Surimi Gelation Chemistry

Surimi and Surimi Seafood, Third Edition

Volumn , Issue , 2013, Pages 101-139

  Lanier, Tyre C ^a   Yongsawatdigul, Jirawat ^b   Carvajal Rondanelli, Patricio ^c  

^a NORTH CAROLINA STATE UNIVERSITY   (United States)

^b SURANAREE UNIVERSITY OF TECHNOLOGY   (Thailand)

^c PONTIFICIA UNIVERSIDAD CATÓLICA DE VALPARAÍSO   (Chile)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 85131973858     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/b16009-9     Document Type: Chapter

References (218)

1. PJ Bechtel. Muscle development and contractile proteins. In: Muscle as Food. PJ Bechtel, ed. Orlando: Academic Press Inc, pp. 2-31, 1986.
2. S Lowey, D Risby. Light chains from fast and slow muscle myosins. Nature 234:81-85, 1971.
3. A Asghar, AM Pearson. Influence of ante- and post-mortem treatments upon muscle composition and meat quality. Adv Food Res 26:53-213, 1980.
4. G Offer. Myosin filaments. In: Fibrous Protein Structure. JM Squire, PJ Vibert, eds. New York: Academic Press, 1987, pp 307-56.
5. FHC Crick. The packing of alpha-helices-Simple coiled-coils. Acta Crystallogr 6(8-9):689-97, 1953.
6. J Walshaw, DN Woolfson. Extended knobs-into-holes packing in classical and complex coiled-coil assemblies. J Struct Biol 144(3):349-61, 2003.
7. B Y Yu. Coiled-coils: Stability, specificity, and drug delivery potentials. Adv Drug Deliver Rev 54(8):1113-1129, 2002.
8. WD Kohn, CM Kay, RS Hodges. Salt effects on protein stability: Two-stranded alpha-helical coiled-coils containing inter- or intrahelical ion pairs. J Mol Biol 267(4):1039-52, 1997.
9. PE Hoppe, RH Waterston. Hydrophobicity variations along the surface of the coiled-coil rod may mediate striated muscle myosin assembly in Caenorhabditis elegans. J Cell Biol 135(2):371-82, 1996.
10. P Burkhard, S Ivaninskii, A Lustig. Improved coiled-coil stability by optimizing ionic interactions. J Mol Biol 318(3):901-10, 2002.
11. MJ Arrizubieta, E Bandman. The role of interhelical ionic interactions in myosin rod assembly. Biochem Bioph Res Co 244(2):588-93, 1998.
12. S Sato, T Tsuchiya. Microstructure of surimi and surimi-based products. In: Surimi Technology. TC Lanier and CM Lee, eds. New York: Marcel Dekker, pp. 501-18, 1992.
13. YM Feng, HO Hultin. Solubility of the proteins of mackerel light muscle at low ionic strength. J Food Biochem 21:479-96, 1997.
14. RW Craig, R Padron. Molecular structure of the sarcomere. In: Myology, 3rd edition. AC Engel, C Franzini-Armstrong, eds. New York: McGraw-Hill, 2004.
15. SD Kelleher, YM Feng, HO Hultin, MB Livingston. Role of initial muscle pH on the solubility of fish muscle proteins in water. J Food Biochem 28(4):279-92, 2004.
16. G Stefansson, H Hultin. On the solubility of cod muscle proteins in water. J Agric Food Chem 42:2656-64, 1994.
17. G Krishnamurthy, HS Chang, HO Hultin, YM Feng, S Srinivasan, SD Kelleher. Solubility of chicken breast muscle proteins in solutions of low ionic strength. J Agric Food Chem 44:408-15, 1996.
18. HS Chang, YM Feng, HO Hultin. Role of pH in gel formation of washed chicken muscle at low ionic strength. J Food Biochem 25(5):439-57, 2001.
19. B Wright. Effect of ultrastructural disruption and protein dispersion on gel-forming in myofibrillar gels. Dissertation, NC State University, Raleigh NC, 2007.
20. Y Ito, R Tatsumi, J-I Wakamatsu, T Nishimura, A Hattori. 2003. The solubilization of myofibrillar proteins of vertebrate skeletal muscle in water. Anim Sci J 74:417-25, 2003.
21. Y Zhang, QZ Zeng, ZW Zhu. Effect of ultrasonic treatment on the activities of endogenous transglutaminase and proteinase in tilapia (Sarotherodon nilotica). J Food Process Eng 34:1695-713, 2011.
22. C Cohen. Why fibrous proteins are romantic. J Struct Biol, 122(1-2):3-16, 1998.
23. M Wick. Filament assembly properties of the sarcomeric myosin heavy chain. Poultry Sci 78(5):735-42, 1999.
24. A Lupas. Coiled coils: New structures and new functions. Trends Biochem Sci 21(10):375-82, 1996.
25. M Lin, JW Park. Extraction of proteins from Pacific whiting mince at various washing conditions. J Food Sci 61:432-38, 1996.
26. HS Chang, HO Hultin, SM Dagher. Effect of MgCl2/sodium pyrophosphate on chicken breast muscle myosin solubilization and gelation. J Food Biochem 25(5):459-74, 2001.
27. M Chang. Thermal gelation properties of muscle protein gels made from different meat sources using alkaline or acid solubilization process. Dissertation, University of Massachusetts, Amherst, 2003.
28. I Undeland, SD Kelleher, HO Hultin. Recovery of functional proteins from herring (Culpea harengus) light muscle by an acid and alkaline solubilization process. J Agric Food Chem 50:7371-79, 2002.
29. R Tahergorabi, J Jaczynski. Physicochemical changes in surimi with salt substitute. Food Chem 132:1281-86, 2012.
30. R Tahergorabi, SK Beamer, KE Matak, J Jaczynski. Salt substitution in surimi seafood and its effects on instrumental quality attributes. LWT-Food Sci Technol 48:175-81, 2012.
31. A Moral, M Tejada, AJ Borderías. Frozen storage behavior of squid (Loligo vulgaris). Refrig Sci Technol 4:325-32, 1981.
32. A Moral, J Morales, C Ruiz-Capillas, P Montero. Muscle protein solubility of some cephalopods (pota and octopus) during frozen storage. J Sci Food Agric 82:663-68, 2002.
33. SMM Iguchi, T Tsuchiya, JJ Matsumoto. Studies on the freeze denaturation of squid actomyosin. Bull Jap Soc Sci Fish 47:1499-506, 1981.
34. MC Gómez-Guillén, O Martínez-Álvarez, P Montero. Functional and thermal gelation properties of squid mantle proteins affected by chilled and frozen storage. J Food Sci 68(6):1962-67, 2003.
35. T Ehara, K Nakagawa, T Tamiya, SF Noguchi, T Tsuchiya. Effect of paramyosin on invertebrate natural actomyosin gel formation. Fish Sci 70:306-13, 2004.
36. T Nakagawa, S Watabe, K Hashimoto. Electrophoretic analysis of sarcoplasmic proteins from fish muscle on polyacrylamide gels. Nippon Suisan Gakk 54:993-98, 1988.
37. LG Wild, SB Lehrer. Fish and shellfish allergy. Curr Allergy Asthma R 5:74-79, 2005.
38. T Suzuki. Fish and Krill Protein Processing Technology. London, UK: Applied Science Publishers, 1981, pp 1-56.
39. C Ladrat, V Verrez-Bagnis, J Noel, J Fleurence. in vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): Effects of cathepsins B, D and L. Food Chem 81:517-25, 2003.
40. G Terova, AG Cattaneo, E Preziosa, G Bernardini, M Saroglia. Impact of acute stress on antimicrobial polypeptides mRNA copy number in several tissues of marine sea bass (Dicentrarchus labrax). BMC Immunol 12:69, 2011.
41. Y Kim, J Yonsawatdigul, JW Park, S Thawornchinsombut. Characteristics of sarcoplasmic proteins and their interaction with myofibrillar proteins. J Food Biochem 29:517-32, 2005.
42. P Tadpichayangkoon, JW Park, J Yongsawatdigul. Conformational changes and dynamic rheological properties of fish sarcoplasmic proteins treated at various pHs. Food Chem 121:1046-52, 2010.
43. M Toyohara, M Murata, M Ando, S Kubota, M Sakaguchi, H Toyohara. Texture changes associated with insolubilization of sarcoplasmic proteins during salt-vinegar curing of fish. J Food Sci 64(5):804-07, 1999.
44. J Yongsawatdigul, BO Hemung. Structural changes and functional properties of threadfin bream sarcoplasmic proteins subjected to pH-shifting treatments and lyophilization. J Food Sci 75(3):C251-57, 2010.
45. M Okada, M Nakayama. The effect of oxidants on jelly strength of kamaboko. Bull Jap Soc Sci Fish 27:203, 1961.
46. G Rodger, P Wilding. Muscle proteins. In: Food Gels. Harris P, ed. London, UK: Elsevier Applied Science Publishers, 1990, p. 361.
47. M Okada. Effect of washing on the jelly forming ability of fish meat. Nippon Suisan Gakkaishi 30:255-261, 1962.
48. T Nakagawa, F Nagayama, H Ozaki, S Watabe, K Hashimoto. Effect of glycolytic enzymes on the gel-forming ability of fish muscle. Nippon Suisan Gakk 55:1045-50, 1989.
49. K Morioka, Y Shimizu. Relationship between the heat-gelling property and composition of fish sarcoplasmic proteins. Nippon Suisan Gakkaishi 59(9):1631, 1993.
50. M Karthikeyan, S Mathew, BA Shamsundar, V Prakash. Fractionation and properties of sarcoplasmic proteins from oil sardine (Sardinella iongiceps): Influence on the thermal gelation behavior of washed meat. J Food Sci 69(3):FEP79-84, 2004.
51. A Jafarpour, EM Gorczyca. Characteristics of sarcoplasmic proteins and their interaction with surimi and kamaboko gel. J Food Sci 74(1):N16-N22, 2009.
52. J Yongsawatdigul, P Piyadhammaviboon. Gel-enhancing effect and protein cross-linking ability of tilapia sarcoplasmic proteins. J Sci Food Agric 87(15):2810-16, 2007.
53. Miyaguchi, Y., Y Hayashi, T Sakamoto. Physiochemical properties of the thermal gel of water-washed meat in the presence of the more soluble fraction of porcine sarcoplasmic protein. Anim Sci J 78:77-84, 2007.
54. EJ Lee, YH Kim, NH Lee, SI Hong, K Yamamoto, YJ Kim. The role of sarcoplasmic protein in hydrostatic pressure-induced myofibrillar protein denaturation. Meat Sci 87:219-22, 2011.
55. YL Xiong. Myofibrillar protein from different muscle fiber types: Implications of biochemical and functional properties in meat processing. Crit Rev Food Sci Nutr 34(3):292-320, 1994.
56. K Morioka, Y Shimizu. Heat-coagulation property of fish sarcoplasmic proteins. Nippon Suisan Gakk 58:1529-33, 1992.
57. K Morioka, Y Shimizu. Contribution of sarcoplasmic proteins to gel formation of fish meat. Nippon Suisan Gakkaishi 56:929-33, 1990.
58. K Morioka, T Nishimura, A Obatake, Y Shimizu. Relationship between the myofibrillar protein gel strengthening effect and the composition of sarcoplasmic proteins from Pacific mackerel. Fish Sci 63(1):111-114, 1997.
59. WC Ko, MS Hwang. Contribution of milkfish sarcoplasmic protein to the thermal gelation of myofibrillar protein. Fish Sci 61:75-78, 1995.
60. NC Siang, K Miwa. Gel strength enhancing effect of aqueous extract of fish kidney tissue. Nippon Suisan Gakkaishi 58:805, 1992.
61. E Okazaki, K Kanna, T Suzuki. Effect of sarcoplasmic protein on rheological properties of fish meat gel formed by retort-heating. Bull Japan Soc Sci Fish 52:1821-27, 1986.
62. A Nowsad, E Katoh, S Kanoh, E Niwa. Effect of sarcoplasmic proteins on the setting of transglutaminase-free paste. Fish Sci 61(6):1039-40, 1995.
63. SJ Siriangkanakun, J. Yongsawatdigul. Trypsin inhibitory activity and gel-enhancing effect of sarcoplasmic proteins from common carp. J Food Sci 77(10):C1124-30, 2012.
64. S Benjakul, W Visessanguan, M Tanaka. Induced formation of dimethylamine and formaldehyde by lizardfish (Saurida micropectoralis) kidney trimethylamine-N-oxide demethylase. Food Chem 84:297-305, 2004.
65. JF Holmquist. Interrelations between salt-extractable protein, actomyosin, Ca-ATPase activity, and kamaboko quality prepared from frozen red hake fillets, mince and surimi. MS thesis, University Massachusetts, Amherst, Massachusetts, 1982, p. 91.
66. J Yongsawatdigul, JW Park, D Kolbe, Y AbuDagga, M Morrissey. Ohmic heating maximizes gel functionality of Pacific whiting surimi. J Food Sci 60(1):10-14, 1995.
67. DD Hamann, PM Amato, MC Wu, EA Foegeding. Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg white. J Food Sci 55:665-69, 1990.
68. P Piyadhammaviboon, J Yongsawatdigul. Proteinase inhibitory activity of sarcoplasmic proteins from threadfin bream (Nemipterus spp.). J Sci Food Agric 90(2):291-98, 2010.
69. RW Carrell, DR Boswell. Serpins: The superfamily of plasma serine proteinase inhibitors. In: Research Monographs in Cell and Tissue Physiology, Vol. 12. AJ Barrett, G Salvesen, eds. Amsterdam, Netherlands: Elsevier, pp. 403-420, 1986.
70. J Travis, GS Salvesen. Human plasma inhibitors. Annu Rev Biochem 52:655-709, 1983.
71. RW Carrell. Therapy by instant evolution. Nature 312:14, 1984.
72. K Hara, H Nakaoka, Y Nosaki, Y Tabata, T Ishihara. Purification and characterization of serine protease inhibitor from white croaker Argyrosomus argentatus ordinary muscle. Nippon Suisan Gakk 51:1029-36, 1985.
73. MP Sangorrin, EJ Folco, C Martone, JJ Sanchez. Purification and characterization of proteinase inhibitor from white croaker skeletal muscle (Micropogon opercuslaris). Int J Biochem Cell Biol 33:691-99, 2001.
74. MJ Cao, K Osatami, K Hara, T Ishihara. Purification of a novel myofibril-bound serine proteinase inhibitor (MBSPI) from the skeletal muscle of lizardfish. Comp Biochem Physiol B128:19-25, 2001.
75. MJ Cao, K Osatomi, R Matsuda, M Ohkubo, K Hara, I Tadashi. Purification of a novel serine proteinase inhibitor from skeletal muscle of white croaker (Argyrosomus argentatus). Biochem Biophys Res Commun 272:485-89, 2000.
76. LC Sun, LG Zhou, CH Du, QF Cai, K Hara, WJ Su, MJ Cao. Glucose-6-phosphate isomerase is an endogenous inhibitor to myofibril-bound serine proteinase of Crucian carp (Carassius auratus). J Agric Food Chem 57:5549-55, 2009.
77. K Li, H Lin, SM Kim. Purification and characterization of a cysteine protease inhibitor from chum salmon (Oncorhynchus keta) plasma. J Agric Food Chem 56(1):106-11, 2008.
78. U Ustadi, KY Kim, SM Kim. Purification and identification of a protease inhibitor from glassfish (Liparis tanakai) eggs. J Agric Food Chem 53(20):7667-72, 2005.
79. PA Carvajal-Rondanelli, TC Lanier. Diffusion of active proteins into fish meat to minimize proteolytic degradation. J Agric Food Chem 58(9):5300-7, 2010.
80. T Fukazawa, T Yasui, Y Hashimoto. Effect of some proteins on binding quality of an experimental sausage. J Food Sci 26(5):541-9, 1961.
81. T Fukazawa, T Yasui, Y Hashimoto. Effect of storage conditions on some physicochemical properties in experimental sausage prepared from fibrils. J Food Sci 26(4):331-36, 1961.
82. J Macfarlane, G Schmidt, R Turner. Binding meat pieces: A comparison of myosin, actomyosin, and sarcoplasmatic proteins as binding agents. J Food Sci 42:1603-5, 1977.
83. K Yamamoto. New explanation of heat-induced gelation structure. Chem Biol 46(11):748-50, 2008.
84. I Banga, A Szent-Gyorgyi. Preparation and properties of myosin A and B. Szeged, Hungary: University of Szeged. Studies from the Institute of Medicinal Chemistry, 1:5-15, 1942.
85. F Straub. Actin. Szeged, Hungary: University of Szeged Studies from the Institute of Medicinal Chemistry, 2:3-15, 1942.
86. A Szent-Gyorgyi. The crystallization of myosin and some of its properties and reactions. Szeged, Hungary: University of Szeged Studies from the Institute of Medicinal Chemistry, 3:76-85, 1943.
87. A Szent-Gyorgyi. Observations on actomyosin. Szeged, Hungary: University of Szeged Studies from the Institute of Medicinal Chemistry, 3:86-92, 1943.
88. M Ishioroshi, K Samejima, T Yashui. Heat-induced gelation of myosin: Factors of pH and salt concentrations. J Food Sci 44:1280-84, 1979.
89. T Lin, JW Park. Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH. J Food Sci 63:215-18, 1998.
90. A Smyth, D Smith, V Vega-Warner, E O’Neill. Thermal denaturation and aggregation of chicken breast muscle and sub fragments. J Agr Food Chem 44:1005-10, 1996.
91. T Gill, J Conway. Thermal aggregation of cod (Gadus morhua) muscle proteins using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a zero length cross-linker. Agric Biol Chem 53: 2553-62, 1989.
92. T Yasui, K Samajima. Recent advances in meat science in Japan: Functionality of muscle proteins in gelation mechanism of structured meat products. Japan Agr Res Quart 24:131-37, 1990.
93. K Yamamoto. Electron microscopy of thermal aggregation of myosin. J Biochem 108(6):896-98, 1990.
94. T Taguchi, M Ishizaka, M Tanaka, Y Nagashima, K Amano. Protein-protein interaction of fish myosin fragments. J Food Sci 52:1103-4, 1987.
95. JK Chan, TA Gill, AT Paulson. Thermal aggregation of myosin subfragments from cod and herring. J Food Sci 58:1057-61, 1069, 1993.
96. S Lowey, H Slayter, A Weeds, H Baker. Substructure of the myosin molecule. I. Sub fragments of myosin by enzymatic degradation. J Mol Biol 42:1-6, 1969.
97. W Visessanguan, H An. Effects of proteolysis and mechanism of gel weakening in heat-induced gelation of fish myosin. J Agric Food Chem 48, 1024-32, 2000.
98. A Sharp, G Offer. The mechanism of formation of gels from myosin molecules. J Sci Food Agric 58:63-73, 1992.
99. L Wicker, TC Lanier, DD Hamann, T Akahane. Thermal transitions in myosin-ANS fluorescence and gel rigidity. J Food Sci 51:1540-43, 1986.
100. J Chan, T Gill. Thermal aggregation of mixed fish myosins. J Agric Food Chem 42(12):2649-55. 1994.
101. T Maita, E Yajima, S Nagata, T Miyanishi, S Nakayama, G Matsuda. The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of the rod, and the complete 1, 938-residue sequence of the heavy chain. J Biochem 55:75-87, 1991.
102. JR Howe, DD Hamann, TC Lanier, JW Park. Fracture of Alaska pollock gels in water: Effects of minced muscle processing and test temperature. J Food Sci 59:770-80, 1994.
103. M Bouraoui, S Nakai, E Li-Chan. in situ investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy. Food Res Int 30:65-72, 1997.
104. NS Miroshinichenko, IV Balanuk, DN Nozdrenko. Packing of myosin molecules in muscle thick filaments. Cell Biol Int 24(6):327-33, 2000.
105. E Niwa. Chemistry of surimi gelation. In: Surimi Technology. TC Lanier, C Lee, eds. New York, NY: Marcel Dekker, 1992, pp. 389-427.
106. GM Gilleland, TC Lanier, DD Hamann. Covalent bonding in pressure-induced fish protein gels. J Food Sci 62(4):713-16, 1997.
107. S Ishizaki, M Ogasawara, M Tanaka, T Taguchi. Ultraviolet denaturation of flying fish myosin and its fragments. Fish Sci 60(5):603-06, 1994.
108. R Yoshinaka, M Shiraishi, S Ikeda, S. Effect of ascorbic acid on the gel formation of fish meat. Bull Jap Soc Sci Fish 38:511, 1972.
109. HG Lee, CM Lee, KH Chung, SA Lavery. Sodium ascorbate affects surimi gel-forming properties. J Food Sci 57:1343, 1992.
110. K Nishimura, M Goto, Y Itoh. Influence of oxygen radicals produced by ascorbic acid on amino acid composition of muscle proteins during the formation of a heat-induced gel of fish meat. Fish Sci 60(6):799-800, 1994.
111. A Kishi, Y Itoh, A Obatake. The polymerization of protein through disulfide bonding during the heating of carp myosin. Nippon Suisan Gakkaishi 61(1):75-80, 1995.
112. A Kishi, Y Itoh, A Obatake. Effects of tap water on the polymerization through SS bonding during the heating of carp myosin. Nippon Suisan Gakkaishi 63(2):242-43, 1997.
113. BY Kim. Rheological investigation of gel structure formation by fish proteins during setting and heat processing. PhD dissertation, North Carolina State University, Raleigh, North Carolina, 1987.
114. S Jiang, C Lan, C Tsao. New approach to improve the quality of mince fish products from freeze-thawed cod and mackerel. J Food Sci 51:310-12, 1986.
115. S Jiang, M Ho, S Jiang, L Lo, H Chen. Color and quality of mackerel surimi as affected by alkaline washing and ozonation. J Food Sci 63(4):652-55, 1998.
116. S Jiang, M Ho, S Jiang, H Chen. Purified NADPH-sulfite reductase from Saccharomyces cerevisiae effects on quality of ozonated mackerel surimi. J Food Sci 63(5):777-781, 1998.
117. E Niwa, E Chen, T Wang, S Kanoh, T Nakayama. Extraordinarity in the temperature-dependence of physical parameters of kamaboko. Nippon Suisan Gakkaishi 54:1789-93, 1988.
118. HG Lee, TC Lanier, DD Hamann. Covalent cross-linking effects on thermo-rheological profiles of fish protein gels. J Food Sci 62(1):25-28, 32, 1997.
119. C Cardoso B Ribeiro, R Mendes. Improvement of the gelling ability in restructured fish products: Effect of 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide level and pH. Eur Food Res Technol 234(6):935-43, 2012.
120. JK Chan, TA Gill, AT Paulson. The dynamics of thermal denaturation of fish myosins. Food Res Int 25: 117-23, 1992.
121. K Samejima, M Ishioroshi, T Yasui. Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin. J Food Sci 46:1412-18, 1981.
122. A Kishi, Y Itoh, A Obatake. The subfragment responsible for the polymerization of myosin heavy chain through SS bonding during the heating of carp myosin. Nippon Suisan Gakkaishi 63(2):237-41, 1997.
123. T Sano, SF Noguchi, JJ Matsumoto, T Tsuchiya. Thermal gelation characteristics of myosin subfragments. J Food Sci 55: 55-58, 1990.
124. T Higuchi, T Ojima, K Nishita. Heat-induced structural changes and aggregation of walley Pollack myosin in the light meromyosin region. Fish Sci 68:1145-50, 2002.
125. JC Acton, RL Dick. Functional roles of heat protein gelation in processed meat. In: Food Proteins. JE Kinsella, WG Soucie, eds. Champaign, IL: Am Oil Chem Soc, 1989.
126. HG Lee, TC Lanier. The role of covalent crosslinking in the texturizing of muscle protein sols. J Muscle Foods 6:125-38, 1996.
127. AB Smyth, DM Smith, E O’Neill. Disulfide bonds influence the heat-induced gel properties of chicken breast muscle myosin. J Food Sci 63(4):584-88, 1998.
128. M Ishioroshi, K Samejima, Y Arie, T Yasui. Effect of blocking the myosin-actin interaction in heat induced gelation of myosin in the presence of actin. Agric Biol Chem 44:2185, 1980.
129. K Samejima, M Ishioroshi, T Yasui. Heat induced gelling properties of actomyosin: Effect of tropomyosin and troponin. Agric Biol Chem 46:535-40, 1982.
130. T Yasui, M Ishioroshi, K Samejima. Effect of actomyosin on heat-induced gelation of myosin. Agric Biol Chem 46:1049-59, 1982.
131. T Sano, T Ohno, H Otsuka-Fuchino, JJ Matsumoto, T Tsuchiya. Carp natural actomyosin: Thermal denaturation mechanism. J Food Sci 59:1002-08, 1994.
132. TC Lanier, TS Lin, YM Liu, DD Hamann. Heat gelation properties of actomyosin and surimi prepared from Atlantic croaker. J Food Sci 47:1921-25, 1982.
133. E Niwa, G Nakajima. Difference in protein structure between elastic kamaboko and brittle one. Nippon Suisan Gakkaishi 41:579, 1975.
134. M Okada. Application of setting phenomenon for improving the quality of kamaboko. Bull Tokai Reg Fish Res 24:67-70, 1959.
135. TC Lanier. Functional properties of surimi. Food Technol 40:107-111, 1986.
136. K Arai, Y Funatsu, S Nanbu, N Yamada, N Kato. Some food additives as affecting materials of heat-induced gel formation with crosslinking of myosin heavy chain of frozen surimi. Proc. 206th Amer. Chem. Soc. Nat. Meet., Chicago.
137. O Esturk, JW Park, S Thawornchinsombut. Effects of thermal sensitivity of fish proteins from various species on rheological properties of gels. J Food Sci 69(8):E412-E16, 2004.
138. Y Funatsu, N Katoh, K Arai. Aggregate formation of salt-soluble proteins in salt-ground meat from walleye pollock surimi during setting. Nippon Suisan Gakkaishi 62(1):112-22, 1996.
139. C Imai, Y Tsukamasa, M Sugiyama, Y Minegishi, Y Shimizu. The effect of setting temperature on the relationship between ε-(γ-glutamyl)lysine crosslink content and breaking strength in salt-ground meat of sardine and Alaska pollock. Nippon Suisan Gakkaishi 62(1):104-11, 1996.
140. E Niwa, T Nakayama, I Hamada. Arylsulfonylatio chloride induced setting of dolphinfish sol. Nippon Suisan Gakkaishi 47:179-82, 1981.
141. E Niwa, R Suzuki, K Sato, T Nakayama, I Hamada. Setting of flesh sol induced by ethylsulfonylation. Nippon Suisan Gakkaishi 47:915-19, 1981.
142. L Wicker, TC Lanier, JA. Knopp, DD Hamann. Influence of various salts on heat-induced ANS fluorescence and gel rigidity development of Tilapia myosin. J Agr Food Chem 37:18-22, 1989.
143. BO Hemung, J Yongsawatdigul. Ca2+ affects physicochemical and conformational changes of threadfin bream myosin and actin in a setting model. J Food Sci 70:C455-60, 2005.
144. AA Nowsad, S Kanoh, E Niwa. Setting of transglutaminase-free actomyosin paste prepared from Alaska pollock surimi. Fish Sci 60(3):295-97, 1994.
145. AA Nowsad, S Kanoh, E Niwa. Setting of surimi paste in which transglutaminase is inactivated by p-chloromeruribenzoate. Fish Sci 60(2):185-88, 1994.
146. T Shoji, H Saeki, A Wakameda, M Nakamura, M Nonaka, M. Gelation of salted paste of Alaska pollock by high hydrostatic pressure and change in myofibrillar protein in it. Nippon Suisan Gakkaishi 56(12):2069-76, 1990.
147. T Ueda, R Kusaba, S Kamimura, E Okazaki, Y Fukuda, K Arai. Effect of heating on quality of pressure-texturized gels from chum salmon mince. Nippon Suisan Gakkaishi 63:600-07, 1997.
148. M Nonaka, R Ito, A Sawa, M Motoki, N Nio, N. Modification of several proteins by using Ca-independent microbial transglutaminase with high-pressure treatment. Food Hydrocolloids 11(3):351-53, 1997.
149. GA MacDonald, TC Lanier, FG Giesbrecht. Interaction of sucrose and zinc for cryoprotection of surimi. J Agric Food Chem 44(1):113-18, 1996.
150. Y Funatsu, H Hosokawa, S Nanbu, K Arai. Effects of sorbitol on gelation and crosslinking of myosin heavy chain of salt-ground meat from walleye pollock. Nippon Suisan Gakkaishi 59(9):1599-1607, 1993.
151. H Takeda, N Seki. Enzyme-catalyzed crosslinking and degradation of myosin heavy chain in walleye pollock surimi paste during setting. Fish Sci 62(3):462-67, 1996.
152. S Wang. Effects of endogenous, fungal and microbial transglutaminase in pollock surimi gelation. MS thesis, NC State University, Raleigh, 2004.
153. T Shoji, H Saeki, A Wakameda, M Nonaka. Influence of ammonium salt on the formation of pressure-induced gel from walleye pollock surimi. Nippon Suisan Gakkaishi 60(1):101-109, 1994.
154. IS Kang, JJ Wang, JCH Shih, T Lanier. Extracellular production of a functional soy cystatin by Bacillus subtilis. J Agric Food Chem 52(16):5052-56, 2004.
155. PJ Torley, TC Lanier. Setting ability of salted beef/pollock surimi mixtures. In: Seafood Science and Technology. E Graham Gligh, ed. Oxford, UK: Fishing News Books Ltd, 1992, pp. 305-16.
156. M Matukawa, F Hirata, S Kimura, K Arai. Effect of sodium pyrophosphate on gelling property and crosslinking of myosin heavy chain in setting-heating gel from walleye pollock surimi. Nippon Suisan Gakkaishi 62(1):94-103, 1996.
157. J Wan, N Seki. Effects of salts on transglutaminase-mediated crosslinking of myosin in suwari gel from walleye pollock. Nippon Suisan Gakkaishi 58(11):2181-87, 1992.
158. Y Shimizu, R Machida, S Takenami. Species variations in the gel-forming characteristics of fish meat paste. Nippon Suisan Gakkaishi 47:95-104, 1981.
159. S Ishikawa. Manufacture of kamaboko and surimi from sardines. II. Effect of temperature during manufacture on the jelly strength of kamaboko. Bull Tokai Reg Fish Res 94:37, 1978.
160. T Ikeuchi, W Simidu. Study on cold storage of brayed fish meat for the material of kamaboko. I. Effects of setting phenomenon on the jelly forming ability of frozen brayed fish meat. Bull Jap Soc Sci Fish 29:51, 1963.
161. H Araki, N Seki. Comparison of reactivity of transglutminase to various fish actomyosins. Bull Jap Soc Sci Fish 59(4):711-16, 1993.
162. E Niwa, T Suzumura, A Nowsad, S Kaho. Setting of actomyosin paste containing few amounts of transglutaminase. Nippon Suisan Gakkaishi 59(12):2043-46, 1993.
163. D Joseph, TC Lanier, DD Hamann. Temperature and pH effects of transglutaminase-catalyzed “setting” of crude fish actomyosin. J Food Sci 59(5):1018-23, 1036, 1994.
164. BO Hemung, ECY Li-Chan, J Yongsawatdigul. Reactivity of fish and microbial transglutaminases on glutaminyl sites of peptides derived from threadfin bream myosin. J Agric Food Chem 56(16):7510-16, 2008.
165. GG Kamath, TC Lanier, EA Foegeding, and DD Hamann. Non-disulfide covalent cross-linking of myosin heavy chain in “setting” of Alaska pollock and Atlantic croaker surimi. J Food Biochem 16:151-72, 1992.
166. NG Lee, JW Park. Calcium compounds to improve gel functionality of Pacific whiting and Alaska pollock surimi. J Food Sci 63(6):969-74, 1998.
167. S Benjakul, W Visessanguan, S Riebroy, S Ishizaki, M Tanaka. Gel-forming properties of surimi produced from bigeye snapper, Priacanthus tayenus and P. macracanthus, stored in ice. J Sci Food Agric 82:1442-51, 2002.
168. K Klesk, J Yongsawatdigul, JW Park, S Viratchakul, P Virulhakul. Physical behavior of tilapia surimi gels at various thermal treatments as compared to Alaska Pollack and Pacific whiting surimi. J Aqua Food Prod 9(3): 91-104, 2000.
169. OG Morales, JA Ramírez, DI Vivanco, M Vázquez. Surimi of fish species from the Gulf of Mexico: Evaluation of the setting phenomenon. Food Chem 75: 43-48, 2001.
170. J Yongsawatdigul, A Worratao, JW Park. Effect of endogenous transglutaminase on threadfin bream surimi gelation. J Food Sci 67:3258-63, 2002.
171. J Yongsawatdigul, JW Park. Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chem 83:409-16, 2003.
172. J Yongsawatdigul, S Sinsuwan. Aggregation and conformational changes of tilapia actomyosin as affected by calcium ion during setting. Food Hydrocolloid 21:359-367, 2007.
173. PK Binsi, BA Shamasundar. Purification and characterisation of transglutaminase from four fish species: Effect of added transglutaminase on the viscoelastic behaviour of fish mince. Food Chem 132:1922-29, 2012.
174. R Ofstad, E Grahl-Madsen, B Gundersen, K Lauritzen, T Solberg, C Solberg. Stability of cod (Gadus morhua L.) surimi processed with CaCl2 and MgCl2 added to the wash water. Int J Food Sci Tech 28(5):419-27, 1993.
175. H Saeki. Gel-forming ability and cryostability of frozen surimi processed with CaCl2 washing. Fish Sci 62(2):252-56, 1996.
176. J Wan, I Kimura, M Satake, N Seki. Effect of calcium ion concentration on the gelling properties and transglutaminase activity of walleye pollock surimi paste. Fish Sci 60(1):107-14, 1994.
177. H Saeki, F Hirata. Behavior of fish meat components during manufacture of frozen surimi through processing with CaCl2 washing. Fish Sci 60(3):335-40, 1994.
178. J Yongsawatdigul, P Piyadhammaviboon, K Singchan. Gel-forming ability of small scale mud carp unwashed and washed mince as related to endogenous proteinases and transglutaminase activities. Eur Food Res Technol 223(6):769-74, 2006.
179. A Worratao, J Yongsawatdigul. Cross-linking of actomyosin by crude tilapia (Oreochromis niloticus) transglutaminase. J Food Biochem 27: 35-51, 2003.
180. S Benjakul, W Visessanguan. Transglutaminase-mediated setting in bigeye snapper surimi. Food Res Int 36:253-66, 2003.
181. N Maruyama, H Nozawa, H, I Kimura, M Satake, N Seki. Transglutaminase-induced polymerization of a mixture of different fish myosins. Fish Sci 61(3):495-500, 1995.
182. H Nozawa, M Ezou. Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin Fish Sci 75:1445-52, 2009.
183. H Ando, M Adachi, K Umeda, A Matsuura, RM Nonaka, R Uchino, H Tanaka, M Motoki, M. Purification and characteristics of novel transglutaminase derived from microorganisms. Agric Bio Chem 53:2613-17, 1989.
184. Y Abe, K Yasunaga, S Kitakami, Y Murakami, T Ota, K Arai. Quality of kamaboko gels from walleye pollock frozen surimi of different grades on applying additive containing TGase. Nippon Suisan Gakkaishi 62(3):439-45, 1996.
185. K Yasunaga, Y Abe, M Yamazawa, K Arai, K. Heat-induced change in myosin heavy chains in salt-ground meat with a food additive containing transglutaminase. Nippon Suisan Gakkaishi 62(4):659-68, 1996.
186. T Asagami, M Ogiwara, A Wakameda, S Noguchi. Effect of microbial transglutaminase on the quality of frozen surimi made from various kinds of fish species. Fish Sci 61(2):267-72, 1995.
187. TC Lanier, IS Kang. Plasma as a source of functional food additives. International Conference of Food System Functionality (http://www.msstate.edu/org/fsfa/web-compilations.htm), Las Vegas, NV, 1997.
188. BO Hemung, ECY Li-Chan, J Yongsawatdigul. Thermal stability of fish natural actomyosin affects reactivity to cross-linking by microbial and fish transglutaminases. Food Chem 111(2):439-46, 2008.
189. S Chanarat, S Benjakul, A H-Kittikun. Comparative study on protein cross-linking and gel enhancing effect of microbial transglutaminase on surimi from different fish. J Sci Food Agric 92(4):844-52, 2012.
190. S Nakamura, M Ogawa, M Saito, S Nakai. Application of polymannosylated cystatin to surimi from roe-herring to prevent gel weakening. FEBS Lett 427:252-54, 1998.
191. AJ Whitmore, P Torley. The transglutaminase mediated setting reaction in surimi and purification of a transglutaminase from plasma. Meat Industry Research Institute of New Zealand (MIRINZ), 1992.
192. K Washizu, K Ando, S Koikeda, S Hirose, A Matsuura, H Takagi, M Motoki, K Takeuchi. Molecular cloning of the gene for microbial transglutaminase from Streptoverticillium and its expression in Streptomyces lividans. Biosci Biotech Biochem 58(1):82-87, 1994.
193. ME Surette, TA Gill, PJ LeBlanc. Biochemical basis of postmortem nucleotide catabolism in cod (Gadus morhua) and its relationship to spoilage. J Agric Food Chem 36:19-22, 1988.
194. PT Lakshmanan, PD Antony, K Gopakumar. Nucleotide degradation and quality changes in mullet (Liza corsula) and pearlspot (Etroplus suratensis) in ice and at ambient temperatures. Food Control 7(6):227-83, 1996.
195. K Gopakumar. Enzymes and enzyme products as quality indices. In: Seafood Enzymes Utilization and Influence on Postharvest Seafood Quality. NF Haard, BK Simpson, eds. New York, NY: Marcel Dekker, pp 337-364, 2000.
196. GA MacDonald, J Lelievre, NDC Wilson. Strength of gels prepared from washed and unwashed minces of hoki (Macruronus novaezelandiae) stored in ice. J Food Sci 55(4):976-78, 982, 1990.
197. RF Ablett, EG Bligh, K Spencer. Influence of freshness on quality of white hake (Urophycistenuis) surimi. Can Inst Food Sci Technol J 24(1/2):36-41, 1991.
198. S Benjakul, W Visessanguan, J Tueksubana. Changes in physico-chemical properties and gel-forming ability of lizardfish (Saurida tumbil) during post-mortem storage in ice. Food Chem 80:535-44, 2003.
199. YS Yean. The quality of surimi made from threadfin bream stored in ice for different periods. Int J Food Sci Tech 28:343-46, 1993.
200. J Yongsawatdigul, JW Park. Biochemical and conformation changes of actomyosin from threadfin bream stored in ice. J Food Sci 67:985-90, 2002.
201. SI Roura, JP Saavedra, RE Truco, M Crupkin. Conformational change in actomyosin from post-spawned hake stored on ice. J Food Sci 57(5):1109-11, 1992.
202. S Benjakul, TA Seymour, MT Morrissey, H An. Physicochemical changes in Pacific whiting muscle proteins during iced storage. J Food Sci 62(4):729-33, 1997.
203. W Sompongse, Y Itoh, S Nagamachi, A Obatake. Effect of the oxidation of SH groups on the stability of carp myosin during ice storage. Fish Sci 62:468-72, 1996.
204. T Kawashima, K Arai, T Saito. Studies on muscular proteins of fish-IX. An attempt on quantitative determination of actomyosin in frozen surimi from Alaska pollock. Bull Jap Soc Sci Fish 39:207-14, 1973.
205. T Ooizumi, K Hashimoto, J Ogura, K Arai. Quantitative aspect for protective effect of sugar and sugar alcohol against denaturation of fish myofibrils. Bull Japan Soc Sci Fish 47:901, 1981.
206. T Ooizumi, Y Nara, K Arai. Protective effect of carboxylic acids, sorbitol and Na-glutamate on heat denaturation of chub mackerel myofibrils. Bull Japan Soc Sci Fish 50(5):875, 1984.
207. M Yamaguchi, T Sekine. Sulfhydryl groups involved in the active site of myosin A adenosine triphosphatase. J Biochem 59:24-33, 1966.
208. ST Jiang, DC Hwang, CS Chen. Denaturation and changes in SH group of actomyosin from milkfish (Chanos chanos) during storage at -20°C. J Agric Food Chem 36:433-37, 1988.
209. N Katoh, H Nozaki, K Komatsu, KI Arai. A new method for evaluation of quality of frozen surimi from Alaska pollock. Relationship between myofibrillar ATPase activity and Kamaboko forming ability of frozen surimi. Nippon Suisan Gakkaishi 48(8):1027-32, 1979.
210. Y Fujii, N Nakamura, Y Ishikawa. Suitability of fresh and frozen fish to fish jelly products. In: General Report of Research of Effective Utilization of Abundantly Caught Dark Fishes. Japan: Fisheries Agency, pp. 119-27, 1978.
211. A Hashimoto, K Arai. Freshness of fish, manufacturing condition and quality of surimi. In: General Report of Research of Effective Utilization of Abundantly Caught Dark Fishes. Japan: Fisheries Agency, pp. 119-27, 1978.
212. JW Park, RW Korhonen, TC Lanier. Effects of rigor mortis on gel-forming properties of surimi and unwashed mince prepared from tilapia. J Food Sci 55:353-55, 360, 1990.
213. GA MacDonald, ND Wilson, TC Lanier. Stabilized mince: An alternative to the traditional surimi process. In: Chilling and Freezing of New Fish Products. Paris: International Institute of Refrigeration, 1990, pp. 69-76.
214. S Abe, W Weng, M Tanaka, K Limpisophon, K Osako. Effect of egg white and setting on the gelation of vinegar cured kamaboko. Nippon Suisan Gakk 75:675-700, 2009.
215. E Niwa, S Ueno, S Kanoh. Mechanism for the gelation of unheated surimi by vinegar curing. Biosci Biotechnol Biochem 56:58-61, 1992.
216. B Techaratanakrai, M Nishida, Y Igarashi, M Watanabe, E Okazaki, K Osako. Effect of setting conditions on mechanical properties of acid-induced kamaboko gel from squid Todarodes pacificus mantle muscle meat. Fish Sci 77:439-46, 2011.
217. B Techaratanakrai, E Okazaki, K Osako. Effect of organic salts on setting gels and their corresponding acids on kamaboko gels prepared from squid Todarodes pacificus mantle muscle. Fish Sci 78:707-15, 2012.
218. TC Lanier. Surimi gelation chemistry. In: Surimi and Surimi Seafood. JW Park, ed. New York: Marcel Dekker, Inc, 2000, pp. 237-266.