Effect of high-temperature setting on gelling characteristic of surimi from some tropical fish

International Journal of Food Science and Technology

Volumn 39, Issue 6, 2004, Pages 671-680

  Benjakul, Soottawat ^a   Visessanguan, Wonnop ^b   Chantarasuwan, Chakkawat ^a  

^a PRINCE OF SONGKLA UNIVERSITY   (Thailand)

^b NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

Author keywords

Cross linking; Gelation; Protein; Solubility; Transglutaminase

Indexed keywords

COVALENT BONDS; FISH SPECIES; GEL STRENGTH; MYOFIBRILLAR PROTEINS;

CATALYSIS; CROSSLINKING; DEFORMATION; GELATION; GELS; PROTEINS; TEXTURES;

FISHERIES;

ALECTIS CILIARIS; HYPEROGLYPHE POROSA; LUTJANUS LUTJANUS; MACROPHTHALMUS; NEMIPTERUS; NEMIPTERUS BIPUNCTATUS; PRIACANTHUS; PRIACANTHUS TAYENUS; SPHYRAENA JELLO;

EID: 2942545081     PISSN: 09505423     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2004.00825.x     Document Type: Article

References (36)

1. Alvarez, C. & Tejada, M. (1997). Influence of texture of suwari gels on kamaboko gels made from sardine (Sardina poilchardus) surimi. Journal of the Science of Food and Agriculture, 79, 472-480.
2. An, H., Peters, M.Y. & Seymour, T.A. (1996). Roles of endogenous enzymes in surimi gelation. Trends in Food Science and Technology, 7, 321-326.
3. Ando, M., Tsukamasa, Y. & Makinodan, Y. (1998). Identification of 170 k component which appears in the setting process of surimi gel. Fisheries Science, 64, 497-498.
4. Araki, H. & Seki, N. (1993). Comparison of reactivity of transglutaminase to various fish actomyosin. Nippon Suisan Gakkaishi, 59, 711-716.
5. Benjakul, S., Visessanguan, W., Ishizaki, S. & Tanaka, M. (2001a). Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus. Journal of Food Science, 66, 1311-1318.
6. Benjakul, S., Visessanguan, W. & Srivilai, C. (2001b). Porcine plasma proteins as gel enhancer in bigeye snapper (Priacanthus tayenus) surimi. Journal of Food Biochemistry, 25, 285-305.
7. Benjakul, S., Visessanguan, W. & Chantarasuwan, C. (2003). Effect of medium temperature setting on gelling characteristic of surimi from some tropical fish. Food Chemistry, 82, 567-574.
8. Chan, J.K., Gill, T.A. & Paulson, A.T. (1992). Cross-linking of myosin heavy chains from cod, herring and silver hake during thermal setting, Journal of Food Science, 57, 906-912.
9. Chawla, S.P., Venugopol, V. & Nair, P.M. (1996). Gelation of proteins from washed muscle of threadfin bream (Nemipterus japonicus) under mild acidic conditions. Journal of Food Science, 54, 362-366.
10. Folk, J.E. (1983). Mechanism and basis for specificity of transglutaminase-catalyzed e-(y-glutamyl) lysine bond formation. Advances in Enzymology, 54, 1-56.
11. Folk, J.E. & Chung, S.I. (1973). Molecular and catalytic properties of transglutaminase. Advances in Enzymology, 38, 109-191.
12. Jiang, S.T. (2000). Enzymes and their effects on seafood texture. In: Seafood Enzymes: Utilization and Influence on Postharvest Seafood Quality (edited by N.F. Haard & B.K. Simpson). Pp. 411-450. New York: Marcel Dekker, Inc.
13. Kamath, G.G., Lanier, T.C., Foegeding, E.A. & Hamann, D.D. (1992). Nondisulfide covalent cross-linking of myosin heavy chain in 'setting' of Alaska pollock and Atlantic croaker surimi. Journal of Food Biochemistry, 16, 151-172.
14. Kim, B.Y., Hamann, D.D., Lanier, T.C. & Wu, M.C. (1986). Effect of freeze-thaw abuse on the viscosity and gel-forming properties of surimi from two species. Journal of Food Science, 51, 951-956.
15. Kimura, I.M., Sugimoto, M., Toyoda, K., Seki, N., Arai, K. & Fujita, T. (1991). A study on the cross-links reaction of myosin in kamaboko 'suwari' gels. Nippon Suisan Gakkaishi, 57, 1386-1396.
16. Kinoshita, M., Toyohara, H. & Shimizu, Y. (1990). Diverse distribution of four distinct types of modori (gel degradation)-inducing proteinases among fish species. Nippon Suisan Gakkaishi, 56, 1485-1492.
17. Kishi, H., Nozawa, H. & Seki, N. (1991). Reactivity of muscle transglutaminase on carp myofibrils and myosin B. Nippon Suisan Gakkaishi, 57, 1203-1210.
18. Kumazawa, Y., Numazawa, T., Seguro, K. & Motoki, M. (1995). Suppression of surimi gel setting by transglutaminase inhibitors. Journal of Food Science, 60, 715-717.
19. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature, 227, 680-685.
20. Lanier, T.C. (1992). Measurement of surimi composition and functional properties. In: Surimi Technology (edited by T.C. Lanier & C.M. Lee). Pp. 123-166. New York: Marcel Dekker, Inc.
21. Lanier, T.C. (2000). Surimi gelation chemistry. In: Surimi and Surimi Seafood (edited by J.W. Park). Pp. 237-265. New York: Marcel Dekker, Inc.
22. Lanier, T.C., Lin, T.S., Hamann, D.D. & Thomas, F.B. (1981). Effect of alkaline protease in minced fish on texture of heat-induced gel. Journal of Food Science, 46, 1643-1645.
23. Lee, N.H., Seki, N., Kato, N., Nakagawa, N., Terui, S. & Arai, K. (1990a). Gel forming ability and cross-linking ability of myosin heavy chain in salted meat paste from threadfin bream. Nippon Suisan Gakkaishi, 56, 329-336.
24. Lee, N.H., Seki, N., Kato, N., Nakagawa, N., Terui, S. & Arai, K. (1990b). Changes in myosin heavy chain and gel forming ability of salt-ground meat from hoki. Nippon Suisan Gakkaishi, 56, 2093-2101.
25. Lowry, O.H., Rosebrough, N.J., Farr, A.L. & Randall, R.J. (1951). Protein measurement with Folin phenol reagent. The Journal of Biological Chemistry, 193, 256-275.
26. Morales, O.G., Ramirez, J.A., Vivanco, D.I. & Vazquez, M. (2001). Surimi of fish species from the gulf of Mexico: evaluation of the setting phenomenon. Food Chemistry, 75, 43-48.
27. Morrissey, M.T. & Tan, S.M. (2000). World resources for surimi. In: Surimi and Surimi Seafood (edited by J.W. Park). Pp. 1-22. New York: Marcel Dekker, Inc.
28. Morrissey, M.T., Wu, J.W., Lin, D. & An, H. (1993). Protease inhibitor effects on torsion measurements and autolysis of Pacific whiting surimi. Journal of Food Science, 58, 1054-1059.
29. Niwa, E. (1992). Chemistry of surimi gelation. In: Surimi Technology (edited by T.C. Lanier & C.M. Lee). Pp. 389428. New York: Marcel Dekker, Inc.
30. Numakura, T., Seki, N., Kimura, I. et al. (1985). Crosslinking reaction of myosin in the fish paste during setting (suwari). Bulletin of the Japanese Society of Scientific Fisheries, 51, 1559-1565.
31. Robinson, H.W., & Hodgen, C.G. (1940). The biuret reaction in the determination of serum protein. I. A study of the condition necessary for the production of the stable color which bears a quantitative relationship to the protein concentration. The Journal of Biological Chemistry, 135, 707-725.
32. Sano, T., Noguchi, S.F., Marsumoto, J.J. & Tsuchiya, T. (1990). Thermal gelation characteristics of myosin subfragments. Journal of Food Science, 55, 55-58.
33. Seki, N., Uno, H., Lee, N.H. et al. (1990). Transglutaminase activity in Alaska pollack muscle and surimi and its reaction with myosin B. Nippon Suisan Gakkaishi, 56, 125-132.
34. Shimizu, Y., Machida, R. & Takanemi, S. (1981). Species variations in the gel forming characteristics of fish meat paste. Nippon Suisan Gakkaishi, 47, 95-104.
35. Steel, R.G.D. & Torrie, J.H. (1980). Pp. 633.Principles and Procedures of Statistics; a Biometrical Approach, 2nd edn. New York: McGraw-Hill.
36. Takeda, H. & Seki,-N. (1996). Enzyme-catalyzed crosslinking and degradation of myosin heavy chain in walleye pollack surimi paste during setting. Fisheries Science, 62, 462-467.