat gels after heating at 90 °C were
Characteristic investigated. Setting at 60 °C with subsequent heating at 90 °C yielded the gel with the highest breaking force
Gel along with coincidentally lowest expressible moisture content (p < 0.05). The highest TCA-soluble peptide
Goat meat content was found in gel set at 70 °C (p < 0.05). Slight decrease in myosin heavy chain band intensity was
Setting
noticeable when setting temperature increased. As setting temperatures increased, a∗ and b∗-values of gels
Temperature
generally increased, while L∗-values decreased (p < 0.05). Gel set at 60 °C had highest hardness, gumminess
and chewiness (p < 0.05). Gel set at 60 °C had the most compact network with immense connectivity of protein
strands. Gels set at 40–60 °C had higher texture and overall likeness scores, compared to the control (p < 0.05).
Prior setting at 60 °C was recommended for making the good quality goat meat gel.

1. Introduction cross-linking of myosin is mediated by endogenous transglutaminase

Goat meat has been widely consumed in Asia and Africa (Arain
et al., 2010). Goat meat is also a crucial food, which is one of the main
products of different traditional dishes in Mediterranean (Teixeira,
Pereira, & Rodrigues, 2011). Goat meat has gained interesting attention
by the ethnic consumers. Popularity and use of goat meat vary with
communities (Wattanachant, Sornprasitt, & Polpara, 2008). Ad-
ditionally, culture, social and economic conditions determine the pre-
ference of consumer for goat meat. In Thailand, the production of goat
meat has gradually increased in recent years (Wasiksiri, Pongprayoon,
Srimai, & Nasae, 2010), due to an increasing consumer’s demand. Ad-
ditionally, goat meat can be extended to the Middle East and niche
markets in Asia. Western countries with ethnic communities that tra-
ditionally consume goat meat are another market, where there are in-
adequate supplies of goat meat or products (Wattanachant et al., 2008).
To widen the consumption of goat meat, value-added products
should be manufactured to meet the consumer’s requirement. Goat
meat can be used for production of gel-type products. Gel-forming
ability and viscoelastic property are integral for meat products. These
properties are governed by bonds stabilizing the gel network
(Tammatinna, Benjakul, Visessanguan, & Tanaka, 2007). Several ap-
proaches have been used to enhance gelling property of mince or wa-
shed mince of fish meat known as ‘surimi’. “Setting” is generally im-
plemented in surimi paste at temperature range of 25–40 °C, in which
(TGase). This contributes to the enhanced gel strength (Tammatinna
et al., 2007). For direct cooking (without prior setting), TGase has a
limited activity due to its thermal inactivation at high temperature.
TGase (EC 2.3.2.13) is able to catalyze the acyl transfer from γ-carboxyl
amide groups of glutamine to ε-amino groups of lysine, resulting in the
formation of ε-(γ-glutamyl) lysine isopeptide (Dondero, Figueroa,
Morales, & Curotto, 2006). To produce gel with good quality from the
meat of land animals including beef and pork (Dondero et al., 2006;
Kim, Carpenter, Lanier, & Wicker, 1993; Park, Brewer, McKeith,
Bechtel, and Novakofski, 1996a, 1996b; Torley & Lanier, 1991), rabbit
(Ishioroshi, Samejima, & Yasui, 1982; Samejima, Ishioroshi, & Yasui,
1981), chicken (Smyth and O'neill, 1997) and quail (Ikhlas, Huda, &
Noryati, 2011), setting is employed before heating or cooking. Never-
theless, Niwa, Suzumura, Nowsad, and Katoh (1993) classified some
mammalian vertebrates such as bovine, pig and whale as non-setting
species. Low setting in those meat species might be owing to low level
of cross-linking enzyme. Moreover, substrate available for enzyme ac-
tivity is restricted. Nevertheless, Dondero, Figueroa, Morales, and
Curotto (2006) stated that endogenous TGase was found in beef. Torley
and Lanier (1991) reported that some beef appeared to have setting
phenomenon at 25 °C. Additionally, Akamittath, Ball, and Hershell
(1992) found that setting occurred in actomyosin from turkey at 4 and
37 °C with the aid of guinea pig liver transglutaminase. TGase or Factor
XIII from crude pig plasma induced the formation of isopeptides in

⁎
Corresponding author.
E-mail address: soottawat.b@psu.ac.th (S. Benjakul).

https://doi.org/10.1016/j.foodchem.2018.06.084
Received 9 February 2018; Received in revised form 11 June 2018; Accepted 18 June 2018
Available online 19 June 2018
0308-8146/ © 2018 Elsevier Ltd. All rights reserved.
S. Mad-Ali et al.
chicken meat ball heated at internal temperature of 71 °C (Tseng, Liu, &
Chen, 2000). For fish mince or surimi, optimum setting temperature
was governed by heat stability of myosin and varied with species
(Benjakul, Chantarasuwan, & Visessanguan, 2003). The optimal setting
temperature generally relates to the habitat and body temperatures of
animal (Benjakul et al., 2003; Kim et al., 1993).
To our knowledge, no information regarding setting and gel for-
mation of goat meat exists. Based on our preliminary study, goat meat
had poor gel-forming ability, compared to fish meat. This may be as-
sociated with low setting phenomenon mediated by endogenous TGase
or poor aggregation or alignment of muscle proteins. The objective of
this investigation was to study the effect of setting temperatures on
properties of heat induced gel from goat meat.
2. Materials and methods
2.1. Chemicals
Sodium dodecyl sulfate (SDS) and β-mercaptoethanol (βME) were
purchased from Sigma (St. Louis, MO, USA). Trichloroacetic acid and
Foline-Ciocalteu's phenol reagent were obtained from Merck
(Darmstadt, Germany). Bis-acrylamide, acrylamide and N,N,N′,N′-tet-
ramethylethylenediamine (TEMED) were procured from Fluka (Buchs,
Switzerland). All chemicals used were of analytical grade.
2.2. Collection and preparation of goat meat
Meat from the Boer goat with the age of approximately 1.5 year was
obtained from a local slaughter house in Hat Yai district, Songkhla
province, Thailand. Goats were slaughtered, following the Muslim
practice (Halal means) by cutting the throat and major blood vessels in
the neck. Goat meat was dissected, pooled and used as the composite
samples. It was placed in polyethylene bag. Then it was transported in
an insulated box containing ice (meat/ice ratio of 1:10, w/w) to the
laboratory of halal research institute, Prince of Songkla University,
within 30 min. Upon arrival, meat was immediately washed with cool
water (5 °C). The external fat and connective tissue were removed
manually. The meat was then postmortem-aged at 4–5 °C for 24 h. After
aging, it was placed in polyethylene bag, heat-sealed and stored at
-20 °C until use. The storage time was not longer than 1 month.
2.3. Effect of setting temperatures on property of goat meat gels
Frozen goat meat was thawed at 4 °C for 4–5 h until the core tem-
perature of 0–2 °C was obtained. Meat samples were washed thoroughly
with running water (4 °C). Sample was minced to uniformity using a
mincer (National Model MK-5080 M, Selangor, Malaysia) for 3 min.
Subsequently, 2.8% NaCl, 0.3% mixed phosphate (sodium tripolypho-
sphate/potassium polyphosphate at a ratio of 7:3), 2.5% sugar, 3%
modified tapioca starch (distarch phosphate) and 0.3% ground black
pepper were added. The mixture was mixed well for 2 min. The tem-
perature was maintained below 10 °C during chopping. Meat paste was
added with distilled water, in which the final moisture content of 80%
was gained. Thereafter, the mixture was chopped for 3 min. Resulting
paste (200 g) was stuffed into a polyvinylidene chloride casing (a dia-
meter: 2.5 cm, total length: 30 cm). Both ends were sealed and sub-
jected to setting at different temperatures (40, 50, 60 or 70 °C) for
30 min in a temperature control water bath (W350, Memmert,
Schwabach, Germany). Set samples were heated at 90 °C for 20 min and
subsequently cooled in iced water for 30 min. The gel samples were
kept at 4 °C for 24 h before analyses.
2.3.1. Breaking force and deformation
Breaking force (gel strength) and deformation (deformability) of
goat meat gels were measured by a texture analyzer (Model TAXT2,
Stable MicroSystems, Surrey, UK) as described by Buamard and
258
Food Chemistry 268 (2018) 257–263
Benjakul (2015). Cylindrical gel samples (2.5 cm in height) were
equilibrated at room temperature (28–30 °C) for 1 h. A spherical
plunger having a diameter of 5 mm and a constant depression speed of
60 mm/min were used for testing. Breaking force and deformation were
recorded.
2.3.2. Texture profile analysis
Texture profile analysis (TPA) of gel samples was conducted fol-
lowing the method of Buamard and Benjakul (2015). A texture analyzer
(Model TA-XT2, Stable Micro- Systems, Surrey, UK) with a cylinder
probe (diameter 35 mm) was used. Hardness, springiness, cohesiveness,
gumminess and chewiness were determined.
2.3.3. Expressible moisture content
Expressible moisture content was determined as per the method of
Buamard and Benjakul (2015). Cylindrical gel sample with 5 mm in
thickness was weighed accurately (X). It was sandwiched between three
pieces of filter paper No.1 (Whatman International Ltd., Maidstone, UK)
at the bottom and two pieces on the top. Subsequently, the samples
were pressed by a standard weight (5 kg) for 2 min. After removal from
the papers, the samples were weighed again (Y). Expressible moisture
content was calculated with the following equation and expressed as
percentage of sample weight:
Expressible moisture content = [(X−Y)/X] × 100
2.3.4. Color of gel
Color of gels was measured by a Hunter lab colorimeter (Color Flex,
Hunter Lab Inc., Reston, VA, USA). L*, a* and b* values were measured.
The colorimeter was warmed up for approximately 10 min. A white
standard was used for calibration. Total difference in color (ΔE*) was
calculated as guided by Mad-Ali, Benjakul, Prodpran, and Maqsood
(2017).
2.3.5. TCA-soluble peptide content
TCA-soluble peptide content as an indicator for protein degradation
was measured following the method of Buamard and Benjakul (2015).
Chopped sample (3 g) was added with cold 5% TCA (27 mL). Homo-
genization was implemented at 11,000 rpm for 2 min using a homo-
genizer (IKA Labortechnik, Selangor, Malaysia). After being stored in
ice for 1 h, homogenate was centrifuged at 8000g for 10 min. Super-
natant was collected and determined for TCA-soluble peptide as per the
method of Lowry, Rosebrough, Farr, and Randall (1951).
2.3.6. SDS-polyacrylamide gel electrophoresis
Protein patterns of goat meat gels were analyzed by SDS-PAGE
under the reducing condition following the method of Laemmli (1970).
Firstly gel samples were finely chopped. Twenty-seven mL of heated
SDS solution (85 °C) were mixed with prepared sample and homo-
genized at 11,000 rpm for 2 min. After incubation at 85 °C for 1 h, the
mixtures were centrifuged at 3500g for 20 min to remove the debris.
Protein concentration of the supernatant was measured by the Biuret
method (Robinson & Hogden, 1940), where bovine serum albumin was
used as standard. Prepared samples were mixed with sample buffer and
the mixture (protein of 15 µg) was loaded onto the gel. SDS-PAGE gel
comprising 10% running gel and 4% stacking gel was used. After se-
paration, the proteins were subjected to staining and destaining as
guided by Buamard and Benjakul (2015).
2.3.7. Microstructures
Microstructure of gel samples was examined using a scanning
electron microscope (SEM). The samples (2–3 mm in thickness) were
fixed with 0.2 M phosphate buffer (pH 7.2) containing 2.5% (v/v)
glutaraldehyde for 3 h at room temperature. After rinsing with distilled
water, the dehydration of specimens was conducted in ethanol with
serial concentrations (25–100%). Samples were subjected to critical
S. Mad-Ali et al.
point drying using CO2 as transition fluid. Dried samples were mounted
on a bronze stub and sputter-coated with gold (Sputter coater SPI-
Module, West Chester, PA, USA). Visualization of specimens were made
using SEM (Quanta 400, FEI, Eindhoven, the Netherlands).
2.4. Sensory property of goat meat ball with different setting temperatures
Goat meat paste was firstly prepared as described previously. Meat
balls (approximately 2.5 cm in diameter) were formed manually and set
at various temperatures before heating at 90 °C for 20 min. Meat balls
were cooled in ice water for 30 min and stored at 4 °C for 24 h before
sensory evaluation. Meat balls were then allowed to stand at room
temperature for 30 min and coded with 3-digit random numbers.
Samples were displayed on the white paper dishes. Thirty non-trained
panelists (aged between 20 and 45) were the staffs and students at the
Department of Food Technology, who were familiar with meat ball. The
9-point hedonic scale was used for assessment of samples according to
the method of Meilgaard, Carr, and Civille (2006).
2.5. Statistical analysis
The experiments were carried out in triplicate. Data were subjected
to analysis of variance (ANOVA). Means was compared by the Duncan's
multiple range test (Steel, Torrie, & Dickey, 1980). Statistical analysis
was run using SPSS for Windows (SPSS Inc., Chicago, IL, USA).
3. Results and discussion
3.1. Effect of different setting temperatures on properties and characteristics
of goat meat gels
3.1.1. Breaking force and deformation
Breaking force and deformation of goat meat gel set at different
temperatures are illustrated in Fig. 1. In general, gels with setting be-
fore heating at 90 °C showed the higher breaking force than the control
gel (without setting) (p < 0.05). Among all samples with prior setting,
lower breaking force was found in gels set at 40 and 50 °C, compared to
Fig. 1. Breaking force and deformation of gels from goat meat with different
setting temperatures. Con: Directly heated gel (without prior setting). Bars re-
present the standard deviation (n = 3). Different lowercase letters on the bars
indicates the significant differences (p < 0.05).
259
Food Chemistry 268 (2018) 257–263
60 °C (p < 0.05). However, setting at 70 °C yielded the gel with lower
breaking force than that set at 60 °C (p < 0.05). During setting, some
proteins underwent denaturation or unfolding. Subsequently, those
unfolded proteins with the extended chains could align themselves and
interact intermolecularly during setting. A stronger gel was obtained in
gel set at 60 °C, which was able to strengthen the gel network as in-
dicated by the highest breaking force (p < 0.05). Apparently, this
setting temperature (60 °C) might be associated with the appropriate
unfolding and aggregation of myosin heavy chains. Castro-Briones et al.
(2009) stated that denaturation of poultry and beef myosin occurred at
55 °C, while fish myosin denatured at 40 °C. At temperature higher than
denaturation temperature, the embedded hydrophobic residues or re-
active sulfhydryl groups might be more exposed and interacted via
hydrophobic-hydrophobic interaction or disulfide bonding, thus fa-
voring the formation of stronger gel. Hydrophobic interactions between
proteins in gels are enhanced by the elevating temperature at least near
to 60 °C (Lanier, Carvajal, & Yongsawatdigul, 2014). Beef myofibrillar
proteins were also found to involve in gel forming at 43–56 °C
(Samejima, Egelandsdal, & Fretheim, 1985). Nevertheless, the setting
time longer than 30 min had no impact on breaking force of resulting
gels (data not shown). It was postulated that protein-crossing mediated
by endogenous TGase or other bondings such as hydrophobic-hydro-
phobic interaction, etc. occurred mainly within the first 30 min. Com-
pared to commercial fish surimi, surimi-like material made from beef
and pork had harder gels when heated above 55 °C (Park et al., 1996a,
1996b). Park et al. (1996a, 1996b) also reported that the hardness of
gel from water-washed pork increased almost linearly with increasing
preheating temperature from 30 to 60 °C. Myosin of rabbit muscle de-
velops a fairly firm gel above 50 °C. This was caused by thermal un-
folding of helical tail portion of myosin heavy chain (Ishioroshi et al.,
1982; Samejima et al., 1981). Transition temperatures of chicken surimi
between 50 and 60 °C were the most vital in gel formation (Smyth and
O'neill, 1997). In addition, setting at 60 °C might be the optimum
temperature for endogenous TGase from goat meat, in which cross-
linking of myosin mediated by TGase might take place to some degree.
TGase from goat meat showed the optimal temperature at 60 °C using
CBZ-Glutaminylglycine (CBZ-Gln-Gly) as a substrate (data not shown).
This plausibly resulted in a firmer gel when set at 60 °C. When higher
setting temperature (70 °C) was used, the slight decrease in breaking
force was found (p < 0.05). At high temperature, aggregation of pro-
teins occurred at a faster rate. This might lead to the induced coagu-
lation with randomly organized network. This phenomenon could
contribute to the lower breaking force of gel set at 70 °C. Control gel or
directly heated gel (non-setting) showed the lowest breaking force
(p < 0.05). Without setting, hydrophobic domains or reactive sulfhy-
dryl groups were involved in the alignment or aggregation of proteins
to a lower extent. Additionally, available substrate residues for TGase
might be limited or buried inside molecules at low temperature. After
setting, set samples were further heated. The heat induced gelation of
myofibrillar proteins was regarded as very crucial process in the sta-
bility and textural aspects of comminuted and reformed meat products
(Antonomanolaki, Vareltzis, Georgakis, & Kaldrymidou, 1999). For the
deformation of goat meat gel, setting could increase deformation of all
gels with prior setting. The control gel showed the lowest deformation
(p < 0.05). It was noted that gels with setting temperatures of
50–70 °C had the similar deformation but possessed higher deformation
than the control (p < 0.05). Thus, setting temperature was an im-
portant factor affecting deformation of goat meat gels.
3.1.2. Textural properties
Textural properties of gel from goat meat with different setting
temperatures are shown in Table 1. Compared to the control gel (non-
setting), those with setting temperature had the higher hardness
(p < 0.05). When setting temperature increased up to 60 °C, gel had
the increased hardness (p < 0.05). Hardness represents the force re-
quired to compress sample to reach a given deformation (Buamard &
S. Mad-Ali et al. Food Chemistry 268 (2018) 257–263

Table 1
Textural properties of gels from goat meat with different setting temperatures.
Setting temperature (°C) Hardness (N) Springiness (cm) Cohesiveness Gumminess (N) Chewiness (N × cm)

a a a a
Con 67.89 ± 2.14 0.95 ± 0.02 0.85 ± 0.01 57.59 ± 1.71 54.87 ± 2.05a
40 86.51 ± 2.15b 0.90 ± 0.01a 0.80 ± 0.01a 69.48 ± 1.30b 62.74 ± 1.12b
50 92.00 ± 1.10c 0.92 ± 0.03a 0.81 ± 0.01a 74.92 ± 0.93c 68.99 ± 1.60c
60 112.91 ± 2.81d 0.92 ± 0.02a 0.82 ± 0.01a 92.47 ± 2.28d 85.37 ± 2.34d
70 88.67 ± 1.50b 0.91 ± 0.02a 0.80 ± 0.01a 71.33 ± 1.77b 65.16 ± 2.33b

Values are presented as mean ± SD (n = 3).

Different lowercase superscripts in the same column indicate significant difference (p < 0.05).
Con: Directly heated gel (without prior setting)
Meat paste was subjected to setting at various temperatures for 30 min, followed by heating at 90 °C for 20 min.

Benjakul, 2015). Nevertheless, the gel set at 70 °C had the lowered
hardness and had similar hardness to that set at 40 °C (p > 0.05). The
result of hardness was in accordance with that of breaking force.
Overall, high setting temperature (70 °C) showed negative effect on gel
strength. The highest hardness in gel set at 60 °C was related with the
highest breaking force (Fig. 1). In general, similar results were found for
gumminess, the necessary energy to break down a semi-solid food be-
fore swallowing (Larzul, Imbert, Bernadet, Guy, & Rémignon, 2006)
and chewiness, the energy required to masticate sample for swallowing
(Chang, Xu, Zhou, Li, & Huang, 2012). Nonetheless, no differences in
springiness, which is defined as elastic recovery that takes place when
the compressive force is removed, and cohesiveness, the ability for
breaking down the internal structure (de Huidobro, Miguel, Blázquez, &
Onega, 2005), were observed among all samples (p < 0.05). For
comminuted meat product texture, cohesiveness is an integral para-
meter, while the secondary parameters included fracturability, gum-
miness and chewiness (Giese, 1995). Park et al. (1996a, 1996b) also
reported that cohesiveness of gels from washed-water pork was un-
changed when preheating from 30 to 60 °C was conducted. Thus, set-
ting temperature was shown to affect gel formation, determining TPA
characteristics of resulting gels.
3.1.3. Expressible moisture content
Expressible moisture content of gels from goat meat with different
setting temperatures is given in Table 2. In general, gels with different
setting temperatures showed no differences in expressible moisture
content (p > 0.05), except gel set at 60 °C, which had the lowest ex-
pressible moisture content (p < 0.05). The higher expressible moisture
content was found in the control gel (p < 0.05), suggesting the poor
ability in water entrapment in gel network. This coincided with the
lowest breaking force of control gel (Fig. 1). The rapidly unfolded
protein contributes to more intense coagulation during direct heating.
More water is liberated from the gel network with uneven protein
dispersion (Chaijan, Panpipat, & Benjakul, 2010). In the present study,
no drip or exudate was found in all the gel samples. This indicated that
all water was imbibed in the gels, but the water holding capacity of gels
varied with the setting temperatures. Therefore, setting/heating con-
dition could be optimized to improve gel-forming ability of goat meat,
in which the stronger gel with high water holding capacity was ob-
tained. The result suggested that setting at 60 °C rendered the goat meat
gel with the highest water holding capacity.
3.1.4. Color
Color of gels from goat meat with different setting temperatures and
the control gel is shown in Table 2. The control gel had the highest L*-
values (lightness) (p < 0.05), while possessed the lowest a* (redness)
and b* (yellowness)-values (p < 0.05), compared to the other samples
(p < 0.05). At highest setting temperature (70 °C), L*-value of gel was
decreased (p < 0.05), whereas a* and b*-values were increased
(p < 0.05). During heat treatment, myoglobin might undergo oxida-
tion and was converted to metmyoglobin, thereby developing brown
color. Denatured haem proteins formed during heating resulted in their
binding to myofibrillar proteins and also cause the discoloration of gel
(Lanier et al., 2014). Furthermore, non-enzymatic browning reaction
might take place and affected the color of gels during heating, espe-
cially at high setting temperature. This was also affirmed by the in-
creases in redness and yellowness. However, there were no differences
in L*, a* and b*-values between gels set at temperatures ranging from
40 to 60 °C (p > 0.05). Among all gel samples, that set at 70 °C had the
highest total difference in color value (ΔE*) (36.93). These results
showed that the setting temperature had the influence on the color of
goat meat gel, apart from gel texture.
3.1.5. TCA-soluble peptide content
TCA-soluble peptide content of goat meat gels set at various tem-
peratures prior to heating at 90 °C is presented in Table 2. Goat meat
paste had TCA-soluble peptide content of 0.40 µmol tyrosine equiva-
lent/g sample. TCA-soluble peptide content is generally used as an in-
dicator of autolytic degradation of muscle protein (Tammatinna et al.,
2007). For all gels tested, no differences in TCA-soluble peptide content
were observed (p > 0.05), except gel set at 70 °C, which had the
highest TCA-soluble peptide content (p < 0.05). The result suggested

Table 2
Expressible moisture content, color and TCA-soluble peptide content of gels from goat meat with different setting temperatures.
Setting Temperatures (°C) Expressible moisture content (%) Color value TCA-soluble peptide content
(µmol tyrosine equivalent/g sample)
L* a* b* ΔE*

Paste – – – – – 0.40 ± 0.03a

Con 12.61 ± 0.05c 64.21 ± 0.54c 0.41 ± 0.28a 9.94 ± 0.87a 30.92 ± 1.26a 0.44 ± 0.02a
40 8.44 ± 0.06b 63.13 ± 1.51b 0.50 ± 0.25a 11.00 ± 0.70a 31.46 ± 1.55a 0.41 ± 0.05a
50 8.23 ± 0.07b 62.98 ± 0.96b 1.04 ± 0.20b 11.16 ± 0.17a 31.77 ± 0.88a 0.46 ± 0.05a
60 6.96 ± 0.08a 61.27 ± 1.85b 1.07 ± 0.44b 11.22 ± 0.96a 33.44 ± 0.53a 0.50 ± 0.07a
70 8.40 ± 0.07b 58.41 ± 0.64a 1.65 ± 0.18c 13.54 ± 0.88b 36.93 ± 0.38b 0.65 ± 0.05b

Values are presented as mean ± SD (n = 3).

Different lowercase superscripts in the same column indicate significant difference (p < 0.05).
Con: Directly heated gel (without prior setting).
* Meat paste was subjected to setting at various temperatures for 30 min, followed by heating at 90 °C for 20 min.

260
S. Mad-Ali et al. Food Chemistry 268 (2018) 257–263

Actin was also found as the second prevalent protein. The MWs of MHC
kDa and actin were estimated to be 210 and 49 kDa, respectively. After
gelation, the decreases in MHC band were found in all gels. The control
250
MHC gel (heated at 90 °C without prior setting) showed higher MHC band
145
intensity than those with prior setting at various temperatures. Setting
before heating at 90 °C could strengthen the gels from goat meat
65 (Fig. 1). Disappearance of MHC bands was likely due to the poly-
Actin merization of MHC. Endogenous TGase plausibly existed in goat meat
45
and might polymerize MHC via non-disulfide covalent bonds. MHC
36
band intensity in gel set at 60 and 70 °C was slightly lower than those
29
set at 40 and 50 °C. Factor XIII, TGase, in crude pig plasma played a role
24 in the formation of ε-(γ-glutamyl) lysine bonds in chicken meat ball
20 when added into the paste and subsequently heated at 85 °C to obtain
17 the internal temperature of 71 °C (Tseng et al., 2000). Setting at 60 °C
might be the optimum temperature of TGase to induce polymerization.
This contributed to a firmer gel as indicated by the highest breaking
M Paste Con 40 50 60 70 force (Fig. 1) and hardness (Table 1). Conversely, decrease in MHC
band intensity in gel set at 70 °C was more likely related to the poly-
Fig. 2. SDS-PAGE patterns of protein in gel from goat meat with different set- merization in conjunction with the slight degradation of MHC taken
ting temperatures. MHC: Myosin heavy chain, M: Marker, Con: Directly heated place simultaneously. This was shown by the occurrence of a new small
gel (without prior setting).
MW lower than 17 kDa in gel set at 70 °C. This result was coincidental
with lower breaking force in gel set at 70 °C, compared to that set at
that protein degradation in goat meat gel took place to some degree 60 °C (Fig. 1). This was also affirmed by the highest TCA-soluble pep-
during setting at 70 °C. Some endogenous proteinases, e.g. cathepsin, tide content in gel set at 70 °C (Table 2). When considering actin band
which are active at high temperature (Tammatinna et al., 2007), might for all gel samples, no differences in band intensity were found, re-
hydrolyze muscle protein in goat meat. Additionally, carboxyl proteases gardless of setting temperatures. It was suggested that actin was not
are generally actively involved in proteolytic breakdown of connectin involved in the gel-formation of goat meat. The result was in ac-
in muscles of land animal during heating at the temperature ranging cordance with Dondero et al. (2006) who reported that MHC bands of
from 60 to 80 °C (Lawrie & Ledward, 2006). Thus, setting temperature beef gels decreased with no obvious change in actin band during in-
was shown to affect the degradation of protein as well as gelation in cubation at 60 °C. The same phenomenon was also found in water-
goat meat. At 70 °C, protein could be hydrolyzed and the short chain washed pork gel with different preheating temperatures (Park et al.,
peptides could not form the strong gel as evidenced by the decreased 1996a, 1996b). Actin was not changed in band intensity for surimi gels
breaking force (Fig. 1) or hardness (Table 1) of gel set at 70 °C. from different species, e.g. bigeye snapper surimi (Benjakul &
Visessanguan, 2003), and walleye pollack surimi (Hossain, Morioka,
3.1.6. Protein patterns of goat meat gels Shikha, & Itoh, 2011). It was suggested that endogenous TGase from
SDS-PAGE protein patterns of goat meat gel prepared at different goat meat might preferentially polymerize MHC rather than other
setting temperatures under reducing condition are shown in Fig. 2. myofibrillar proteins. Thus, setting temperature more likely had impact
Meat paste contained myosin heavy chain (MHC) as the major protein. on protein pattern of gel from goat meat, particularly MHC.

Con 40

50 60 70

Fig. 3. Electron microscopic images of gel from goat meat with different setting temperatures. Con: Directly heated gel (without prior setting). Number denote setting
temperature (°C). Magnification: 10,000×.

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S. Mad-Ali et al. Food Chemistry 268 (2018) 257–263

Table 3
Likeness score of goat meat balls with different setting temperatures.
Setting temperatures (°C) Attributes

Appearance Color Odor Flavor Taste Texture Overall

b b a b a a
Con 7.33 ± 1.27 7.12 ± 1.41 6.97 ± 1.03 7.17 ± 0.91 7.30 ± 1.02 7.03 ± 1.22 7.11 ± 0.80a
40 7.40 ± 0.89b 7.3 ± 0.95b 6.93 ± 1.05a 7.03 ± 1.07b 7.23 ± 0.94a 7.13 ± 1.25ab 7.20 ± 1.03ab
50 7.50 ± 1.14b 7.4 ± 1.07b 7.03 ± 1.27a 7.07 ± 0.94b 7.37 ± 0.85a 7.50 ± 0.73b 7.47 ± 0.82ab
60 7.33 ± 1.09b 7.13 ± 1.11b 6.93 ± 1.31a 7.27 ± 1.01c 7.40 ± 1.04a 7.57 ± 0.97b 7.57 ± 0.90b
70 6.93 ± 0.74a 6.73 ± 0.91a 6.87 ± 1.01a 6.83 ± 1.09a 7.13 ± 1.04a 7.13 ± 1.25a 7.10 ± 0.92a

Values are presented as mean ± SD (n = 3).

Different lowercase superscripts in the same column indicate significant difference (p < 0.05).
Con: Directly heated gel (without prior setting).
Meat paste was subjected to setting at various temperatures for 30 min, followed by heating at 90 °C for 20 min.

3.1.7. Microstructures
Microstructures of gel from goat meat without and with different
setting temperatures are illustrated in Fig. 3. The control gel displayed a
coarser and looser network with larger cavities or voids. Network of
goat meat gel with prior setting, followed by heating had more com-
pactness and higher density than that observed in the control gel. The
result suggested that setting might effectively enhance the connectivity
of protein strands in gel network, in which the alignment or aggregation
of proteins was augmented. Higher interconnectivity and density of
protein strands were associated with increased breaking force of goat
meat gel with the appropriate setting temperature (Fig. 1). More rigid
gel was related to denser network (Buamard & Benjakul, 2015). Setting
at 60 °C rendered gel with the highest connectivity, and more likely
enhanced cross-linking of proteins. The finer network with higher
protein cross-linking was related with increased water holding capacity
as indicated by the lower expressible moisture content (Table 2).
Chantrapornchai and McClements (2002) documented that fine-
stranded networks with relatively small pores showed high water
holding capacity, whereas particulate networks containing relatively
large pores had low water holding capacity. Therefore, setting tem-
perature had the marked impact on connectivity, density and rigidity of
gel network of goat meat.
3.2. Impact of different setting temperatures on sensory property of goat
meat balls
formed to some degree and accumulated in meat balls. This might lower
the likeness score of flavor. Generally, gel set at 60 °C possessed the
higher textural and overall likeness score, compared to the control gel
(p < 0.05). This coincided with the highest hardness, gumminess and
chewiness of gel set at 60 °C (Table 2). However, there were no dif-
ferences in aforementioned attributes between meat balls with setting
temperatures of 40–60 °C. Therefore, setting temperature had the im-
pact on sensory property of goat meat balls.
4. Conclusion
Characteristic and gel-forming ability of goat meat were governed
by setting temperature. Prime quality gel with improved breaking force,
textural and sensory characteristics was obtained when setting at 60 °C
prior to heating at 90 °C was conducted. Setting at temperature higher
than 70 °C induced protein degradation and lowered the lightness of
gel. Setting at 60 °C prior to heating at 90 °C also yielded goat meat ball
with increased acceptability.
Acknowledgements
The authors would like to express their sincere thanks to the Halal
Institute of Prince of Songkla University, for the financial support
(Contract No. HAL06H59) and the Department of Food Technology,
PSU, for equipment. Special thanks go to General Starches Co., Ltd for
providing modified starches throughout the project.

Likeness score of gels from goat meat with different setting tem-
peratures is shown in Table 3. Setting at temperature up to 60 °C had no
effect on the appearance and color likeness of the resulting gel
(p > 0.05). However, setting at 70 °C caused the decreases in likeness
score (p < 0.05). This result might be related to the more brownish
color in gel set at 70 °C as evidenced by the lowest L*-value with con-
comitant increase in a* and b*-values (Table 2). No differences in taste
and odor likeness score among all the samples tested were observed
(p > 0.05). According to Madruga, Arruda, Narain, and Souza (2000),
some methyl-branched chain fatty acids existed in subcutaneous fat and
contributed to goat meat odor. The “goat-like” odor note was associated
with the presence of 4-methyloctanoic acid and 4-ethyloctanoic acids.
The presence of both fatty acids results in “goaty/sweaty” odor found in
cooked goat meat (Madruga et al., 2000). In the present study, fat
content was manually removed from goat meat before gel preparation.
Negligible goat-like odor was found for all samples. It was noted that
gel set at 60 °C had the highest flavor likeness (p < 0.05), while the
lowest score was obtained in gel set at 70 °C (p < 0.05). Setting at
higher temperature could induce undesirable reaction, especially lipid
oxidation. Heterocyclic compounds with 1–3 sulfur atoms in 5 and 6
membered rings (e.g. trithiolanes, trithianes, thiophenes) are prevalent
in boiled beef (Mottram, 1998). Those sulfur containing compounds
provide low odor thresholds with sulfurous, onion-like and meaty ar-
omas. With setting at 70 °C for 30 min, those compounds could be
Conflict of interest
The authors declared that there is no conflict of interest including
any financial, personal or other connections with other people or in-
stitutes.
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