Gelation Properties of Fish Proteins under Ohmic Heating

  • Jae W. Park
  • Jirawat Yongsawatdigul


One of the most important functional properties of fish protein is its gel-forming ability. It is essential to understand both intrinsic and extrinsic factors affecting fish protein gelation in order to obtain a finished product with desirable texture. Among these factors, endogenous enzymes greatly contribute to structural changes of fish myofibrillar proteins negatively (by protease) or positively (by transglutaminase). Activity of these enzymes can be controlled using a proper heating method. Recently ohmic heating was introduced for food application. Its unique characteristics, rapid and uniform heating, were evaluated as a promising means for various fish protein gelation. The following discussion will focus on general principles of ohmic heating, gelation of fish proteins, linear heating patterns of ohmic heating, and gelation properties of fish proteins under ohmic heating


Myosin Heavy Chain Myofibrillar Protein Ohmic Heating Fish Protein Gelation Property 
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  1. AbuDagga, Y.; Kolbe, E. Thermophysical properties of surimi paste at cooking temperature. J. Food Eng 1997,32(3), 325–337CrossRefGoogle Scholar
  2. Arntfield, S.D.; Murray, E.D. Heating rate affects thermal properties and network formation for vicilin and ovalbumin at various pH values. J. Food Sci 1992, 57, 640–646CrossRefGoogle Scholar
  3. Barbut, S.; Mittal, G.S. Effect of heating rate on meat batter stability texture and gelation. J. Food Sci 1990, 55, 334–337CrossRefGoogle Scholar
  4. Camou, J.P.; Sebranek, J.G.; Oslon, D.G. Effect of heating rate and protein concentration on gel strength and water loss of muscle protein gels. J. Food Sci 1989, 54, 850–854CrossRefGoogle Scholar
  5. Chan, J.K.; Gill, T.A.; Paulson, A.T. The dynamics of thermal denaturation of fish myosins. Food Res. Int 1992, 25,117–123CrossRefGoogle Scholar
  6. Chan, J.K.; Gill, T.A.; Paulson, A.T. Thermal aggregation of mysoin subfragments from cod and herring. J. Food Sci 1993, 58, 1057–1061, 1069CrossRefGoogle Scholar
  7. Datta, A.K. and Hu, W. optimization of quality in microwave heating. Food Technol 1992, 46(12), 53–56Google Scholar
  8. de Alwis, A.A.P; Fryer, P.J. The use of direct resistance heating in the food industry. J. Food Eng 1990, 11,3–27CrossRefGoogle Scholar
  9. de Alwis, A.A.P. and Fryer, P.J. Operability of the ohmic heating process: electrical conductivity effects. J. Food Eng 1992, 15,21–48CrossRefGoogle Scholar
  10. Ferry, J.D. Protein gels. Adv. Protein Chem 1948, 4, 1–78CrossRefGoogle Scholar
  11. Foegeding, E.A. Functional properties of turkey salt-soluble proteins. J. Food Sci 1987, 52, 1495–1499CrossRefGoogle Scholar
  12. Gill, T.A.; Conway, J.T. Thermal aggregation of cod muscle proteins usingl-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a zero-length cross-linker. Agrie. Biol. Chem 1989, 53, 2553–2562CrossRefGoogle Scholar
  13. Goodno, C.C.; Swenson, C.A. Thermal transition of myosin and its helical fragments. 11. Solvent-induced variations in conformational stability. Biochem 1975, 14, 873–877CrossRefGoogle Scholar
  14. Hermansson, A.M. Aggregation and denaturation involved in gel formation. In Functionality and Protein Structure A. Pour-El, Ed. ACS Symp. Ser. 92. Amer. Chem. Soc., Washington, D.C., 1979, 92, 81Google Scholar
  15. Howe, J.R.; Hamann, D.D.; Lanier, T.C.; Park, J.W. Fracture of Alaska pollock gels in water: Effects of minced muscle processing and test temperature J. Food Sci 1994, 59, 777–780CrossRefGoogle Scholar
  16. Kamath, G.G.; Lanier, T.C.; Foegeding, E.A.; Hamann, D.D. Non-disulfide covalent cross-linking of myosin heavy chain in “setting” of Alaska pollock and Atlantic croaker surimi. J. Food Biochem 1992, 16, 151–172CrossRefGoogle Scholar
  17. Kim, B.Y. Rheological Investigation of Gel Structure Formation by Fish Proteins During Setting and Heat Processing, Ph.D. Thesis, North Carolina State University, Raleigh, NC. 1987Google Scholar
  18. Klesk, K.; Yongsawatdigul, J.; Park, J.W.; Virulhakul, P.; Viratchakul, S. Oregon State University, unpublished data. 1998Google Scholar
  19. Lanier, T.C. Chemistry of surimi. In Surimi and Surimi Seafood Editor, Park, J.W. OSU Surimi Technology School, Astoria, OR, 1997, ppl-18Google Scholar
  20. Lee, N.G.; Park, J.W. Effects of calcium compounds on gelation properties of Pacific whiting and Alaska pollock surimi. J. Food Sci 1998, in pressGoogle Scholar
  21. Liu, Y.M.; Lin, T.S.; Lanier, T.C. Thermal denaturation and aggregation of actomyosin and surimi prepared from Atlantic croaker. J. Food Sci 1982, 47, 1916–1920CrossRefGoogle Scholar
  22. Mulvihill, D.M.; Kinsella, J.E. Gelation characteristics of whey proteins and beta-lactoglobulin. Food Technol 1987, 41(9), 102—111Google Scholar
  23. Niwa, E. Chemistry of surimi gelation. In Surimi Technology; Lanier, T.C.; Lee, C.M. Eds. Marcel Dekker, New York, 1992, p.429–501Google Scholar
  24. Park, J.W. Manufacturing of surimi seafood. In Surimi and Surimi Seafood. Editor, Park, J.W. OSU Surimi Technology School, Astoria, OR, 1997, pp254–295Google Scholar
  25. Park, J.W.; Lanier, T.C. Effects of salt and sucrose addition on the thermal denaturation and aggregation of water-leached fish muscle. J. Food Biochem J. Food Biochem 1990, 14, 395–404Google Scholar
  26. Park, J.W.; Yongsawatdigul, J.; Lin, T.M. Rheological behavior and potential cross-linking of Pacific whiting surimi. J. Food Sci 1994, 59, 773–776CrossRefGoogle Scholar
  27. Sano, T.; Noguchi, S.F.; Matsumoto, J.J.; Tsuchiya, T. Effect of ionic strength on dynamic viscoelectric behavior of myosin during thermal gelation. J. Food Sci 1990a, 55, 51–54, 70CrossRefGoogle Scholar
  28. Sano, T.; Noguchi, S.F.; Matsumoto, J.J.;Tsuchiya, T. Thermal gelation characteristics of mysoin subfragments. J. Food Sci 1990b, 55, 55–58, 70CrossRefGoogle Scholar
  29. Sastry, S.K. and Palaniappan, S. Ohmic heating of liquid-particle mixtures. Food Technol 1992, 46(12), 64–67Google Scholar
  30. Seguro, K.; Kumazawa, Y.; Ohtsuka, T.; Toiguchi, S.; Motoki, M. Microbial transglutaminase and c-(y-glutamyl)lysine crosslink effects on elastic properties of kamaboko gels. J. Food Sci 1995, 60, 305–311CrossRefGoogle Scholar
  31. Seymour, T.A.; Morrissey, T.M.; Peters, M.Y.,; An, H. Purification and characterization of Pacific whiting protease. J. Food Agric. Food Chem 1994, 42, 2421–2427CrossRefGoogle Scholar
  32. Shiba, M. Properties of kamaboko gels prepared by using a new heating apparatus. Nippon Suisan Gakkaishi 1992, 58, 895–901CrossRefGoogle Scholar
  33. Shiba, M. Quality of kamaboko from vacuum-treated salt ground meat from several fish by applying joui heat. Nippon Suisan Gakkaishi 1993, 59, 1007–1011CrossRefGoogle Scholar
  34. Shiba, M.; Numakura, T. Quality of heated gel from walleye polloack surimi by applying joule heat. Nippon Suisan Gakkaishi 1992, 58, 903–907CrossRefGoogle Scholar
  35. Taguchi, T.; Ishizaka, M.; Tanaka, M.; Nagashima, Y.; Amano, K. ProteinOprotein interaction of fish myosin fragment. J. Food Sci 1987, 52, 1103–1104CrossRefGoogle Scholar
  36. Wang, S.L.; Lanier, T.C. Effects of endogenous, fungal, and microbial transglutaminase in pollock surimi gelation.Presented at the Annual Meeting of Institute of Food Technologists, Atlanta, GA. June 20–24, 1998Google Scholar
  37. Wright, D.J.; Leach, I.B.; Wilding, J. Differential scanning calorimetric studies of muscle and its constituent proteins. J. Sci. Food Agric 1977, 28, 557–564CrossRefGoogle Scholar
  38. Wu, H.; Kolbe, E.; Park, J.W.; Flugstad, B.; Yongsawatdigul, J. Ohmic heating of surimi paste at frequencies to 200 kHz. Abstract #35B-7. Presented at the Annual Meeting of Institute of Food Technologists, Orlando, FL. June 14–18, 1997Google Scholar
  39. Wu, J.Q.; Hamann, D.D.; Foegeding, E.A. Myosin gelation kinetic study based on rheological measurement. J. Agric. Food Chem 1991, 39, 229–236CrossRefGoogle Scholar
  40. Yongsawatdigul, J.; Park, J.W. Linear heating rate affects gelation of alska pollock and Pacific whiting surimi. J. Food Sci 1996, 61, 149–153CrossRefGoogle Scholar
  41. Yonsawatdigul, J.; Park, J.W.; Kolbe, E.; AbuDagga, Y.; Morrissesy, M.T. ohmic heating maximizes gel functionality of Pacific whiting surimi. J. Food Sci 1995, 60, 1–5CrossRefGoogle Scholar
  42. Yoon, W.B. and Park, J.W. Oregon State University, unpublished data. 1996Google Scholar
  43. Zhao, Y.; Kolbe, E.; Flugstad, B. Oregon State University, unpublished data. 1997Google Scholar

Copyright information

© Springer Science+Business Media New York 1999

Authors and Affiliations

  • Jae W. Park
    • 1
  • Jirawat Yongsawatdigul
    • 2
  1. 1.Seafood Laboratory and Department of Food Science and TechnologyOregon State UniversityAstoriaUSA
  2. 2.School of Food TechnologySuranaree University of TechnologyNakhon RatchasimaThailand

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