Effects of Casein on Gelling Properties of Surimi Paste

Fisheries Science

Volumn 62, Issue 3, 1996, Pages 421-426

  Yamashita, Tamiharu ^a   Araki, Hideyo ^b   Seki, Nobuo ^b  

^a Hiroshima Prefectural Food Technological Research Center   (Japan)

^b HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Casein; Kamaboko; Surimi; Transglutaminase

Indexed keywords

EID: 0001006050     PISSN: 09199268     EISSN: None     Source Type: Journal    
DOI: 10.2331/fishsci.62.421     Document Type: Article

References (28)

1. K. Ikura, T. Kometani, and M. Yoshikawa: Crosslinking of casein components by transglutaminase. Agric. Biol. Chem., 44, 1567-1573 (1980).
2. M. Motoki, N. Nio, and K. Takinami: Functional properties of food proteins polymerized by transglutaminase. Agric. Biol. Chem., 48, 1257-1261 (1984).
3. F. Traoré and J. C. Meunier: Cross-linking of caseins by human placental factor XIIIa. J. Agric. Food Chem., 39, 1892-1896 (1991).
4. M. Nonaka, H. Sakamoto, S. Toiguchi, H. Kawajiri, T. Soeda, and M. Motoki: Sodium caseinate and skim milk gels formed by incubation with microbial transglutaminase. J. Food Sci., 57, 1214-1218 (1992).
5. F. Traoré and J. C. Meunier: Cross-linking activity of placental FXIIIa on whey proteins. J. Agric. Food Chem., 40, 399-402 (1992).
6. C. Larré, M. Chiarello, S. Dudek, M. Chence, and J. Gueguen: Action of transglutaminase on the constitutive polypeptides of pea legumin: J. Agric. Food Chem., 41, 1816-1820 (1993).
7. 2+-independent transglutaminase. Biosci. Biotech. Biochem., 58, 864-869 (1994).
8. M.-C. Alexandre, Y. Popineau, G. Viroben, M. Chiarello, A. Lelion, and J. Gueguen: Wheat γ gliadin as substrates for bovine plasma factor XIII. J. Agric. Food Chem., 41, 2208-2214 (1993).
9. N. Seki, H. Uno, N.-H. Lee, I. Kimura, K. Toyoda, T. Fujita, and K. Arai: Transglutaminase activity in Alaska pollack muscle and surimi, and its reaction with myosin B. Nippon Suisan Gakkaishi, 56, 125-132 (1990).
10. I. Kimura, M. Sugimoto, K. Toyoda, N. Seki, K. Arai, and T. Fujita: A study on the cross-linking reaction of myosin in kamaboko suwari gels. Nippon Suisan Gakkaishi, 57, 1389-1396 (1991).
11. G. G. Kamath, T. C. Lanier, E. A. Foegeding, and D. D. Hamann: Nondisulfide covalent cross-linking of myosin heavy chain in setting of Alaska pollock and Atlantic croaker surimi. J. Food Biochem., 16, 151-172 (1992).
12. Y. Tsukamasa, K. Sato, Y. Shimizu, C. Imai, M. Sugiyama, Y. Minegishi, and M. Kawabata: ε-(γ-Glutamyl)lysine crosslink formation in sardine myofibril sol during setting at 25°C. J. Food Sci., 58, 785-787 (1993).
13. T. Suzuki: Fish and krill protein: processing technology, 1st ed., Applied Science Publishers Ltd., London, 1981, pp. 62-114.
14. T. Yamashita: Effects of commercial soybean protein and wheat gluten as subsidiary materials on physical properties of kamaboko. Nippon Shokuhin Kogyo Gakkaishi., 38, 883-890 (1991).
15. B. Yoo and C. M. Lee: Rheological relationships between surimi sol and gel as affected by ingredients. J. Food Sci., 58, 880-883 (1993).
16. L. Kurth and P. J. Rogers: Transglutaminase catalyzed cross-linking of myosin to soya protein, casein and gluten. J. Food Sci., 49, 573-576 (1984).
17. H. Kishi, H. Nozawa, and N. Seki: Reactivity of muscle transglutaminase on carp myofibrils and myosin B. Nippon Suisan Gakkaishi, 57, 1203-1210 (1991).
18. R. Takashi, K. Arai, and T. Saito: Preparation of actomyosin from carp muscle. Nippon Suisan Gakkaishi, 36, 169-172 (1970).
19. H. Fraenkel-Conrat: in "Methods in Enzymology" (ed. by S. P. Colowick and N. O. Caplan), Vol. IV, Academic Press, New York, 1957, pp. 247-269.
20. T. Numakura, N. Seki, I. Kimura, K. Toyoda, T. Fujita, K. Takama, and K. Arai: Cross-linking reaction of myosin in the fish paste during setting. Nippon Suisan Gakkaishi, 51, 1559-1565 (1985).
21. L. Loland, T. Urayama, J. W. C. Kiewiet, and H. L. Nossel: Diagnostic and genetic studies on fibrin-stabilizing factor with a new assay based on amine incorporation. J. Clin. Invest., 48, 1054-1064 (1969).
22. H. Araki and N. Seki: Comparison of reactivity of transglutaminase to various fish actomyosins. Nippon Suisan Gakkaishi, 59, 711-716 (1993).
23. K. Weber and M. Osborn: The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem., 244, 4406-4412 (1969).
24. J. Wan, J. Miura, and N. Seki: Effects of monovalent cations on cross-linking of myosin in suwari gels from walleye pollack. Nippon Suisan Gakkaishi, 58, 583-590 (1992).
25. J. Wan, I. Kimura, M. Satake, and N. Seki: Effect of calcium ion concentration on the gelling properties and transglutaminase activity of walleye pollack surimi paste. Fisheries Sci., 60, 107-113 (1994).
26. Y. Kumazawa, T. Numazawa, K. Seguro, and M. Motoki: Suppression of surimi gel setting by transglutaminase inhibitors. J. Food Sci., 60, 715-717, 726 (1995).
27. M. Yamazawa: Relationship between the swelling ability of starch granules and their kamaboko-gel reinforcing effect. Nippon Suisan Gakkaishi, 57, 971-975 (1991).
28. J. M. Kim and C. M. Lee: Effect of starch on textural properties of surimi gel. J. Food Sci., 52, 722-725 (1987).