Abstract
Pacific whiting surimi gels heated slowly in a water bath exhibited poor gel quality, while the ohmically heated gels without holding at 55°C showed more than a twofold increase in shear stress and shear strain over conventionally heated gels. Degradation of myosin and actin was minimized by ohmic heating, resulting in a continuous network structure. Ohmic heating with a rapid heating rate was an effective method for maximizing gel functionality of Pacific whiting surimi without enzyme inhibitors. In linear heating, slow heating rates increased proteolysis in Pacific whiting surimi as shown by degradation of myosin heavy chain and low shear stress and shear strain. Proteolysis of whiting surimi was decreased by the presence of beef plasma protein (BPP) to a greater extent at rapid heating rates (20 and 30°C/min) than at slow heating rates (1 and 5°C/min). Shear stress of Alaska pollock surimi gels with or without BPP increased as heating rate decreased, but shear strain was unaffected. An increase in shear stress was accompanied by an increase of cross-linked myosin heavy chain.
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References
An, H.; Weerasinghe, V.; Seymour, T.A.; Morrissey, M.T. Cathepsin degradation of Pacific whiting proteins. J. Food Sci. 1994, 59, 1013–1017, 1033.
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.
Biss, C.H.; Coombes, S.A.; Skudder, P.J. The development and application of ohmic heating for the continuous processing of particulate food stuffs. In Processing Engineering in the Food Industry; Field, R.W.; Howell J.A., Eds.; Elsevier Applied Science Publishers, Essex, U.K., 1989; pp. 17–27.
Camou, J.P.; Sebranek, J.G.; Olson, 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.
Chan, J.K.; Gill, T.A.; Paulson, A. Cross-linking of myosin heavy chains from cod, herring and silver hake during thermal setting. J. Food Sci. 1992, 57, 906–912.
Chang-Lee, M.V.; Pacheo-Aguilar, R.; Crawford, D.L.; Lampila, L. Proteolytic activity of surimi from Pacific whiting (Merluccius productus) and heat-set gel texture. J. Food Sci. 1989, 54, 1116–1119, 1124.
de Alwis, A.A.P.; Fryer, P.J. The use of direct resistance heating in the food industry. J. Food Eng. 1990, 77, 3–27.
Erickson, M.C.; Gordon, D.T.; Anglemier, A.F. Proteolytic activity in the sarcoplasmic fluid of parasitized Pacific whiting (Merluccius productus) and unparasitized true cod (Gadus macrocephalus). J. Food Sci. 1983, 48, 1315–1319.
Ferry, J.D. Protein gels. Adv. Protein Chem. 1948, 4, 1–78.
Foegeding, E.A.; Dayton, W.R.; Allen, C.E. Effect of heating rate on thermally formed myosin, fibrinogen, and albumin gels. J. Food Sci. 1986a, 57, 104–108, 112.
Foegeding, E.A.; Dayton, W.R.; Allen, C.E. Interaction of myosin-albumin and myosin-fibrinogen to form protein gels. J. Food Sci. 1986b, 57, 109–112.
Greene, D.H.; Babbitt, J. Control of muscle softening and protease parasite interactions in arrowtooth flounder (Atheresthes stomias). J. Food Sci. 1990, 55, 579–580.
Hamann, D.D.; MacDonald, G.A. Rheology and texture properties of surimi and surimi-based foods. In Surimi Technology; Lanier, T.C; Lee, C.M., Eds., Marcel Dekker, Inc., New York, 1992; pp. 429–501.
Hamann, D.D.; Amato, P.M.; Wu, M.C.; Foegeding, E.A. Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg white. J. Food Sci. 1990, 55, 665–669.
Hermansson, A.M. Aggregation and denaturation involved in gel formation. In Functionality and Protein Structure; Pour-El, A., Ed., ACS Symposium Series 92, Amer. Chem. Soc., Washington, DC, 1979; p. 81.
Kamath, G.G.; Lanier, T.C; Foegeding, E.A.; Hamann, D.D. Nondisulfide covalent cross-linking of myosin heavy chain in “setting” of Alaska pollock and Atlantic croaker surimi. J. Food Biochem. 1992, 16, 151–172
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.
Kimura, I.; Sugimoto, M.; Toyoda, K.; Seki, N.; Arai, K.; Fujita, T. A study on the cross-linking reaction of myosin in kamaboko “suwari” gels. Nippon Suisan Gakkaishi 1991, 57, 1389–1396.
MacDonald, G.A.; Stevens, J.; Lanier, T.C. Characterization of New Zealand hoki and southern blue whiting surimi compared to Alaska pollock surimi. J. Aquatic Food Product Technol. 1994, 3, 19–38.
Montejano, J.G.; Hamann, D.D.; Lanier, T.C. Thermally induced gelation of selected comminuted muscle systems: Rheological changes during processing, final strengths and microstructure. J. Food Sci. 1984, 49, 1496–1505.
Morrissey, M.T.; Wu, J.W.; Lin, D.; An, H. Protease inhibitor effects on torsion measurements and autolysis of Pacific whiting surimi. J. Food Sci. 1993, 58, 1050–1054.
Mulvihill, D.M.; Kinsella, J.E. Gelation characteristics of whey proteins and beta-lactoglobulin. Food Technol. 1987, 41(9), 102–111.
Nagahisa, E.; Nishimuro, S.; Fujita, T. Kamaboko-forming ability of the jellied meat of Pacific hake. Bull. Jap. Soc. Sci. Fish. 1981, 49, 901–906.
Niwa, E. Chemistry of surimi gelation. In Surimi Technology; Lanier, T.C.; Lee, C.M., Ed.; Marcel Dekker, Inc., New York, 1992; pp. 429–501.
Numakura, T.; Seki, N.; Kimura, I.; Toyoda, K.; Fujita, T.; Takama, K.; Arai, K. Cross-linking reaction of myosin in the fish paste during setting (suwari). Nippon Suisan Gakkaishi 1985, 53, 633–639.
Park J.W.; Yongsawatdigul, J.; Lin, T.M. Rheological behavior and potential cross-linking of Pacific whiting (Mer-liccius productus) surimi gel. J. Food Sci. 1994, 59, 773–776.
Patashnik, M.; Groninger, H.S., Jr.; Barnett, H.; Kudo, G.; Koury, B. Pacific whiting (Merluccius productus): I. Abnormal muscle texture caused by myxosporidianinduced proteolysis. Mar. Fish. Rev. 1982, 44(5), 1–12.
Parrot, D.L. Use of ohmic heating for aseptic processing of food particulates. Food Technol. 1992, 46(12), 68–72.
Porter, R.W. Use of potato inhibitor in Pacific whiting surimi. In Pacific Whiting: Harvesting, Processing, Marketing and Quality; Sylvia, G.; Morrissey, M.T., Eds.; Oregon Sea Grant Publication, Corvallis, OR, 1992; pp. 33–35.
Roussel, H.; Cheftel, J.C. Characteristics of surimi and kamaboko from sardines. Int. J. Food. Sci. Technol. 1988, 23, 601–623.
Seki, N.; Uno, H.; Lee, N.H.; Kimura, I.; Toyoda, K.; Fujita, T.; Arai, K. Transglutaminase activity in Alaska pollock muscle and surimi, and its reaction with myosin B. Nippon Suisan Gakkaishi 1990, 56, 125–132.
Seymour, T.A.; Morrissey, M.T.; Peters, M.Y.; An, H. Purification and characterization of Pacific whiting proteases. J. Agric. Food Chem. 1994, 42, 2421–2427.
Toyohara, H. and Shimizu, Y. Relation between the modori phenomenon and myosin heavy chain breakdown in threadfin-bream gel. Agric. Biol. Chem. 1988, 52, 255–257.
Toyohara, H.; Kineshita, M.; Kimura, I.; Satake, M.; Sakaguchi, M. Cathepsin LO like protease in Pacific hake muscle infected by myxosporidian parasites. Nippon Suisan Gakkaishi 1993, 59, 1101–1107.
Yongsawatdigul, J. Textural and Electrical Properties of Pacific Whiting Surimi under Ohmic Heating, Ph.D. Thesis, Oregon State University, Corvallis, OR, 1996.
Yongsawatdigul, J.; Park, J.W. Linear heating rate affects gelation of Alaska pollock and Pacific whiting surimi. J. Food Sci. 1996, 61, 149–153.
Yongsawatdigul, J.; Park, J.W.; Kolbe, E.; Abudagga, Y; Morrissey, M.T. Ohmic heating maximizes gel functionality of Pacific whiting surimi. J. Food Sci. 1995, 60, 10–14.
Ziegler, G.R.; Acton, J.C. Mechanisms of gel formation by proteins of muscle tissue. Food Technol. 1984, 38(5), 77–82.
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Park, J.W., Yongsawatdigul, J., Kolbe, E. (1998). Proteolysis and Gelation of Fish Proteins under Ohmic Heating. In: Shahidi, F., Ho, CT., van Chuyen, N. (eds) Process-Induced Chemical Changes in Food. Advances in Experimental Medicine and Biology, vol 434. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1925-0_3
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