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Gelation Properties of Fish Proteins under Ohmic Heating

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Quality Attributes of Muscle Foods

Abstract

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

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References

  • AbuDagga, Y.; Kolbe, E. Thermophysical properties of surimi paste at cooking temperature. J. Food Eng 1997,32(3), 325–337

    Article  Google Scholar 

  • 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, 640–646

    Article  CAS  Google Scholar 

  • Barbut, S.; Mittal, G.S. Effect of heating rate on meat batter stability texture and gelation. J. Food Sci 1990, 55, 334–337

    Article  Google Scholar 

  • 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, 850–854

    Article  CAS  Google Scholar 

  • Chan, J.K.; Gill, T.A.; Paulson, A.T. The dynamics of thermal denaturation of fish myosins. Food Res. Int 1992, 25,117–123

    Article  CAS  Google Scholar 

  • 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, 1069

    Article  CAS  Google Scholar 

  • Datta, A.K. and Hu, W. optimization of quality in microwave heating. Food Technol 1992, 46(12), 53–56

    Google Scholar 

  • de Alwis, A.A.P; Fryer, P.J. The use of direct resistance heating in the food industry. J. Food Eng 1990, 11,3–27

    Article  Google Scholar 

  • de Alwis, A.A.P. and Fryer, P.J. Operability of the ohmic heating process: electrical conductivity effects. J. Food Eng 1992, 15,21–48

    Article  Google Scholar 

  • Ferry, J.D. Protein gels. Adv. Protein Chem 1948, 4, 1–78

    Article  CAS  Google Scholar 

  • Foegeding, E.A. Functional properties of turkey salt-soluble proteins. J. Food Sci 1987, 52, 1495–1499

    Article  CAS  Google Scholar 

  • 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, 2553–2562

    Article  CAS  Google Scholar 

  • Goodno, C.C.; Swenson, C.A. Thermal transition of myosin and its helical fragments. 11. Solvent-induced variations in conformational stability. Biochem 1975, 14, 873–877

    Article  CAS  Google Scholar 

  • 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, 81

    Google Scholar 

  • 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, 777–780

    Article  Google Scholar 

  • 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, 151–172

    Article  CAS  Google Scholar 

  • 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. 1987

    Google Scholar 

  • Klesk, K.; Yongsawatdigul, J.; Park, J.W.; Virulhakul, P.; Viratchakul, S. Oregon State University, unpublished data. 1998

    Google Scholar 

  • Lanier, T.C. Chemistry of surimi. In Surimi and Surimi Seafood Editor, Park, J.W. OSU Surimi Technology School, Astoria, OR, 1997, ppl-18

    Google Scholar 

  • 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 press

    Google Scholar 

  • 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, 1916–1920

    Article  CAS  Google Scholar 

  • Mulvihill, D.M.; Kinsella, J.E. Gelation characteristics of whey proteins and beta-lactoglobulin. Food Technol 1987, 41(9), 102—111

    Google Scholar 

  • Niwa, E. Chemistry of surimi gelation. In Surimi Technology; Lanier, T.C.; Lee, C.M. Eds. Marcel Dekker, New York, 1992, p.429–501

    Google Scholar 

  • Park, J.W. Manufacturing of surimi seafood. In Surimi and Surimi Seafood. Editor, Park, J.W. OSU Surimi Technology School, Astoria, OR, 1997, pp254–295

    Google Scholar 

  • 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, 395–404

    CAS  Google Scholar 

  • Park, J.W.; Yongsawatdigul, J.; Lin, T.M. Rheological behavior and potential cross-linking of Pacific whiting surimi. J. Food Sci 1994, 59, 773–776

    Article  CAS  Google Scholar 

  • 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, 70

    Article  Google Scholar 

  • Sano, T.; Noguchi, S.F.; Matsumoto, J.J.;Tsuchiya, T. Thermal gelation characteristics of mysoin subfragments. J. Food Sci 1990b, 55, 55–58, 70

    Article  Google Scholar 

  • Sastry, S.K. and Palaniappan, S. Ohmic heating of liquid-particle mixtures. Food Technol 1992, 46(12), 64–67

    Google Scholar 

  • 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, 305–311

    Article  CAS  Google Scholar 

  • 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, 2421–2427

    Article  CAS  Google Scholar 

  • Shiba, M. Properties of kamaboko gels prepared by using a new heating apparatus. Nippon Suisan Gakkaishi 1992, 58, 895–901

    Article  Google Scholar 

  • Shiba, M. Quality of kamaboko from vacuum-treated salt ground meat from several fish by applying joui heat. Nippon Suisan Gakkaishi 1993, 59, 1007–1011

    Article  Google Scholar 

  • Shiba, M.; Numakura, T. Quality of heated gel from walleye polloack surimi by applying joule heat. Nippon Suisan Gakkaishi 1992, 58, 903–907

    Article  Google Scholar 

  • Taguchi, T.; Ishizaka, M.; Tanaka, M.; Nagashima, Y.; Amano, K. ProteinOprotein interaction of fish myosin fragment. J. Food Sci 1987, 52, 1103–1104

    Article  CAS  Google Scholar 

  • 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, 1998

    Google Scholar 

  • Wright, D.J.; Leach, I.B.; Wilding, J. Differential scanning calorimetric studies of muscle and its constituent proteins. J. Sci. Food Agric 1977, 28, 557–564

    Article  CAS  Google Scholar 

  • 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, 1997

    Google Scholar 

  • Wu, J.Q.; Hamann, D.D.; Foegeding, E.A. Myosin gelation kinetic study based on rheological measurement. J. Agric. Food Chem 1991, 39, 229–236

    Article  CAS  Google Scholar 

  • Yongsawatdigul, J.; Park, J.W. Linear heating rate affects gelation of alska pollock and Pacific whiting surimi. J. Food Sci 1996, 61, 149–153

    Article  CAS  Google Scholar 

  • 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, 1–5

    Article  Google Scholar 

  • Yoon, W.B. and Park, J.W. Oregon State University, unpublished data. 1996

    Google Scholar 

  • Zhao, Y.; Kolbe, E.; Flugstad, B. Oregon State University, unpublished data. 1997

    Google Scholar 

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Park, J.W., Yongsawatdigul, J. (1999). Gelation Properties of Fish Proteins under Ohmic Heating. In: Xiong, Y.L., Chi-Tang, H., Shahidi, F. (eds) Quality Attributes of Muscle Foods. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4731-0_28

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  • DOI: https://doi.org/10.1007/978-1-4615-4731-0_28

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7144-1

  • Online ISBN: 978-1-4615-4731-0

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