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Characteristics and properties of goat meat gels and balls as affected by setting conditions

Characteristics and properties of goat meat gels and balls as affected by setting conditions The properties of goat meat gels without and with 120  mmol/kg CaCl as influenced by setting time (30–120 min) at 60°C were studied. A gel set for 60 min with subsequent cooking for 20 min in the presence of CaCl had the highest breaking force and deformation with coincidentally lowest expressible moisture content (P < 0.05). However, no differences in the trichloroacetic acid-soluble peptide content were observed for all gels tested (P > 0.05). A  decrease in the myosin heavy- chain band intensity was noticeable when CaCl was incorporated, suggesting increased protein cross-linking. As setting time increased, the L* values increased with varying a* values, whereas no differences in b* values of gels were found, regardless of CaCl addition (P > 0.05). The gel containing CaCl with setting time of 60 min had the highest hardness, cohesiveness, gumminess, and chewiness (P  <  0.05) and showed the compact network with high interconnection between strands. Goat meat balls prepared under aforementioned conditions had higher texture and overall likeness scores, compared with the control (P < 0.05). Therefore, prior setting at 60°C for 60 min in the presence of CaCl is recommended for the manufacture of goat meat balls with improved quality. Key words: characteristic; gel; goat meat; setting; meat ball; calcium chloride. products can be prepared from goat meat. Viscoelastic property and Introduction gel-forming ability are generally essential for meat products. Protein Goat meat is extensively consumed in Africa and Asia (Arain et al., aggregation associated with several bonds, which stabilize the gel 2010) and is also used in the preparation of several dishes in the network, plays a major role in gelation (Tammatinna et al., 2007). Mediterranean region (Teixeira et al., 2011). Although interest in goat Different methods have been used to promote the gelling prop- meat varies in different communities, goat meat has created a niche as erty of mince or washed mince of fish meat (surimi). Surimi paste a popular choice for consumers of ethnic food (Wattanachant et al., is basically set, thus allowing endogenous transglutaminase (TGase) 2008). In general, consumer’s preference for goat meat is governed to induce the cross-linking of myosin. This leads to the increased by culture, and social and economic conditions. In Thailand, there gel strength (Tammatinna et  al., 2007). The acyl transfer from has been an increase in the production of goat meat in recent years γ-carboxyl amide groups of glutamine to ε-amino groups of lysine (Wasiksiri et al., 2010), owing to increasing consumer demand. Goat can be catalysed by TGase (EC 2.3.2.13), leading to the formation of meat production and consumption has also been extended to other ε-(γ-glutamyl) lysine linkage (Dondero et al., 2006). Likewise, meat niche markets in the Middle East and Asia. Furthermore, there is gel from terrestrial animals including pigs and cattle (Torley and another potential market in ethnic communities in western countries, Lanier, 1991; Kim et al., 1993; Park et al., 1996a; Dondero et al., which traditionally consume goat meat (Wattanachant et al., 2008). 2006), quails (Ikhlas et  al., 2011), rabbits (Samejima et  al., 1981; To widen the utilization of goat meat, value-added products Ishioroshi et al., 1982), and chickens (Smyth and O’neill, 1997) can should be produced to meet consumer demand and gel-type © The Author(s) 2019. Published by Oxford University Press on behalf of Zhejiang University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by- nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 130 S. Mad-Ali and S. Benjakul, 2019, Vol. 3, No. 2 be improved with prior setting before cooking. Nonetheless, Niwa group was used as the control (without CaCl addition). After CaCl 2 2 et al. (1993) documented that some mammalian vertebrates such as addition, the paste was mixed for another 1 min. During chopping, pigs, whales, and cattle were non-setting species. Low setting in those the temperature was maintained below 10°C. Distilled water was meats might be attributed to a low level of TGase. Furthermore, added to the meat paste to obtain a final moisture content of 80 the substrate available for TGase is likely to be limited. However, per cent and the mixture was further chopped for 3  min. Samples Dondero et al. (2006) found endogenous TGase in beef. Torley and of the paste obtained (200  g), without and with CaCl addition, Lanier (1991) documented that setting phenomenon was evident in were stuffed into polyvinylidene chloride casings with a diameter of beef at 25°C. The formation of isopeptides in chicken meat balls 2.5 cm. Both ends were sealed and subjected to incubation at 60°C heated to 71°C was induced by TGase from crude pig plasma (Tseng for different times (30, 60, and 120 min) in a temperature-controlled et al., 2000). water bath (W350, Memmert, Schwabach, Germany). The set Recently, Mad-Ali et  al. (2018) found that the optimal setting samples were subsequently cooked at 90°C for 20 min, followed by temperature of gel from goat meat was 60°C, indicating the role cooling in iced water for 30 min. The gel samples were kept at 4°C of endogenous TGase in the cross-linking of myosin heavy chains for 24 h before analysis. (MHC). In general, endogenous TGase is calcium-dependent enzyme and its activity can be maximized by adding calcium to Analysis the meat paste prior to setting (Chanarat et  al., 2012). A  lack of Breaking force and deformation sufficient calcium ions may limit setting mediated by endogenous The breaking force and deformation of the goat meat gels TGase in goat meat. Moreover, a sufficient setting time could allow were measured using a texture analyser (Model TAXT2, Stable TGase to induce protein cross-linking effectively. To the best of our MicroSystems, Surrey, UK) as tailored by Buamard and Benjakul knowledge, no information regarding the impact of setting times (2015). Before measurement, the cylindrical gel samples (2.5  cm and calcium ions on gel formation in goat meat exists. Thus, the in height) were equilibrated at room temperature (28–30°C). objective of this study was to determine the influence of setting time A  spherical plunger with a diameter of 5  mm and a constant and calcium (CaCl ) incorporation on the gelling properties of goat depression speed of 60 mm/min was used for testing. meat. Texture profile analysis Texture profile analysis (TPA) of the gel samples was performed Materials and Methods according to the method of Buamard and Benjakul (2015). A texture Chemicals analyser (Model TA-XT2, Stable Micro- Systems, Surrey, UK) with β-mercaptoethanol (βME) and sodium dodecyl sulfate (SDS) were a cylinder probe (35  mm in diameter) was used.The springiness procured from Sigma (St. Louis, MO). Foline–Ciocalteu’s phenol hardness, gumminess, chewiness, and cohesiveness of the samples reagent and trichloroacetic acid (TCA) were obtained from Merck were recorded. (Darmstadt, Germany). Acrylamide, bis-acrylamide, and N,N,N′,N′- tetramethylethylenediamine (TEMED) were purchased from Fluka Expressible moisture content (Buchs, Switzerland). The expressible moisture content was measured following the method of Benjakul et al. (2010). Sliced gel samples (5 mm thickness) were Collection and preparation of goat meat weighed accurately and placed between No.1 filter paper (Whatman Meat from a 1-year-old Boer goat was obtained from a local International Ltd., Maidstone, UK) with one piece at the bottom and slaughter house in Hat Yai district, Songkhla province, Thailand. two pieces on the top. The samples were subsequently pressed by a The goat meat was dissected, pooled, and used as composite samples. standard weight (5 kg) for 2 min. The samples were weighed again Meat (10 kg) was placed in a polyethylene bag and was transported after removal from the filter paper. The expressible moisture content in an insulated box containing ice (meat/ice ratio of 1:10, w/w) to the was calculated by the following equation: department of Food Technology, Prince of Songkla University, within Expressible moisture content = [(X − Y)/X] × 100, 30 min. Upon arrival, the meat was immediately washed with cool where X is the weight before compression and Y is the weight after water (5°C). The connective tissue and external fat were removed compression. manually. The meat was then aged at 4–5°C for 24 h. Subsequently, it was placed in a polyethylene bag, heat-sealed, and stored at −20°C until use. The storage time was not longer than 1 month. Colour L*, a*, and b* values were measured by a Hunter lab colourimeter (Color Flex, Hunter Lab Inc., Reston, VA). The colourimeter was The impact of setting times and CaCl on the warmed-up for approximately 10 min. A white standard was used properties of goat meat gels for calibration. The total difference in colour (∆E*) was calculated Preparation of gel samples as recommended by Mad-Ali et al. (2017). The frozen goat meat was thawed at 4°C until a core temperature of 0–2°C was achieved. The meat was washed thoroughly with TCA-soluble peptide content running water (4°C). A  sample was minced to uniformity using a mincer (National Model MK-5080M, Selangor, Malaysia) for 3 min. The TCA-soluble peptide content was determined following the Subsequently, 0.3 per cent phosphate, 2.5 per cent NaCl, 2.5 per method of Morrissey et al. (1993). The chopped sample was added cent sugar, 0.3 per cent ground black pepper, and 3 per cent distarch with cold 5 per cent TCA. After homogenization and centrifugation, phosphate were added. The mixture was mixed well for 2 min. The TCA-soluble peptide from supernatant was determined according to paste obtained was divided into two groups. The first group was the method of Lowry et al. (1951) and expressed as μmol tyrosine added with CaCl at a concentration of 120  mmol/kg. Another equivalent/g sample. 2 Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 Goat meat gels and balls, 2019, Vol. 3, No. 2 131 SDS-polyacrylamide gel electrophoresis The protein patterns of the goat meat gels were analysed by SDS- polyacrylamide gel electrophoresis (SDS-PAGE) (reducing condition) as per the method of Laemmli (1970). The SDS-PAGE gel consisted of 10 per cent running gel and 4 per cent stacking gel. After separation, the proteins were stained and destained as detailed by Buamard and Benjakul (2015). Microstructure and sensory properties of goat meat ball with the selected setting condition Goat meat balls containing 0 and 120 mmol/kg CaCl without and with prior setting (60  min) were prepared in the same manner as detailed above, except that the paste was formed manually into a spherical shape (approximately 2.5  cm in diameter). After heating followed by cooling, the meat balls were tempered as described above. All the samples were subjected to analysis. Microstructure The microstructure of the meatball samples was examined using a scanning electron microscope (SEM) following the method of Mad- Ali et al. (2018). The prepared samples were mounted on a bronze stub and sputter-coated with gold (Sputter coater SPI-Module, West Chester, PA). The specimens were visualized using an SEM (Quanta 400, FEI, Eindhoven, the Netherlands). Sensory property The meat balls were coded with 3-digit random numbers. The samples Figure 1. Breaking force and deformation of goat meat gels with different were displayed on white paper dishes. Thirty non-trained panellists setting times in the absence and presence of CaCl . Bars represent the (aged between 20 and 45)  comprising staff and students from the standard deviation (n  =  3). Different uppercase letters on the bars within Department of Food Technology, Prince of Songkla University, who the same setting time indicate significant differences (P  <  0.05). Different were familiar with meat balls were asked to taste and rate the goat lowercase letters on the bars indicate significant differences (P < 0.05). meat balls. To assess the samples, a nine-point hedonic scale was used as per the method of Meilgaard et al. (2006). setting time, polymerization of MHC might take place to a greater extent, resulting in a strengthened gel. The addition of CaCl at a level Statistical analysis of 120 mmol/kg with a setting time of 60 min prior to subsequent The experiments were carried out in triplicate. Data were subjected heating for 20 min increased the breaking force of the resulting gel to analysis of variance (ANOVA). Means were compared by the by 23.2 per cent, compared with that without CaCl prepared under Duncan’s multiple range test (Steel et al., 1980). Statistical analysis the same setting/heating condition. Nevertheless, no further increases was conducted using SPSS for Windows (SPSS Inc., Chicago, IL). in breaking force and deformation were obtained when setting times exceeded 60 min (P > 0.05). This might be due to the unavailability of substrate for the TGase since most of the substrate underwent Results and Discussion cross-linking within the first 60 min. For the gel without CaCl , the Effect of setting times and calcium chloride on breaking forces and deformation were also increased when setting properties of goat meat gels was implemented (P < 0.05). The result suggested that setting also played a role in enhancing gel strength. This was plausibly attributed Breaking force and deformation to indigenous TGase, which could act to some degree in the presence The breaking force and deformation of the goat meat gels set for of indigenous Ca ions. During setting at 60°C, the muscle protein different times at 60°C and the control gel (without prior setting) underwent unfolding, in which hydrophobic domains were exposed. in the absence and presence of 120  mmol/kg CaCl are illustrated As a result, hydrophobic–hydrophobic interaction could be formed, in Figure 1. When comparing the breaking force and deformation thus strengthening the gel network as evidenced by the increased of the goat meat gels without and with CaCl , higher values were breaking force. However, setting time (30–60 min) had no impact on found for those with CaCl added (P < 0.05). The use of CaCl was 2 2 both breaking force and deformation of gels without added CaCl (P therefore able to improve the gel strength of the goat meat as shown > 0.05). Kim et al. (1993) reported that beef myofibril pre-incubated by the increased breaking force, compared with those without at 60°C for 0–8 h before cooking at 80°C had similar shear stress. CaCl . Calcium ions at a sufficient concentration might play an Actomyosins in chicken, pork, and beef set at 30°C for various times integral role in the activation of the endogenous TGase present in (0–5 h) also showed no marked differences in breaking force (Niwa goat meat. Endogenous TGase was reported to induce the formation et al., 1993). of ε-(γ-glutamyl) lysine linkage between MHC during setting, thus All the gels with different setting times had higher breaking strengthening the gel network (Tsukamasa et al., 2002). When CaCl forces and deformations than the corresponding controls (P < 0.05). was incorporated, the breaking force and deformation increased With the same setting time, those with added CaCl possessed with increasing setting time up to 60 min (P < 0.05). With extended 2 Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 132 S. Mad-Ali and S. Benjakul, 2019, Vol. 3, No. 2 higher breaking forces and deformations (P < 0.05). CaCl has been (15–90 min). Cohesiveness is an essential parameter for comminuting reported to improve the textural property of heat-set gel in sev- meat products, whereas the secondary parameters include chewiness, eral kinds of fish, e.g., goatfish and bigeye snapper, by activating gumminess, and fracturability (Giese, 1995). For chewiness, the energy endogenous TGase (Julavittayanukul et  al., 2006; Benjakul et  al., required to masticate sample to the point required for swallowing it 2010). CaCl at levels of 10–120 mmol/kg was used for enhancing (Buamard and Benjakul, 2015), similar results were found to hardness gel properties of different fish species (Benjakul et al., 2004). and gumminess. Overall, goat meat gel containing CaCl (120 mmol/ Therefore, addition of 120 mmol/kg CaCl in combination with kg) with a setting time of 60 min had the improved textural properties. prior setting at 60°C for 60 min effectively increased the breaking The result was in agreement with breaking force and deformation force and deformation of gel from goat meat, in which breaking (Figure 1). Therefore, setting with appropriate times in conjunction force and deformation were increased by 52.6 and 27.4 per cent, with the addition of CaCl was effective in improvement of the TPA compared with that without CaCl and prior setting (direct heating). characteristics of the goat meat gel. Textural properties Expressible moisture content The textural properties of the goat meat gel with different setting times Lower expressible moisture contents were found in all the samples in the absence and presence of 120 mmol/kg CaCl are shown in Table subjected to prior setting, regardless of the addition of CaCl , compared 2 2 1. Compared with the control gels (direct heating), those with CaCl with the control samples (without setting) (P < 0.05) (Table 2). More added showed the higher hardness than those without CaCl (P < 0.05). water is generally liberated from the gel network with uneven protein With increasing setting time, the resulting gels had the increase in dispersion (Chaijan et al., 2010). For goat meat gel without CaCl , the hardness up to 60 min for those added with CaCl . Nevertheless, no setting time had no impact on the expressible moisture content (P > differences in hardness for the gels without CaCl were found with 0.05). For those containing CaCl , the decreases in expressible mois- 2 2 increases in setting time from 30 to 120 min (P > 0.05). ture contents were found as the setting time increased up to 60 min Hardness represents the force needed to compact a sample to (P < 0.05). No difference was noted between gels having setting times cause it to deform (Buamard and Benjakul, 2015). The hardness of 60 and 120 min (P > 0.05). CaCl might help develop the ordered results were in agreement with those for the breaking force (Figure structure, which could imbibe more water via the formation of non- 1). Ramırez et  ́ al. (2003) documented that when surimi from striped disulfide covalent bonds. Additionally, Ca ions could provide charge mullet containing CaCl was incubated at 39.3°C for 60  min, the to the protein, thus favouring water binding in the gel network. CaCl 2 2 maximum shear stress (89.6 kPa) was obtained. Higher springiness, most likely enhanced gel-forming ability through the formation of non- elastic recovery taking place when the compressive force is removed disulfide covalent bonds during setting, particularly for the longer time. (de Huidobro et al., 2005), was found for gel added with CaCl when As a result, a gel with three-dimensional network could entrap more setting (30–120 min) was implemented (P < 0.05). Setting time had no water as indicated by lowered expressible moisture content. Benjakul impact on springiness for gels without CaCl (P > 0.05). The springi- et al. (2010) also reported that the addition of CaCl contributed to the 2 2 ness result was in agreement with that for deformation (Figure 1), increase in water-holding capacity of surimi gel from goatfish. Thus, which refers to the elasticity of the gel (Chaijan et  al., 2010). Both the addition of CaCl in conjunction with setting with sufficient time gumminess (the energy necessary to break down a semi-solid food could enhance water entrapment of gel from goat meat. before swallowing) and chewiness (the energy required to masticate Colour a sample for swallowing) (Chang et al., 2012) increased when CaCl was added (P < 0.05). Similar results as influenced by setting time were The L* value of the control gels (without setting) was higher when attained to those of hardness. In general, there were no differences CaCl was added (P < 0.05) (Table 2). Irrespective of the addition of in cohesiveness, the capability of breaking down the internal struc- CaCl , increases in the L*value (lightness) of the gels were obtained ture (de Huidobro et  al., 2005), in gels without CaCl subjected to as the setting time increased (P < 0.05). This was probably due to the various setting times (P > 0.05). Nevertheless, gels containing CaCl fact that setting for a longer time caused denaturation of the pro- with setting times of 60 or 120  min had the increase in cohesive- tein, particularly pigments retained in the muscle, resulting in more ness (P < 0.05). Park et al. (1996b) reported that the cohesiveness of turbidity as indicated by the increased L* value. The gels showed surimi-like pork was unaltered when set at 50°C for different times varying a* values. For all gels, a* value was lowered, compared Table 1. Textural properties of goat meat gels with different setting times in the absence and presence of CaCl Treatments Setting* times (min) Hardness (N) Springiness (cm) Cohesiveness Gumminess (N) Chewiness (N × cm) Aa Aa Aa Aa Aa Without 120 mmol/kg CaCl 0 69.61 ± 1.85 0.89 ± 0.02 0.79 ± 0.01 53.79 ± 1.71 47.88 ± 1.05 Cb Ba ABa Cb Cb 30 114.88 ± 2.15 0.91 ± 0.02 0.80 ± 0.01 92.10 ± 1.30 83.72 ± 1.12 Db ABa ABa Cb Cb 60 112.12 ± 1.10 0.90 ± 0.01 0.81 ± 0.01 90.69 ± 0.93 81.71 ± 1.60 Db ABa BCa Cb Cb 120 112.91 ± 1.81 0.90 ± 0.02 0.82 ± 0.01 91.64 ± 2.28 83.46 ± 0.57 Ba ABa ABa Ba Ba With 120 mmol/kg CaCl 0 90.67 ± 1.50 0.90 ± 0.03 0.81 ± 0.01 73.44 ± 1.77 66.12 ± 0.78 Eb Cb BAa Db Db 30 128.12 ± 1.36 0.93 ± 0.01 0.81 ± 0.01 102.64 ± 1.26 95.42 ± 0.69 Fc Bb Cb Ec Ec 60 135.10 ± 1.27 0.92 ± 0.02 0.83 ± 0.00 112.13 ± 1.84 103.17 ± 1.02 Fc Cb Cb Ec Ec 120 137.03 ± 1.74 0.93 ± 0.01 0.83 ± 0.01 113.70 ± 1.59 105.74 ± 1.08 *Setting was conducted at 60°C. Values are presented as mean ± SD (n = 3). concentration indicate significant difference (P < 0.05). Different lowercase superscripts in the same column within the same CaCl Different uppercase superscripts in the same column indicate significant differences ( P < 0.05). Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 Goat meat gels and balls, 2019, Vol. 3, No. 2 133 with the control gel (without setting), except the gel containing 2007). During cooking at temperatures ranging from 60 to 80°C, CaCl and set for 60 min, which showed a higher a* value than the carboxyl proteases are associated with the proteolytic breakdown of corresponding control (P  <  0.05). No differences in the b* values connectin in the muscles of terrestrial animals (Lawrie and Ledward, of gels set for various times were found, regardless of the addition 2006). Park et al. (1996b) found that proteolysis of myosin in surimi- of CaCl (P > 0.05). Lower b* values were found in all the samples like pork took place during pre-incubation at 50°C for 30–90  min. with prior setting when compared with the control gels (without The result revealed that protein muscle from goat meat was likely to setting) (P  <  0.05). Protein denaturation or coagulation more be resistant to the degradation even for extended time, regardless of likely dominated a browning reaction such as a Maillard reaction. CaCl used. Therefore, setting time had no profound impact on prote- This resulted in the lower b* value as the setting time increased. olysis of gel from goat meat. Additionally, denatured haem proteins formed during heating plaus- ibly interacted with myofibrillar proteins, affecting the gel colour SDS-polyacrylamide gel electrophoresis (Lanier et al., 2014). For the gels without CaCl , the decreases in ∆E* The SDS-PAGE protein patterns of the goat meat gels prepared using values were found as the setting time increased (P < 0.05). For the different setting times without and with 120 mmol/kg CaCl are shown gels containing CaCl , gel with setting times of 30–120 min showed in Figure 2. Meat paste contained MHC as the major component. Actin no difference in ∆E* value (P > 0.05). When comparing gels without was also found as the second most prevalent protein. After gelation, and with CaCl , the latter had higher L* with lower ∆E* values than decreases in the MHC band were found in all the gels. The control gel the former (P < 0.05). CaCl played a role in improving the colour (heated at 90°C without prior setting) showed a higher MHC band in- of the gel. Benjakul et al. (2010) reported that CaCl might form a tensity than those with prior setting. Decreases in the MHC bands were complex with some anions in the muscle, resulting in the formation likely due to the polymerization of MHC as mediated by endogenous of insoluble particles, contributing to the light scattering in goatfish TGase. Protein cross-links stabilized by non-disulfide covalent bonds surimi gel. Therefore, setting with CaCl could improve the colour were stable under the condition used for SDS-PAGE. For gels without of the gel from goat meat by increasing the L* value and decreasing CaCl , no marked differences in MHC band intensity were observed the ∆E* values. with different setting times. The result revealed that setting time had no impact on the protein patterns of the goat meat gels when no CaCl TCA-soluble peptide content was added. This was consistent with the similar breaking force and No differences in the TCA-soluble peptide content among the goat deformation between those aforementioned samples (Figure 1). It meat gels with all setting times and that of goat meat paste were no- was noted that no obvious degradation of protein components was ticeable (P > 0.05) (Table 2). Goat meat paste possessed a TCA-soluble observed in all treatments. This result was in agreement with low TCA- peptide content of 0.40 µmol tyrosine equivalent/g sample. With the soluble peptide content for all gels tested (Table 2). However, MHC same setting time, similar TCA-soluble peptide contents were obtained of surimi-like pork decreased due to degradation when subjected to between samples without and with CaCl addition (P > 0.05). The setting at 50°C for 30–90 min (Park et al., 1996b). For gels with CaCl 2 2 result suggested that no degradation in the goat meat gels took place, addition, MHC band intensity decreased continuously as setting times regardless of CaCl addition or setting times. In general, autolytic deg- increased. However, no marked differences in MHC band intensity radation of muscle proteins is indicated by the TCA-soluble peptide were found in gels set for 60 and 120 min, suggesting that setting more content (Tammatinna et  al., 2007). The degradation occurs during than 60  min could not further polymerize MHC. When comparing heat-induced gelation of muscle proteins as a result of endogenous the protein patterns between gels without and with CaCl addition at proteinases (An et  al., 1996). Certain endogenous proteinases, e.g., the same setting time, the latter showed a lower MHC band intensity cathepsin, are activated at high temperatures (Tammatinna et  al., than the former. This was in accordance with higher breaking force Table 2. Expressible moisture content, colour, and TCA-soluble peptide content of goat meat gels with different setting times in the absence and presence of CaCl Treatments Setting** Expressible Colour value TCA-soluble times (min) moisture peptide content L* a* b* ∆E* content (%) (µmol tyrosine equivalent/g sample) Paste – – – – – 0.40 ± 0.03 Db Aa He Cb Dc Aa Without 120 mmol/kg CaCl 0 12.61 ± 0.05 57.26 ± 0.44 1.34 ± 0.13 15.26 ± 0.59 38.60 ± 0.62 0.40 ± 0.03 Ca Bb Db Ba Cb Aa 30 8.54 ± 0.06 60.03 ± 0.10 0.54 ± 0.07 12.18 ± 0.53 34.40 ± 0.28 0.42 ± 0.04 Ca Bb Ed ABa Cb Aa 60 8.63 ± 0.07 60.53 ± 0.26 0.73 ± 0.09 11.12 ± 0.07 34.53 ± 0.26 0.46 ± 0.06 Ca Cc Ca ABa Ba Aa 120 8.96 ± 0.08 63.50 ± 0.28 0.22 ± 0.08 11.03 ± 0.08 31.20 ± 0.24 0.46 ± 0.04 Cc Ba Fc Cb Cc Aa With 120 mmol/kg CaCl 0 8.75 ± 0.14 60.66 ± 0.65 0.82 ± 0.08 14.48 ± 0.73 35.14 ± 0.35 0.41 ± 0.05 Bb Cb Aa Aa Aa Aa 30 7.25 ± 0.02 64.67 ± 0.24 0.11 ± 0.04 10.56 ± 0.43 28.91 ± 0.20 0.40 ± 0.03 Aa Cb Gd Aa Aa Aa 60 5.52 ± 0.10 63.66 ± 0.65 1.11 ± 0.02 9.93 ± 0.22 29.19 ± 0.55 0.42 ± 0.05 Aa Dc Bb Aa Aa Aa 120 5.97 ± 0.08 66.05 ± 1.12 0.35 ± 0.08 9.85 ± 0.18 28.41 ± 0.99 0.42 ± 0.06 **Setting was conducted at 60°C. Values are presented as mean ± SD (n = 3). Different lowercase superscripts in the same column within the same CaCl concentration indicate significant difference (P < 0.05). Different uppercase superscripts in the same column indicate significant difference ( P < 0.05). Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 134 S. Mad-Ali and S. Benjakul, 2019, Vol. 3, No. 2 Figure 2. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) patterns of proteins in goat meat gels with different setting times in the absence and presence of CaCl . MHC = myosin heavy chain; M = molecular weight marker. Numbers denote setting time (minute). and deformation (Figure 1) as well as the hardness (Table 1) of the with CaCl addition rendered meat ball possessing compact and latter. Mad-Ali et  al. (2018) documented that the optimal tempera- interconnective structure. ture of TGase from goat meat was 60°C when CBZ-glutaminylglycine was used as a substrate. A  calcium-dependent acyl-transfer reaction Likeness score is considered as a reaction of cross-linking of MHC catalysed by en- Likeness scores of goat meat balls prepared without and with setting dogenous TGase during setting (Lee and Park, 1998). The result at 60°C for 60  min in the presence and absence of 120  mmol/kg reconfirmed that endogenous TGase played an important role in poly- CaCal are shown in Table 3. Meat balls prepared by direct heating merization of MHC in gels from goat meat. Factor XIII or TGase from (without prior setting) had lower appearance likeness than those crude pig plasma actively induced the formation of ε-(γ-glutamyl) ly- with prior setting for 60 min, regardless of CaCl addition (P < 0.05). sine isopeptides in chicken meat balls heated to obtain an internal tem- This result coincided with lower color likeness, more likely related perature of 71°C (Tseng et  al., 2000). For the control gels (without to lower lightness (L* values) in both directly heated samples (Table setting), the MHC band intensity of gel with CaCl was lower than 2). No differences in the odour, flavour, and taste likeness scores that without CaCl . During heating, TGase might be active to some ex- among all gels tested were found (P > 0.05). Goat meat’s odour is tent until it was inactivated at denaturation temperature. Nevertheless, attributed to some fatty acids, most especially the methyl-branched no changes in actin were found in all samples. It could be deduced chain found in its subcutaneous fat (Madruga et al., 2000). A ‘goat- that among the myofibrillar proteins, MHC was easily polymerised by like’ odour was perceived by the panellist, which could be attributed TGase from goat meat. Thus, setting time and CaCl synergistically to the presence of 4-ethyloctanoic acids and 4-methyloctanoic acid affected protein cross-linking in gel from goat meat. in the cooked meat. The ‘sweaty/goaty’ odour detected in cooked goat meat was more likely due to the presence of both fatty acids. In Effect of the selected setting times on this study, the fat content was removed manually from the goat meat microstructure and sensory property of goat before the production of the meat balls. Negligible goat-like odour was perceived for all the meatball samples, regardless of setting and meat balls CaCl addition. Meat balls set for 60 min in the presence of CaCl Microstructures 2 2 possessed the highest texture likeness (P < 0.05) and overall likeness The microstructures of goat meat balls without and with prior (P < 0.05) scores. This was attributed to the highest hardness, setting at 60°C for 60 min in the presence and absence of 120 mmol/ cohesiveness, gumminess, and chewiness of this sample (Table kg CaCal are illustrated in Figure 3. The control gel (without 1). Therefore, appropriate setting time in conjunction with CaCl setting) showed a looser and coarser network with larger voids 2 addition directly influenced the sensory property of goat meat balls. or cavities. Network of gel from goat meat ball with prior setting, followed by heating, possessed a higher density and more com- pactness than that observed in the control gel. The result suggested Conclusions that setting might effectively promote the connectivity of protein strands in gel network, in which the aggregation or alignment of The gel-forming ability and characteristics of goat meat were proteins was increased. Compared with gels without CaCl , those determined by setting time. A good quality gel with improved textural with CaCl addition had higher compact network with high inter- and sensory properties was obtained when CaCl was incorporated and 2 2 connection between strands. Density and higher interconnectivity setting at 60°C for 60 min before cooking for 20 min was conducted. of protein strands were involved in the increased breaking force of Under aforementioned conditions, the polymerization of the MHC and goat meat gel (Figure 1). More rigid gel was related to denser net- the lightness of the gel increased. Goat meat ball prepared under the work (Buamard and Benjakul, 2015). Setting at 60°C for 60  min selected condition showed the increased likeness scores. Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 Goat meat gels and balls, 2019, Vol. 3, No. 2 135 Figure 3. Electron microscopic images of goat meat balls without and with prior setting in the absence and presence of CaCl . Numbers denote setting time (minute), C; Magnification: 10,000×. Table 3. Likeness score of goat meat balls without and with prior setting in the absence and presence of CaCl Treatments Setting* Attributes times (min) Appearance Colour Odour Flavour Taste Texture Overall a a a a a a a Without 120 mmol/kg 0 6.83 ± 1.28 6.21 ± 1.21 7.17 ± 1.14 7.28 ± 1.13 7.31 ± 1.07 6.97 ± 1.30 6.93 ± 0.96 b b a a a ab ab CaCl 60 7.20 ± 1.05 7.03 ± 1.30 7.00 ± 1.41 7.16 ± 0.89 7.13 ± 0.96 7.14 ± 0.95 7.31 ± 0.93 a b a a a ab ab With 120 mmol/kg 0 7.07 ± 1.13 7.01 ± 1.09 7.10 ± 1.23 7.17 ± 1.20 7.31 ± 1.20 7.00 ± 1.00 7.21 ± 1.21 b b a a a c b CaCl 60 7.34 ± 1.14 7.10 ± 1.26 7.00 ± 1.41 7.21 ± 1.29 7.17 ± 1.28 7.72 ± 0.87 7.66 ± 0.94 *Setting was conducted at 60°C. Values are presented as mean ± SD (n = 3). Different lowercase superscripts in the same column indicate significant difference ( P < 0.05). Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 136 S. Mad-Ali and S. Benjakul, 2019, Vol. 3, No. 2 Lawrie, R. A., Ledward, D. A. (2006). Lawrie’s Meat Science. UK: Woodhead Acknowledgements Publishing Limited and CRC Press LLC. The authors would like to express their sincere thanks to the Office of Higher Lee, N., Park, J. W. (1998). Calcium compounds to improve gel functionality of Pa- Education Commission, Ministry of Education, Thailand and the Halal Institute cific whiting and Alaska pollock surimi. Journal of Food Science, 63: 969–974. of Prince of Songkla University, for financial support. Special thanks go to General Lowry,  O.  H., Rosebrough,  N.  J., Farr,  A.  L., Randall,  R.  J. (1951). Protein Starches Co., Ltd for providing modified starches throughout the project. measurement with the folin phenol reagent. The Journal of Biological Chemistry, 193: 265–275. Mad-Ali, S., Benjakul, S., Prodpran, T., Maqsood, S. (2017). 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Characteristics and properties of goat meat gels and balls as affected by setting conditions

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Oxford University Press
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© The Author(s) 2019. Published by Oxford University Press on behalf of Zhejiang University Press.
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Abstract

The properties of goat meat gels without and with 120  mmol/kg CaCl as influenced by setting time (30–120 min) at 60°C were studied. A gel set for 60 min with subsequent cooking for 20 min in the presence of CaCl had the highest breaking force and deformation with coincidentally lowest expressible moisture content (P < 0.05). However, no differences in the trichloroacetic acid-soluble peptide content were observed for all gels tested (P > 0.05). A  decrease in the myosin heavy- chain band intensity was noticeable when CaCl was incorporated, suggesting increased protein cross-linking. As setting time increased, the L* values increased with varying a* values, whereas no differences in b* values of gels were found, regardless of CaCl addition (P > 0.05). The gel containing CaCl with setting time of 60 min had the highest hardness, cohesiveness, gumminess, and chewiness (P  <  0.05) and showed the compact network with high interconnection between strands. Goat meat balls prepared under aforementioned conditions had higher texture and overall likeness scores, compared with the control (P < 0.05). Therefore, prior setting at 60°C for 60 min in the presence of CaCl is recommended for the manufacture of goat meat balls with improved quality. Key words: characteristic; gel; goat meat; setting; meat ball; calcium chloride. products can be prepared from goat meat. Viscoelastic property and Introduction gel-forming ability are generally essential for meat products. Protein Goat meat is extensively consumed in Africa and Asia (Arain et al., aggregation associated with several bonds, which stabilize the gel 2010) and is also used in the preparation of several dishes in the network, plays a major role in gelation (Tammatinna et al., 2007). Mediterranean region (Teixeira et al., 2011). Although interest in goat Different methods have been used to promote the gelling prop- meat varies in different communities, goat meat has created a niche as erty of mince or washed mince of fish meat (surimi). Surimi paste a popular choice for consumers of ethnic food (Wattanachant et al., is basically set, thus allowing endogenous transglutaminase (TGase) 2008). In general, consumer’s preference for goat meat is governed to induce the cross-linking of myosin. This leads to the increased by culture, and social and economic conditions. In Thailand, there gel strength (Tammatinna et  al., 2007). The acyl transfer from has been an increase in the production of goat meat in recent years γ-carboxyl amide groups of glutamine to ε-amino groups of lysine (Wasiksiri et al., 2010), owing to increasing consumer demand. Goat can be catalysed by TGase (EC 2.3.2.13), leading to the formation of meat production and consumption has also been extended to other ε-(γ-glutamyl) lysine linkage (Dondero et al., 2006). Likewise, meat niche markets in the Middle East and Asia. Furthermore, there is gel from terrestrial animals including pigs and cattle (Torley and another potential market in ethnic communities in western countries, Lanier, 1991; Kim et al., 1993; Park et al., 1996a; Dondero et al., which traditionally consume goat meat (Wattanachant et al., 2008). 2006), quails (Ikhlas et  al., 2011), rabbits (Samejima et  al., 1981; To widen the utilization of goat meat, value-added products Ishioroshi et al., 1982), and chickens (Smyth and O’neill, 1997) can should be produced to meet consumer demand and gel-type © The Author(s) 2019. Published by Oxford University Press on behalf of Zhejiang University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by- nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 130 S. Mad-Ali and S. Benjakul, 2019, Vol. 3, No. 2 be improved with prior setting before cooking. Nonetheless, Niwa group was used as the control (without CaCl addition). After CaCl 2 2 et al. (1993) documented that some mammalian vertebrates such as addition, the paste was mixed for another 1 min. During chopping, pigs, whales, and cattle were non-setting species. Low setting in those the temperature was maintained below 10°C. Distilled water was meats might be attributed to a low level of TGase. Furthermore, added to the meat paste to obtain a final moisture content of 80 the substrate available for TGase is likely to be limited. However, per cent and the mixture was further chopped for 3  min. Samples Dondero et al. (2006) found endogenous TGase in beef. Torley and of the paste obtained (200  g), without and with CaCl addition, Lanier (1991) documented that setting phenomenon was evident in were stuffed into polyvinylidene chloride casings with a diameter of beef at 25°C. The formation of isopeptides in chicken meat balls 2.5 cm. Both ends were sealed and subjected to incubation at 60°C heated to 71°C was induced by TGase from crude pig plasma (Tseng for different times (30, 60, and 120 min) in a temperature-controlled et al., 2000). water bath (W350, Memmert, Schwabach, Germany). The set Recently, Mad-Ali et  al. (2018) found that the optimal setting samples were subsequently cooked at 90°C for 20 min, followed by temperature of gel from goat meat was 60°C, indicating the role cooling in iced water for 30 min. The gel samples were kept at 4°C of endogenous TGase in the cross-linking of myosin heavy chains for 24 h before analysis. (MHC). In general, endogenous TGase is calcium-dependent enzyme and its activity can be maximized by adding calcium to Analysis the meat paste prior to setting (Chanarat et  al., 2012). A  lack of Breaking force and deformation sufficient calcium ions may limit setting mediated by endogenous The breaking force and deformation of the goat meat gels TGase in goat meat. Moreover, a sufficient setting time could allow were measured using a texture analyser (Model TAXT2, Stable TGase to induce protein cross-linking effectively. To the best of our MicroSystems, Surrey, UK) as tailored by Buamard and Benjakul knowledge, no information regarding the impact of setting times (2015). Before measurement, the cylindrical gel samples (2.5  cm and calcium ions on gel formation in goat meat exists. Thus, the in height) were equilibrated at room temperature (28–30°C). objective of this study was to determine the influence of setting time A  spherical plunger with a diameter of 5  mm and a constant and calcium (CaCl ) incorporation on the gelling properties of goat depression speed of 60 mm/min was used for testing. meat. Texture profile analysis Texture profile analysis (TPA) of the gel samples was performed Materials and Methods according to the method of Buamard and Benjakul (2015). A texture Chemicals analyser (Model TA-XT2, Stable Micro- Systems, Surrey, UK) with β-mercaptoethanol (βME) and sodium dodecyl sulfate (SDS) were a cylinder probe (35  mm in diameter) was used.The springiness procured from Sigma (St. Louis, MO). Foline–Ciocalteu’s phenol hardness, gumminess, chewiness, and cohesiveness of the samples reagent and trichloroacetic acid (TCA) were obtained from Merck were recorded. (Darmstadt, Germany). Acrylamide, bis-acrylamide, and N,N,N′,N′- tetramethylethylenediamine (TEMED) were purchased from Fluka Expressible moisture content (Buchs, Switzerland). The expressible moisture content was measured following the method of Benjakul et al. (2010). Sliced gel samples (5 mm thickness) were Collection and preparation of goat meat weighed accurately and placed between No.1 filter paper (Whatman Meat from a 1-year-old Boer goat was obtained from a local International Ltd., Maidstone, UK) with one piece at the bottom and slaughter house in Hat Yai district, Songkhla province, Thailand. two pieces on the top. The samples were subsequently pressed by a The goat meat was dissected, pooled, and used as composite samples. standard weight (5 kg) for 2 min. The samples were weighed again Meat (10 kg) was placed in a polyethylene bag and was transported after removal from the filter paper. The expressible moisture content in an insulated box containing ice (meat/ice ratio of 1:10, w/w) to the was calculated by the following equation: department of Food Technology, Prince of Songkla University, within Expressible moisture content = [(X − Y)/X] × 100, 30 min. Upon arrival, the meat was immediately washed with cool where X is the weight before compression and Y is the weight after water (5°C). The connective tissue and external fat were removed compression. manually. The meat was then aged at 4–5°C for 24 h. Subsequently, it was placed in a polyethylene bag, heat-sealed, and stored at −20°C until use. The storage time was not longer than 1 month. Colour L*, a*, and b* values were measured by a Hunter lab colourimeter (Color Flex, Hunter Lab Inc., Reston, VA). The colourimeter was The impact of setting times and CaCl on the warmed-up for approximately 10 min. A white standard was used properties of goat meat gels for calibration. The total difference in colour (∆E*) was calculated Preparation of gel samples as recommended by Mad-Ali et al. (2017). The frozen goat meat was thawed at 4°C until a core temperature of 0–2°C was achieved. The meat was washed thoroughly with TCA-soluble peptide content running water (4°C). A  sample was minced to uniformity using a mincer (National Model MK-5080M, Selangor, Malaysia) for 3 min. The TCA-soluble peptide content was determined following the Subsequently, 0.3 per cent phosphate, 2.5 per cent NaCl, 2.5 per method of Morrissey et al. (1993). The chopped sample was added cent sugar, 0.3 per cent ground black pepper, and 3 per cent distarch with cold 5 per cent TCA. After homogenization and centrifugation, phosphate were added. The mixture was mixed well for 2 min. The TCA-soluble peptide from supernatant was determined according to paste obtained was divided into two groups. The first group was the method of Lowry et al. (1951) and expressed as μmol tyrosine added with CaCl at a concentration of 120  mmol/kg. Another equivalent/g sample. 2 Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 Goat meat gels and balls, 2019, Vol. 3, No. 2 131 SDS-polyacrylamide gel electrophoresis The protein patterns of the goat meat gels were analysed by SDS- polyacrylamide gel electrophoresis (SDS-PAGE) (reducing condition) as per the method of Laemmli (1970). The SDS-PAGE gel consisted of 10 per cent running gel and 4 per cent stacking gel. After separation, the proteins were stained and destained as detailed by Buamard and Benjakul (2015). Microstructure and sensory properties of goat meat ball with the selected setting condition Goat meat balls containing 0 and 120 mmol/kg CaCl without and with prior setting (60  min) were prepared in the same manner as detailed above, except that the paste was formed manually into a spherical shape (approximately 2.5  cm in diameter). After heating followed by cooling, the meat balls were tempered as described above. All the samples were subjected to analysis. Microstructure The microstructure of the meatball samples was examined using a scanning electron microscope (SEM) following the method of Mad- Ali et al. (2018). The prepared samples were mounted on a bronze stub and sputter-coated with gold (Sputter coater SPI-Module, West Chester, PA). The specimens were visualized using an SEM (Quanta 400, FEI, Eindhoven, the Netherlands). Sensory property The meat balls were coded with 3-digit random numbers. The samples Figure 1. Breaking force and deformation of goat meat gels with different were displayed on white paper dishes. Thirty non-trained panellists setting times in the absence and presence of CaCl . Bars represent the (aged between 20 and 45)  comprising staff and students from the standard deviation (n  =  3). Different uppercase letters on the bars within Department of Food Technology, Prince of Songkla University, who the same setting time indicate significant differences (P  <  0.05). Different were familiar with meat balls were asked to taste and rate the goat lowercase letters on the bars indicate significant differences (P < 0.05). meat balls. To assess the samples, a nine-point hedonic scale was used as per the method of Meilgaard et al. (2006). setting time, polymerization of MHC might take place to a greater extent, resulting in a strengthened gel. The addition of CaCl at a level Statistical analysis of 120 mmol/kg with a setting time of 60 min prior to subsequent The experiments were carried out in triplicate. Data were subjected heating for 20 min increased the breaking force of the resulting gel to analysis of variance (ANOVA). Means were compared by the by 23.2 per cent, compared with that without CaCl prepared under Duncan’s multiple range test (Steel et al., 1980). Statistical analysis the same setting/heating condition. Nevertheless, no further increases was conducted using SPSS for Windows (SPSS Inc., Chicago, IL). in breaking force and deformation were obtained when setting times exceeded 60 min (P > 0.05). This might be due to the unavailability of substrate for the TGase since most of the substrate underwent Results and Discussion cross-linking within the first 60 min. For the gel without CaCl , the Effect of setting times and calcium chloride on breaking forces and deformation were also increased when setting properties of goat meat gels was implemented (P < 0.05). The result suggested that setting also played a role in enhancing gel strength. This was plausibly attributed Breaking force and deformation to indigenous TGase, which could act to some degree in the presence The breaking force and deformation of the goat meat gels set for of indigenous Ca ions. During setting at 60°C, the muscle protein different times at 60°C and the control gel (without prior setting) underwent unfolding, in which hydrophobic domains were exposed. in the absence and presence of 120  mmol/kg CaCl are illustrated As a result, hydrophobic–hydrophobic interaction could be formed, in Figure 1. When comparing the breaking force and deformation thus strengthening the gel network as evidenced by the increased of the goat meat gels without and with CaCl , higher values were breaking force. However, setting time (30–60 min) had no impact on found for those with CaCl added (P < 0.05). The use of CaCl was 2 2 both breaking force and deformation of gels without added CaCl (P therefore able to improve the gel strength of the goat meat as shown > 0.05). Kim et al. (1993) reported that beef myofibril pre-incubated by the increased breaking force, compared with those without at 60°C for 0–8 h before cooking at 80°C had similar shear stress. CaCl . Calcium ions at a sufficient concentration might play an Actomyosins in chicken, pork, and beef set at 30°C for various times integral role in the activation of the endogenous TGase present in (0–5 h) also showed no marked differences in breaking force (Niwa goat meat. Endogenous TGase was reported to induce the formation et al., 1993). of ε-(γ-glutamyl) lysine linkage between MHC during setting, thus All the gels with different setting times had higher breaking strengthening the gel network (Tsukamasa et al., 2002). When CaCl forces and deformations than the corresponding controls (P < 0.05). was incorporated, the breaking force and deformation increased With the same setting time, those with added CaCl possessed with increasing setting time up to 60 min (P < 0.05). With extended 2 Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 132 S. Mad-Ali and S. Benjakul, 2019, Vol. 3, No. 2 higher breaking forces and deformations (P < 0.05). CaCl has been (15–90 min). Cohesiveness is an essential parameter for comminuting reported to improve the textural property of heat-set gel in sev- meat products, whereas the secondary parameters include chewiness, eral kinds of fish, e.g., goatfish and bigeye snapper, by activating gumminess, and fracturability (Giese, 1995). For chewiness, the energy endogenous TGase (Julavittayanukul et  al., 2006; Benjakul et  al., required to masticate sample to the point required for swallowing it 2010). CaCl at levels of 10–120 mmol/kg was used for enhancing (Buamard and Benjakul, 2015), similar results were found to hardness gel properties of different fish species (Benjakul et al., 2004). and gumminess. Overall, goat meat gel containing CaCl (120 mmol/ Therefore, addition of 120 mmol/kg CaCl in combination with kg) with a setting time of 60 min had the improved textural properties. prior setting at 60°C for 60 min effectively increased the breaking The result was in agreement with breaking force and deformation force and deformation of gel from goat meat, in which breaking (Figure 1). Therefore, setting with appropriate times in conjunction force and deformation were increased by 52.6 and 27.4 per cent, with the addition of CaCl was effective in improvement of the TPA compared with that without CaCl and prior setting (direct heating). characteristics of the goat meat gel. Textural properties Expressible moisture content The textural properties of the goat meat gel with different setting times Lower expressible moisture contents were found in all the samples in the absence and presence of 120 mmol/kg CaCl are shown in Table subjected to prior setting, regardless of the addition of CaCl , compared 2 2 1. Compared with the control gels (direct heating), those with CaCl with the control samples (without setting) (P < 0.05) (Table 2). More added showed the higher hardness than those without CaCl (P < 0.05). water is generally liberated from the gel network with uneven protein With increasing setting time, the resulting gels had the increase in dispersion (Chaijan et al., 2010). For goat meat gel without CaCl , the hardness up to 60 min for those added with CaCl . Nevertheless, no setting time had no impact on the expressible moisture content (P > differences in hardness for the gels without CaCl were found with 0.05). For those containing CaCl , the decreases in expressible mois- 2 2 increases in setting time from 30 to 120 min (P > 0.05). ture contents were found as the setting time increased up to 60 min Hardness represents the force needed to compact a sample to (P < 0.05). No difference was noted between gels having setting times cause it to deform (Buamard and Benjakul, 2015). The hardness of 60 and 120 min (P > 0.05). CaCl might help develop the ordered results were in agreement with those for the breaking force (Figure structure, which could imbibe more water via the formation of non- 1). Ramırez et  ́ al. (2003) documented that when surimi from striped disulfide covalent bonds. Additionally, Ca ions could provide charge mullet containing CaCl was incubated at 39.3°C for 60  min, the to the protein, thus favouring water binding in the gel network. CaCl 2 2 maximum shear stress (89.6 kPa) was obtained. Higher springiness, most likely enhanced gel-forming ability through the formation of non- elastic recovery taking place when the compressive force is removed disulfide covalent bonds during setting, particularly for the longer time. (de Huidobro et al., 2005), was found for gel added with CaCl when As a result, a gel with three-dimensional network could entrap more setting (30–120 min) was implemented (P < 0.05). Setting time had no water as indicated by lowered expressible moisture content. Benjakul impact on springiness for gels without CaCl (P > 0.05). The springi- et al. (2010) also reported that the addition of CaCl contributed to the 2 2 ness result was in agreement with that for deformation (Figure 1), increase in water-holding capacity of surimi gel from goatfish. Thus, which refers to the elasticity of the gel (Chaijan et  al., 2010). Both the addition of CaCl in conjunction with setting with sufficient time gumminess (the energy necessary to break down a semi-solid food could enhance water entrapment of gel from goat meat. before swallowing) and chewiness (the energy required to masticate Colour a sample for swallowing) (Chang et al., 2012) increased when CaCl was added (P < 0.05). Similar results as influenced by setting time were The L* value of the control gels (without setting) was higher when attained to those of hardness. In general, there were no differences CaCl was added (P < 0.05) (Table 2). Irrespective of the addition of in cohesiveness, the capability of breaking down the internal struc- CaCl , increases in the L*value (lightness) of the gels were obtained ture (de Huidobro et  al., 2005), in gels without CaCl subjected to as the setting time increased (P < 0.05). This was probably due to the various setting times (P > 0.05). Nevertheless, gels containing CaCl fact that setting for a longer time caused denaturation of the pro- with setting times of 60 or 120  min had the increase in cohesive- tein, particularly pigments retained in the muscle, resulting in more ness (P < 0.05). Park et al. (1996b) reported that the cohesiveness of turbidity as indicated by the increased L* value. The gels showed surimi-like pork was unaltered when set at 50°C for different times varying a* values. For all gels, a* value was lowered, compared Table 1. Textural properties of goat meat gels with different setting times in the absence and presence of CaCl Treatments Setting* times (min) Hardness (N) Springiness (cm) Cohesiveness Gumminess (N) Chewiness (N × cm) Aa Aa Aa Aa Aa Without 120 mmol/kg CaCl 0 69.61 ± 1.85 0.89 ± 0.02 0.79 ± 0.01 53.79 ± 1.71 47.88 ± 1.05 Cb Ba ABa Cb Cb 30 114.88 ± 2.15 0.91 ± 0.02 0.80 ± 0.01 92.10 ± 1.30 83.72 ± 1.12 Db ABa ABa Cb Cb 60 112.12 ± 1.10 0.90 ± 0.01 0.81 ± 0.01 90.69 ± 0.93 81.71 ± 1.60 Db ABa BCa Cb Cb 120 112.91 ± 1.81 0.90 ± 0.02 0.82 ± 0.01 91.64 ± 2.28 83.46 ± 0.57 Ba ABa ABa Ba Ba With 120 mmol/kg CaCl 0 90.67 ± 1.50 0.90 ± 0.03 0.81 ± 0.01 73.44 ± 1.77 66.12 ± 0.78 Eb Cb BAa Db Db 30 128.12 ± 1.36 0.93 ± 0.01 0.81 ± 0.01 102.64 ± 1.26 95.42 ± 0.69 Fc Bb Cb Ec Ec 60 135.10 ± 1.27 0.92 ± 0.02 0.83 ± 0.00 112.13 ± 1.84 103.17 ± 1.02 Fc Cb Cb Ec Ec 120 137.03 ± 1.74 0.93 ± 0.01 0.83 ± 0.01 113.70 ± 1.59 105.74 ± 1.08 *Setting was conducted at 60°C. Values are presented as mean ± SD (n = 3). concentration indicate significant difference (P < 0.05). Different lowercase superscripts in the same column within the same CaCl Different uppercase superscripts in the same column indicate significant differences ( P < 0.05). Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 Goat meat gels and balls, 2019, Vol. 3, No. 2 133 with the control gel (without setting), except the gel containing 2007). During cooking at temperatures ranging from 60 to 80°C, CaCl and set for 60 min, which showed a higher a* value than the carboxyl proteases are associated with the proteolytic breakdown of corresponding control (P  <  0.05). No differences in the b* values connectin in the muscles of terrestrial animals (Lawrie and Ledward, of gels set for various times were found, regardless of the addition 2006). Park et al. (1996b) found that proteolysis of myosin in surimi- of CaCl (P > 0.05). Lower b* values were found in all the samples like pork took place during pre-incubation at 50°C for 30–90  min. with prior setting when compared with the control gels (without The result revealed that protein muscle from goat meat was likely to setting) (P  <  0.05). Protein denaturation or coagulation more be resistant to the degradation even for extended time, regardless of likely dominated a browning reaction such as a Maillard reaction. CaCl used. Therefore, setting time had no profound impact on prote- This resulted in the lower b* value as the setting time increased. olysis of gel from goat meat. Additionally, denatured haem proteins formed during heating plaus- ibly interacted with myofibrillar proteins, affecting the gel colour SDS-polyacrylamide gel electrophoresis (Lanier et al., 2014). For the gels without CaCl , the decreases in ∆E* The SDS-PAGE protein patterns of the goat meat gels prepared using values were found as the setting time increased (P < 0.05). For the different setting times without and with 120 mmol/kg CaCl are shown gels containing CaCl , gel with setting times of 30–120 min showed in Figure 2. Meat paste contained MHC as the major component. Actin no difference in ∆E* value (P > 0.05). When comparing gels without was also found as the second most prevalent protein. After gelation, and with CaCl , the latter had higher L* with lower ∆E* values than decreases in the MHC band were found in all the gels. The control gel the former (P < 0.05). CaCl played a role in improving the colour (heated at 90°C without prior setting) showed a higher MHC band in- of the gel. Benjakul et al. (2010) reported that CaCl might form a tensity than those with prior setting. Decreases in the MHC bands were complex with some anions in the muscle, resulting in the formation likely due to the polymerization of MHC as mediated by endogenous of insoluble particles, contributing to the light scattering in goatfish TGase. Protein cross-links stabilized by non-disulfide covalent bonds surimi gel. Therefore, setting with CaCl could improve the colour were stable under the condition used for SDS-PAGE. For gels without of the gel from goat meat by increasing the L* value and decreasing CaCl , no marked differences in MHC band intensity were observed the ∆E* values. with different setting times. The result revealed that setting time had no impact on the protein patterns of the goat meat gels when no CaCl TCA-soluble peptide content was added. This was consistent with the similar breaking force and No differences in the TCA-soluble peptide content among the goat deformation between those aforementioned samples (Figure 1). It meat gels with all setting times and that of goat meat paste were no- was noted that no obvious degradation of protein components was ticeable (P > 0.05) (Table 2). Goat meat paste possessed a TCA-soluble observed in all treatments. This result was in agreement with low TCA- peptide content of 0.40 µmol tyrosine equivalent/g sample. With the soluble peptide content for all gels tested (Table 2). However, MHC same setting time, similar TCA-soluble peptide contents were obtained of surimi-like pork decreased due to degradation when subjected to between samples without and with CaCl addition (P > 0.05). The setting at 50°C for 30–90 min (Park et al., 1996b). For gels with CaCl 2 2 result suggested that no degradation in the goat meat gels took place, addition, MHC band intensity decreased continuously as setting times regardless of CaCl addition or setting times. In general, autolytic deg- increased. However, no marked differences in MHC band intensity radation of muscle proteins is indicated by the TCA-soluble peptide were found in gels set for 60 and 120 min, suggesting that setting more content (Tammatinna et  al., 2007). The degradation occurs during than 60  min could not further polymerize MHC. When comparing heat-induced gelation of muscle proteins as a result of endogenous the protein patterns between gels without and with CaCl addition at proteinases (An et  al., 1996). Certain endogenous proteinases, e.g., the same setting time, the latter showed a lower MHC band intensity cathepsin, are activated at high temperatures (Tammatinna et  al., than the former. This was in accordance with higher breaking force Table 2. Expressible moisture content, colour, and TCA-soluble peptide content of goat meat gels with different setting times in the absence and presence of CaCl Treatments Setting** Expressible Colour value TCA-soluble times (min) moisture peptide content L* a* b* ∆E* content (%) (µmol tyrosine equivalent/g sample) Paste – – – – – 0.40 ± 0.03 Db Aa He Cb Dc Aa Without 120 mmol/kg CaCl 0 12.61 ± 0.05 57.26 ± 0.44 1.34 ± 0.13 15.26 ± 0.59 38.60 ± 0.62 0.40 ± 0.03 Ca Bb Db Ba Cb Aa 30 8.54 ± 0.06 60.03 ± 0.10 0.54 ± 0.07 12.18 ± 0.53 34.40 ± 0.28 0.42 ± 0.04 Ca Bb Ed ABa Cb Aa 60 8.63 ± 0.07 60.53 ± 0.26 0.73 ± 0.09 11.12 ± 0.07 34.53 ± 0.26 0.46 ± 0.06 Ca Cc Ca ABa Ba Aa 120 8.96 ± 0.08 63.50 ± 0.28 0.22 ± 0.08 11.03 ± 0.08 31.20 ± 0.24 0.46 ± 0.04 Cc Ba Fc Cb Cc Aa With 120 mmol/kg CaCl 0 8.75 ± 0.14 60.66 ± 0.65 0.82 ± 0.08 14.48 ± 0.73 35.14 ± 0.35 0.41 ± 0.05 Bb Cb Aa Aa Aa Aa 30 7.25 ± 0.02 64.67 ± 0.24 0.11 ± 0.04 10.56 ± 0.43 28.91 ± 0.20 0.40 ± 0.03 Aa Cb Gd Aa Aa Aa 60 5.52 ± 0.10 63.66 ± 0.65 1.11 ± 0.02 9.93 ± 0.22 29.19 ± 0.55 0.42 ± 0.05 Aa Dc Bb Aa Aa Aa 120 5.97 ± 0.08 66.05 ± 1.12 0.35 ± 0.08 9.85 ± 0.18 28.41 ± 0.99 0.42 ± 0.06 **Setting was conducted at 60°C. Values are presented as mean ± SD (n = 3). Different lowercase superscripts in the same column within the same CaCl concentration indicate significant difference (P < 0.05). Different uppercase superscripts in the same column indicate significant difference ( P < 0.05). Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 134 S. Mad-Ali and S. Benjakul, 2019, Vol. 3, No. 2 Figure 2. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) patterns of proteins in goat meat gels with different setting times in the absence and presence of CaCl . MHC = myosin heavy chain; M = molecular weight marker. Numbers denote setting time (minute). and deformation (Figure 1) as well as the hardness (Table 1) of the with CaCl addition rendered meat ball possessing compact and latter. Mad-Ali et  al. (2018) documented that the optimal tempera- interconnective structure. ture of TGase from goat meat was 60°C when CBZ-glutaminylglycine was used as a substrate. A  calcium-dependent acyl-transfer reaction Likeness score is considered as a reaction of cross-linking of MHC catalysed by en- Likeness scores of goat meat balls prepared without and with setting dogenous TGase during setting (Lee and Park, 1998). The result at 60°C for 60  min in the presence and absence of 120  mmol/kg reconfirmed that endogenous TGase played an important role in poly- CaCal are shown in Table 3. Meat balls prepared by direct heating merization of MHC in gels from goat meat. Factor XIII or TGase from (without prior setting) had lower appearance likeness than those crude pig plasma actively induced the formation of ε-(γ-glutamyl) ly- with prior setting for 60 min, regardless of CaCl addition (P < 0.05). sine isopeptides in chicken meat balls heated to obtain an internal tem- This result coincided with lower color likeness, more likely related perature of 71°C (Tseng et  al., 2000). For the control gels (without to lower lightness (L* values) in both directly heated samples (Table setting), the MHC band intensity of gel with CaCl was lower than 2). No differences in the odour, flavour, and taste likeness scores that without CaCl . During heating, TGase might be active to some ex- among all gels tested were found (P > 0.05). Goat meat’s odour is tent until it was inactivated at denaturation temperature. Nevertheless, attributed to some fatty acids, most especially the methyl-branched no changes in actin were found in all samples. It could be deduced chain found in its subcutaneous fat (Madruga et al., 2000). A ‘goat- that among the myofibrillar proteins, MHC was easily polymerised by like’ odour was perceived by the panellist, which could be attributed TGase from goat meat. Thus, setting time and CaCl synergistically to the presence of 4-ethyloctanoic acids and 4-methyloctanoic acid affected protein cross-linking in gel from goat meat. in the cooked meat. The ‘sweaty/goaty’ odour detected in cooked goat meat was more likely due to the presence of both fatty acids. In Effect of the selected setting times on this study, the fat content was removed manually from the goat meat microstructure and sensory property of goat before the production of the meat balls. Negligible goat-like odour was perceived for all the meatball samples, regardless of setting and meat balls CaCl addition. Meat balls set for 60 min in the presence of CaCl Microstructures 2 2 possessed the highest texture likeness (P < 0.05) and overall likeness The microstructures of goat meat balls without and with prior (P < 0.05) scores. This was attributed to the highest hardness, setting at 60°C for 60 min in the presence and absence of 120 mmol/ cohesiveness, gumminess, and chewiness of this sample (Table kg CaCal are illustrated in Figure 3. The control gel (without 1). Therefore, appropriate setting time in conjunction with CaCl setting) showed a looser and coarser network with larger voids 2 addition directly influenced the sensory property of goat meat balls. or cavities. Network of gel from goat meat ball with prior setting, followed by heating, possessed a higher density and more com- pactness than that observed in the control gel. The result suggested Conclusions that setting might effectively promote the connectivity of protein strands in gel network, in which the aggregation or alignment of The gel-forming ability and characteristics of goat meat were proteins was increased. Compared with gels without CaCl , those determined by setting time. A good quality gel with improved textural with CaCl addition had higher compact network with high inter- and sensory properties was obtained when CaCl was incorporated and 2 2 connection between strands. Density and higher interconnectivity setting at 60°C for 60 min before cooking for 20 min was conducted. of protein strands were involved in the increased breaking force of Under aforementioned conditions, the polymerization of the MHC and goat meat gel (Figure 1). More rigid gel was related to denser net- the lightness of the gel increased. Goat meat ball prepared under the work (Buamard and Benjakul, 2015). Setting at 60°C for 60  min selected condition showed the increased likeness scores. Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 Goat meat gels and balls, 2019, Vol. 3, No. 2 135 Figure 3. Electron microscopic images of goat meat balls without and with prior setting in the absence and presence of CaCl . Numbers denote setting time (minute), C; Magnification: 10,000×. Table 3. Likeness score of goat meat balls without and with prior setting in the absence and presence of CaCl Treatments Setting* Attributes times (min) Appearance Colour Odour Flavour Taste Texture Overall a a a a a a a Without 120 mmol/kg 0 6.83 ± 1.28 6.21 ± 1.21 7.17 ± 1.14 7.28 ± 1.13 7.31 ± 1.07 6.97 ± 1.30 6.93 ± 0.96 b b a a a ab ab CaCl 60 7.20 ± 1.05 7.03 ± 1.30 7.00 ± 1.41 7.16 ± 0.89 7.13 ± 0.96 7.14 ± 0.95 7.31 ± 0.93 a b a a a ab ab With 120 mmol/kg 0 7.07 ± 1.13 7.01 ± 1.09 7.10 ± 1.23 7.17 ± 1.20 7.31 ± 1.20 7.00 ± 1.00 7.21 ± 1.21 b b a a a c b CaCl 60 7.34 ± 1.14 7.10 ± 1.26 7.00 ± 1.41 7.21 ± 1.29 7.17 ± 1.28 7.72 ± 0.87 7.66 ± 0.94 *Setting was conducted at 60°C. Values are presented as mean ± SD (n = 3). Different lowercase superscripts in the same column indicate significant difference ( P < 0.05). Downloaded from https://academic.oup.com/fqs/article-abstract/3/2/129/5428525 by Ed 'DeepDyve' Gillespie user on 11 June 2019 136 S. 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