LWT - Food Science and Technology 66 (2016) 318e323
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Effect of setting conditions on proteolysis and gelling properties of spotted featherback (Chitala ornata) muscle Piyawan Tachasirinukun a, Manat Chaijan b, Siriporn Riebroy a, * a b
Food and Nutrition Program, Faculty of Agriculture, Kasetsart University, Bangkok 10900, Thailand Department of Food Technology, School of Agricultural Technology, Walailak University, Thasala, Nakhon Si Thammarat 80160, Thailand
a r t i c l e i n f o
a b s t r a c t
Article history: Received 25 March 2015 Received in revised form 7 September 2015 Accepted 19 October 2015 Available online 22 October 2015
Gels from spotted featherback (SF) muscle were prepared by different setting conditions including 4 C/ 18 h, 25 C/30 min, 25 C/2 h, 40 C/30 min and 60 C/30 min followed by cooking at 90 C/20 min. Directly cooked gel was used as a control. SF gels set at 4 C/18 h and 60 C/30 min exhibited higher proteolytic degradation than did by other setting temperatures and control (P < 0.05) as evidenced by TCA-soluble peptides and the marked decrease in myosin heavy chain (MHC) under SDS-PAGE. For gelling properties, setting at 60 C/30 min showed the gel with lowest breaking force and highest expressible drip whereas setting at 25 C/30 min rendered the gel with highest breaking force (P < 0.05). Indeed, the higher the setting temperature applied the lower the a* value was observed (P < 0.05). However, the L* and b* values were varied among setting conditions. A finer structure of SF gel correlated well with the breaking force, particularly at medium setting temperature (25 C/30 min). Therefore, the setting regimes strongly influenced the proteolysis and gel properties of SF muscle. Setting at 25 C for 30 min was the best suit to prevent the proteolysis and hence strengthen the gel of SF muscle. © 2015 Elsevier Ltd. All rights reserved.
Keywords: Spotted featherback (Chitala ornata) Proteolysis Setting temperature Gel properties
1. Introduction Gelation is one of important functional properties of fish mince, surimi (washed fish mince) and ground meat. Basically, gelation is the cross-linking of randomly dispersed polymer chains to form a three-dimensional network (Smith, 1991) which including initial denaturation to cause protein unfolding, proteineprotein interactions and aggregation giving rise to matrices capable of holding water, fat or other components through physico-chemical forces (Mulvihill & Kinsella, 1987; Sikorski, 2001). However, proteineprotein interaction, known as association, aggregation and polymerization, are dependent upon temperatures, pH, and the type of muscle proteins used (Deng, Andrews, & Laursen, 1997). The three-dimensional structure is responsible for the elasticity and the textural strength of the gel (Sikorski, 2001). Myofibrillar proteins, particularly myosin and actomyosin, which are composed of multiple corporative domains, are able to form highly viscoelastic and rigid gels (Xiong, 1997). In general, protein gelation has been traditionally achieved by heating (Totosaus, Montejano, Salazar, & Guerrero, 2002). Upon heating, the denaturation and degradation
* Corresponding author. . E-mail address:
[email protected] (S. Riebroy). http://dx.doi.org/10.1016/j.lwt.2015.10.050 0023-6438/© 2015 Elsevier Ltd. All rights reserved.
of muscle proteins can occur with varying degrees depending on temperature and time. The influence of setting phenomenon on gel properties of surimi has been reported (Benjakul, Visessanguan, Riebroy, Ishizaki, & Tanaka, 2002). The setting temperature can affect enzymatic activities, protein degradation and gelation (Huang, Seguro, Motoki, & Tawada, 1992). In the case of surimi, incubation the sol at 0e40 C prior to heating is generally used for gel strengthening (Lanier, 1992). Setting can be performed at low temperatures (0e4 C), medium temperatures (25 C) and high temperatures (40 C) (Lanier, 1992), whereas protein degradation caused by proteinases, commonly found at 50e60 C (Lee et al., 1990; Kamath, Lanier, Foegeding, & Hamann, 1992) leading to gel structure disintegration or softening (Benjakul, Visessanguan, & Chantarasuwan, 2004; Jiang, 2000). Benjakul, Chantarasuwan, & Visessanguan, (2003) suggested that setting at different temperatures produces different gel characteristics and setting at low temperature usually takes a longer time. Spotted featherback (Chitala ornata, SF) is an important freshwater fish in economic value of Thailand. In general, SF meat has been used to produce many kinds of foods such as fish ball, fried curry-fish cake and som-fug (fermented fish sausage). SF is commonly sold in the form of scraped meat in plastic bags and kept on ice during transportation and distribution. For nutritional value,
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spotted featherback meat is a good source of protein (Puwastein et al., 1999). Generally, heating is usually applied for SF meat processing. SF meat can be mixed with other adjunct ingredients (salt, sugar, chili paste, etc.) and kept on ice overnight (18e24 h) before cooking. This preparation can be considered as low temperature setting of SF meat. In this traditional preparation, proteolysis and biochemical changes of muscle can be taken place to some degrees during iced storage. Those changes would associate with poorer gelling characteristics of final products. However, many products and recipes from SF mince were directly cooked (without setting). For instance, Thai green curry with fish ball (Kang-Keaw-Wan) production, the SF meat is knead with a pinch of salt (about 0.33%) and the ballshaped of mixture is boiled without setting. From point of view, SF meat is popularly used as a raw material for production of food product with high quality in textural properties. However, no information regarding the degradation of muscle proteins and gelforming ability of SF meat as affected by different setting conditions has been reported. Therefore, the objective of this study was to investigate the effect of setting conditions on proteolysis and gel properties of SF meat. 2. Materials and methods 2.1. Chemicals Sodium chloride (NaCl) and bromophenol blue were obtained from Carlo Erba (Milan, Italy). Trichloroacetic acid (TCA), methanol and bis-acrylamide were purchased from Merck (Darmstadt, Germany). Acetic acid, glutaraldehyde, ethanol, and b-mercaptoethanol (bME) was obtained from Sigma (Steinheim, Germany). N,N,N0 ,N0 - tetramethylethylenediamine (TEMED) was obtained from AMRESCO (Solon, OH, USA). Coomassie brilliant blue R-250 was obtained from Panreac (Barcelona, Spain). 2.2. Fish samples and preparation Fresh SF (body length about 60e65 cm and an average weight of 1.5e2.0 kg) were obtained from Bangpakong River, Prachin Buri, Thailand. After capture within 12 h, fish were transported in ice with a fish/ice ratio of 1:2 (w/w) to Food and Nutrition Laboratory, Faculty of Agriculture, Kasetsart University within 1 h. The whole fish were immediately washed, filleted and manually scraped into meat. The meat was kept on ice (2 h) during preparation and analysis. The pH value of SF meat was measured as described by the method of Benjakul, Seymour, Morrissey, and An (1997). 2.3. Gel preparation Before gel preparation, SF meat was manually mixed to uniformity. Moisture content of sample was measured according to the method of AOAC (2000) and adjusted to 80%. Then, the sample were added with 2.5 g/100 g NaCl and chopped for 5 min to obtain the homogenous sol. The sol was stuffed into polyvinylidine casing with a diameter of 2.5 cm and both ends of the casing were sealed tightly. To prepare gel, the sols were incubated at several conditions including 4 C/18 h, 25 C/30 min, 25 C/2 h, 40 C/30 min, 60 C/ 30 min prior heating at 90 C/20 min. The gel without setting was heated directly and used as the control. The gels were cooled in icewater for 30 min and stored for 24 h at 4 C prior to analyses.
319
homogenised with 27 ml of TCA (5 g/100 ml) at speed no.2 (11,000 rpm) using a homogeniser (T18 basic, IKA, Staufen, Germany). The homogenate were kept on ice for 1 h and centrifuged at 8000 g for 5 min using a refrigerated centrifuge (Allegra X-15R centrifuge, Beckman Coulter, California, USA). The soluble peptides in the supernatant were measured by the Lowry method (Lowry, Rosebrough, Farr, & Randall, 1951) and expressed as mmol tyrosine/g dry weight. 2.5. SDSepolyacrylamide gel electrophoresis (SDS-PAGE) SDS-PAGE was carried out according to the method of Leammli (1970) using 10 g/100 ml running gel and 4 g/100 ml stacking gel. Gel sample (3 g) were mixed with 27 ml of 5 g/100 ml SDS and homogenised for 1 min. The homogenate were incubated at 85 C for 1 h to dissolve the proteins, followed by centrifuged at 8500 g for 5 min at room temperature using a centrifuge (Allegra X-15R centrifuge, Beckman Coulter, USA). Protein concentrations were determined according to the Biuret method (Robinson & Hodgen, 1940) using bovine serum albumin as a standard. Solubilized samples were mixed at a 1:1 (v/v) ratio with the sample buffer (0.5 M TriseHCl, pH 6.8, containing 4 g/100 ml SDS and 20 g/100 ml glycerol) in the presence of 10 ml/100 ml bME. Samples (10 mg protein) were loaded onto polyacrylamide gels. The electrophoresis was carried out at 15 mA per gel using a vertical gel electrophoresis unit (Mini-Protean II; Bio-Rad Laboratories, Richmond, California, USA). After separation, protein bands were stained with 0.05% (w/ v) Coomassie Blue R-250 in 15 ml/100 ml methanol and 5 ml/ 100 ml acetic acid and destained with 30 ml/100 ml methanol and 10 ml/100 ml acetic acid. 2.6. Determination of expressible drip Expressible drip was measured according to the method of Ng (1978). A gel sample with a thickness of 0.5 cm were weighed and placed between two pieces of Whatman filter paper no. 1 at the top and three pieces of the same type of filter paper at the bottom. The standard weight (5 kg) were placed on the top of the sample and maintained for 2 min. The sample were then removed and weighed again. Expressible drip were calculated and expressed as percentage of sample weight. 2.7. Determination of textural properties Texture analysis, breaking force and deformation, of the gel were performed using a Texture Analyzer (TA-XT plus, Stable Micro System, Surrey, UK). Gels were equilibrated and evaluated at room temperature (25e28 C). Five cylinder-shaped samples with a length of 2.5 cm were prepared and subjected to determination. Breaking force (gel strength) and deformation (elasticity and deformability) were measured using the texture analyser equipped with a spherical plunger (diameter 5 mm, depression speed of 60 mm/min). 2.8. Determination of colour The colour of sample was measured in L* (lightness), a* (redness/greenness) and b* (yellowness/blueness) the using a ColorFlex (Colorflex, HunterLab, USA). 2.9. Determination of microstructure
2.4. Determination of TCA-soluble peptides TCA-soluble peptides were determined according to the method of Morrissey, Wu, Lin, & An (1993). Gel samples (3 g) were
Microstructure of gels with different setting temperatures and direct heating were determined as described by Jones and Mandigo (1982). Samples with a thickness of 2e3 mm were fixed with
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2.5 ml/100 ml glutaraldehyde in 0.2 mol/L phosphate buffer (pH 7.2) for 2 h. The samples were then rinsed for 1 h in distilled water before being dehydrated in ethanol with serial concentrations of 50, 70, 80, 90 and 100 ml/100 ml. Dried samples were mounted on a bronze stub and sputter-coated with gold. The specimens were visualised using a scanning electron microscope (JSM-5410LV, Jeol, Tokyo, Japan) at an acceleration voltage of 15 kV.
(1990) reported that proteolytic degradation of fish gels could be classified into two types according to the localization of the gel degradation-inducing factor (GIF) in muscle cells which can be induced by sarcoplasmic GIF. From the results, the protein degradation can be occurred during setting, especially 60 C for 30 min and 4 C for 18 h. Thus, the setting condition was strongly affected SF protein degradation.
2.10. Statistical analysis
3.1.2. Protein patterns Based on protein patterns (Fig. 2), myosin heavy chain (MHC) band intensity markedly decreased when SF gel was subjected to setting at 60 C for 30 min. However, no marked changes in actin bands of all samples were observed. Setting at 25 C, the longer the setting time applied, the lower the MHC band intensity was observed. Generally, optimum temperature for setting among species may be determined by the heat-stability of myosin and the rate of cross-linking may be dependent on the conformation of the substrate myosin at a given temperature rather than on the optimum temperature of transglutaminase activity (Benjakul, Chantarasuwan, et al., 2003; Kamath et al., 1992). The result was in accordance with Takeda and Seki (1996) and Ando, Tsukamasa, and Makinodan (1998), who found degradation products with molecular weights of 150 and 170 kDa during setting of walleye pollack surimi paste at 25 C and 30 C, respectively. Furthermore, Benjakul et al. (2004) found degradation products with molecular weights of 120 and 150 kDa during setting of surimi from threadfin bream, bigeye snapper, barracuda and bigeye croaker. From the result, setting at 25 C for 30 min showed the gel with greater polymerization of MHC and it was coincidental with the lowered TCA-soluble peptide content in this gel (Fig. 1). The setting temperatures would affect the proteinase activity. From the results, the proteolysis of SF muscle proteins occurred during setting at 4 C for 18 h and 60 C for 30 min, however the MHC was lowered obviously in latter setting condition. Thus, the SF meat could set at 25 C for 30 min prior to heating at 90 C for 20 min to minimize the protein degradation.
The data were subjected to analysis of variance (ANOVA) and mean comparison was performed by Duncan's Multiple Range Test (Steel & Torrie, 1980). Statistical analysis was performed using SPSS statistical analysis program (version 19.0). 3. Results and discussion 3.1. Proteolysis of spotted featherback (SF) gel as influenced by different setting conditions 3.1.1. TCA-soluble peptides Generally, TCA-soluble peptides of SF gels with prior setting at 4 C for 18 h and 60 C for 30 min were greater than those setting at other conditions (P > 0.05) (Fig. 1). The results indicated that the degradation of muscle proteins obviously occurred during setting at 4 C and 60 C. Proteases are found in the soluble sarcoplasmic component of muscle tissue, in association with cellular organelles, connective tissues and myofibrils, and in the interfiber space (Ashie & Simpson, 1997). Kamath et al. (1992) found that proteolysis in croaker paste increased with increasing temperature of setting between 40 and 50 C. The presence of proteolytic enzymes in fish muscle might be activated at 60 C, while both endogenous and microbial proteases (particularly psychrophilic bacteria) might contribute to the proteolysis at 4 C with longer incubation time. No differences in TCA-soluble peptides of gels setting at 25 C for 2 h and the control were found (P > 0.05). The setting at 25 C for 30 min exhibited the lowest TCA-soluble peptides (P < 0.05). This result was in agreement with Benjakul, Chantarasuwan, et al. (2003) who reported that suwari gel from some tropical fish, prepared by setting at 25 C, showed lower degradation, although the setting time increased up to 8 h Toyohara, Kinoshita, and Shimizu
3.2. Properties of spotted featherback (SF) gel as influenced by different setting conditions 3.2.1. Expressible drip The expressible drip of SF gels is shown in Table 1. SF gel
TCA-soluble peptide content (μmoles tyrosine/g dry weight)
12 kDa
9
a
b d
a
c
c
6
206 116 97.4
MHC
66.2 Actin
45
3
0 4/18
25/30
25/2
40/30
60/30
control
setting conditions Fig. 1. TCA-soluble peptides of gels from SF meat prepared by different setting conditions; 4/18: 4 C/18 h, 25/30: 25 C/30 min, 25/2: 25 C/2 h, 40/30: 40 C/30 min, 60/ 30: 60 C/30 min and without setting (control) followed by cooking at 90 C/20 min. Bars represent the standard deviation from triplicate determinations. Different letters indicated significant differences (P < 0.05).
S
4/18
25/30
25/2
40/30
60/30 control
Fig. 2. SDSepolyacrylamide gel electrophoresis (SDS-PAGE) protein pattern of SF gels prepared by different setting conditions; 4/18: 4 C/18 h, 25/30: 25 C/30 min, 25/2: 25 C/2 h, 40/30: 40 C/30 min, 60/30: 60 C/30 min and without setting (control) followed by cooking at 90 C/20 min. MHC: myosin heavy chain.
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underwent setting at 60 C for 30 min revealed the highest expressible drip (P < 0.05). No differences in expressible drip of SF gels setting at 4 C for 18 h, 25 C for 30 min or 2 h were observed (P > 0.05). SF gel setting at 40 C for 30 min exhibited the lowest expressible drip (P < 0.05). Niwa (1992) suggested that the more water retained in the gel network when gels had low expressible drip. Gradual alignment of protein molecules at medium temperature contributed to more ordered-network, which could imbibe more water (Benjakul, Chantarasuwan, et al., 2003). Chaijan, Panpipat, and Benjakul (2010) reported that gel of Indian
Table 1 Expressible drip (%) of gels from SF meat prepared by different setting conditions. Setting conditions
Expressible drip (%)
4 C 18 h 25 C 30 min 25 C 2 h 40 C 30 min 60 C 30 min 90 C 20 min (control)
90 90 90 90 90
C C C C C
20 20 20 20 20
min min min min min
4.02 4.00 3.89 3.62 4.81 3.97
± ± ± ± ± ±
0.07*b** 0.06bc 0.07c 0.01d 0.08a 0.32c
* Values are given as mean ± S.D. from five determinations. ** Different superscripts indicate the significant differences (P < 0.05).
24
800
c
16
a
b
a
ab
b
a
ab
c
600
Breaking force (g)
Deformation (mm)
20
321
12 8 4
d
e f
400
200
0
0 4/18
25/30
25/2
40/30
60/30
4/18
control
25/30
25/2
40/30
60/30
control
setting conditions
setting conditions
Fig. 3. Breaking force and deformation of gels from SF meat prepared by different setting conditions; 4/18: 4 C/18 h, 25/30: 25 C/30 min, 25/2: 25 C/2 h, 40/30: 40 C/30 min, 60/ 30: 60 C/30 min and without setting (control) followed by cooking at 90 C/20 min. Bars indicated standard deviation from five determinations. Different letters indicated significant differences (P < 0.05).
(A)
70
(B)
2.0 a
65
a b
a
b
d
e
a*
L*
c
1.5
60
c
1.0
d
e
e
40/30
60/30
0.5
55
0.0
50 4/18
25/30
25/2
40/30
60/30
control
4/18
25/30
25/2
control
setting conditions
setting conditions
(C)
14
a
13 b 12
b*
c
c
40/30
60/30
d
e 11 10 9 8 4/18
25/30
25/2
control
setting conditions Fig. 4. L* (A), a* (B) and b* (C) of gels from SF meat prepared by different setting conditions; 4/18: 4 C/18 h, 25/30: 25 C/30 min, 25/2: 25 C/2 h, 40/30: 40 C/30 min, 60/30: 60 C/ 30 min and without setting (control) followed by cooking at 90 C/20 min. Bars represent the standard deviation from five determinations. Different letters indicated significant differences (P < 0.05).
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Fig. 5. Microstructure of SF gels from SF meat prepared by different setting conditions; 4/18: 4 C/18 h, 25/30: 25 C/30 min, 25/2: 25 C/2 h, 40/30: 40 C/30 min, 60/30: 60 C/ 30 min and without setting (control) followed by cooking at 90 C/20 min.
mackerel, short-bodied mackerel and frigate mackerel surimi set at 60 C for 30 min prior heating had the highest expressible drip. During heating at 90 C for 20 min, rapid unfolding of proteins results in more intense coagulation (Niwa, 1992; Tammatinna, Benjakul, Visessanguan, & Tanaka, 2007). Therefore, the appropriate setting could be used to improve gel forming ability via nondisulfide covalent bonds. Different expressible moisture content suggested the differences in water holding capacity of gel network (Tammatinna et al., 2007). Low expressible moisture content of the gels suggested the more water retained in gel network (Niwa, 1992). From the results, expressible drip of SF gel was influenced by setting temperatures, particularly setting at 60 C for 30 min. Therefore, setting at low and medium temperatures could be used to improve the water holding capacity of SF gel. 3.2.2. Textural properties The breaking force and deformation of SF gels set under different conditions are shown in Fig. 3. SF gels set at 25 C for 30 min prior to heating at 90 C for 20 min exhibited the highest breaking force (P < 0.05), while gel set at 60 C for 30 min showed the lowest breaking force (P < 0.05). Generally, gelling properties of surimi were affected by the setting condition (Jiang, 2000; Lanier, 1992). Different setting temperatures resulted in the different breaking force of SF gel. During setting, several bonds induced protein aggregation particularly hydrophobic interaction and disulfide bonds were established (Benjakul, Visessanguan, Ishizaki, & Tanaka, 2001). Formation of large aggregates is presumably a prerequisite for formation of a good elastic gel (Chan, Gill, & Paulson, 1992). Also, heat-activated proteinases were associated with the degradation of surimi protein and gel softening (Benjakul, Visessanguan, & Tueksuban, 2003; Niwa, 1992). Proteolytic activity in fish muscle is associated with gel weakening in surimi (An, Peters, & Seymour, 1996; Benjakul et al., 2004). Chaijan et al.
(2010) found that the modori gel (set at 60 C) of Indian mackerel, short-bodied mackerel and frigate mackerel surimi exhibited the lowest breaking force compared to other setting conditions. Surimi gels from bigeye snapper, barracuda and bigeye croaker set at high temperature (40 C) showed higher protein degradation, compared with those set at medium temperature (25 C) (Benjakul, Visessanguan, et al., 2003, 2004). This phenomenon was induced by endogenous heat activated proteases, which can degrade myosin (Jiang, 2000). The lowest breaking force of SF gel set at 60 C for 30 min was in agreement with the highest TCA-soluble peptide content (Fig. 1) and protein degradation in SDS-PAGE pattern (Fig. 2). The high breaking force was concomitant with the decrease in MHC band intensity and the formation of high molecular weight polymerised protein band (Fig. 2). Gels set at 25 C for 30 min prior to heating at 90 C for 20 min showed the lowest deformation (P < 0.05) and no differences in deformation were observed among the other samples. From the results, breaking force of SF gel was governed by setting conditions. Furthermore, the proteolysis also contributed to poorer gel quality, particularly SF gel setting at 60 C for 30 min (Figs. 1 and 2). 3.2.3. Color L*, a* and b* values of SF gels set under different conditions are shown in Fig. 4. The SF gel set at 40 C for 30 min and 60 C for 30 min had higher L* value than other samples (P < 0.05) (Fig. 4A). The water release caused by denaturation and aggregation of muscle proteins might be taken place to a greater extent with high temperature setting (Table 1). Released water, especially at the gel surface, would increase the degree of light scattering. As a consequence, the L* value was increased. However, decrease in L* of the control (without setting) was observed (P > 0.05). This phenomenon can be influenced by temperature and possibly due to the greater denaturation, degradation and oxidation of pigments or
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other muscle proteins. Lower a* value of sample prepared by setting at 40 C for 30 min and 60 C for 30 min was observed (P < 0.05) (Fig. 4B). The results indicated that oxidation of myoglobin possibly occurred to a greater extent during heat-induced gelation. Myoglobin and haemoglobin play an essential role in the whiteness of gel (Chaijan, Benjakul, Visessanguan, & Faustman, 2007; Chen, 2000). Therefore, setting temperatures directly affected on colour of SF gels. 3.2.4. Microstructure Microstructures of gels from SF meat set under different conditions are illustrated in Fig. 5. The gels set at 4 C for 18 h, 25 C for 30 min, 25 C for 2 h and 40 C for 30 min showed finer and longer strands than those set at 60 C for 30 min and direct heating (control). When setting at 60 C for 30 min was applied, the gel network was disorganized and the three dimensional gel network was destroyed, corresponding to the very weak gel. This disruption of gel network was related to the degradation of MHC by proteases (Cao et al., 1999; Ngo, Katsuji, & Yoshiaki, 2010). The microstructure of gel has correlated well with the gel strength. As a result, setting at 25 C for 30 min enhanced the gel formation and induced a fine with a smaller and compact gel network, correlated with the highest gel strength. 4. Conclusion The setting conditions directly affected the proteolysis and gel properties of SF meat. The proteolysis significantly occurred during setting at 4 C for 18 h and 60 C for 30 min, contributing to the lowered water holding capacity and gel weakening of SF meat. From the results, setting at medium temperatures (25 C) could be used for SF gel production showing better gel quality than other setting regimes. Therefore, this setting condition is a promising means to improve gel quality of SF meat. Acknowledgements This study was financially supported from the research scholarship for international publication, the Graduate School, Kasetsart University, Bangkok, Thailand. References Ando, M., Tsukamasa, Y., & Makinodan, Y. (1998). Identification of 170 k component which appears in the setting process of surimi gel. Fisheries Science, 64, 497e498. An, H., Peters, M. Y., & Seymour, T. A. (1996). Roles of endogenous enzymes in suirmi gelation. Journal of Food Science and Technology, 7(10), 321e326. AOAC. (2000). Official method of analysis of AOAC international (17th ed.). Washington, DC: Association of Official Analytical Chemists. Ashie, I. N. A., & Simpson, B. K. (1997). Proteolysis in food myosystems e a review. Journal of Food Biochemistry, 21, 91e123. Benjakul, S., Chantarasuwan, C., & Visessanguan, W. (2003). Effect of medium temperature setting on gelling characteristic of surimi from some tropical fish. Journal of Food Chemistry, 82, 567e574. Benjakul, S., Seymour, T. A., Morrissey, M. T., & An, H. (1997). Physicochemical changes in Pacific whiting muscle proteins during iced storage. Journal of Food Science, 62, 729e733. Benjakul, S., Visessanguan, W., & Chantarasuwan, C. (2004). Effect of hightemperature setting on gelling characteristic of surimi from some tropical fish. Journal of Food Science and Technology, 39, 671e680. Benjakul, S., Visessanguan, W., Ishizaki, S., & Tanaka, M. (2001). Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus. Journal of Food Science, 66, 1311e1318. Benjakul, S., Visessanguan, W., Riebroy, S., Ishizaki, S., & Tanaka, M. (2002). Gelforming properties of surimi produced from bigeye snapper, Priacanthus tayenus and P. macracanthus, stored in ice. Journal of the Science of Food and Agriculture, 82, 1142e1451. Benjakul, S., Visessanguan, W., & Tueksuban, J. (2003). Heat activated proteolysis in
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