Abstract
Salted pastes of surimi, a myofibrillar concentrate of fish muscle, gel at pressures near 300 MPa. High pressure processing has been thought to induce de-naturation and gelation of myofibrillar proteins mainly by disruption of protein intramolecular hydrophobic interactions which subsequently reform intennolecularly. We have shown that pressure-induced surimi gels evidence disulfide bonding as well. Endogenous transglutaminase (TGase) evidently survives the pressure treatment, and subsequent TGase-mediated setting of Alaska pollock surimi pastes at 25°C results in very strong gels as compared to those prepared without prior pressurization. High pressure during freezing or thawing greatly accelerates these operations and can reduce ice crystal size and associated tissue damage. Yet pressure treatment can destabilize proteins which might lower fish quality. Infusion of certain carbohydrates into muscle prior to pressure-assisted freezing/thawing can achieve both baroprotection and cryoprotection of the muscle proteins. Pressure treatment has not proven useful for inactivation of proteolytic enzymes that degrade fish quality.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Ashie, I.N.A. Application of high hydrostatic pressure and oc2-macroglobulin to control postharvest seafood texture deterioration. Ph.D. thesis, McGill Univ., Montreal Canada, 1995, 239 pp.
Ashie, I.; Lanier, T.C. Baroprotection of fish proteins by sugars and polyols. Abst. Intl. Conf. Food Sci. Technol, Fine Particle Soc., Chicago, IL, 1996.
Berg Y.N.; Lebedeva, N.A.; Markina, E.A.; Ivanov, I.I. The effect of high pressure on some properties of myosin. Biokhimiya 1965, 30, 277–281.
Buttkus, H. The sulfhydryl content of rabbit and trout myosins in relation to protein stability. Can. J. Biochem. 1971, 49, 97–107.
Carvajal, P.A.; Lanier, T.C. Cryoprotection of intact meats by carbohydrate infusion. J. Food Sci. 1997 (in press).
Carvajal, P.A.; MacDonald, G.A.; Lanier, T.C. Cryostabilization of muscle proteins. Cryobiology 1997 (in press)
Cheftel, J.-C. Effects of high hydrostatic pressure on food constituents: an overview. In High Pressure and Biotechnology; Balny, C; Hayashi, R.; Heremans, K.; Masson, P., Eds.; Colloque INSERM, John Libbey Eurotext Ltd., 1992; Vol. 224, pp 195–209.
Chung, Y.C.; Gebrehiwot, A.; Farkas, D.R; Morrissey, M.T. Gelation of surimi by high hydrostatic pressure. J. Food Sci. 1994, 59, 523–524, 525
Connell, J. J. The relative stabilities of the skeletal muscle myosins of some animals. Biochem. J. 1961, 80, 503–509.
Demazeau, G. The demystification of the pressure parameter for industrial applications. In High Pressure and Biotechnology; Balny, C.; Hayashi, R.; Heremans, K.; Masson, P., Eds.; Colloque INSERM, John Libbey Eurotext Ltd., 1992; Vol. 224, pp 481–491.
Deplace, G., Mertens, B. The commercial application of high pressure technology in the food processing industry. In High Pressure and Biotechnology; Balny, C; Hayashi, R.; Heremans, K.; Masson, P., Eds.; Colloque INSERM, John Libbey Eurotext Ltd., 1992, Vol. 224, pp 469–479.
Deuchi, T.; Hayashi, R. High pressure treatments at subzero temperature: application to preservation, rapid freezing and rapid thawing of foods. In High Pressure and Biotechnology; Balny, C; Hayashi, R.; Heremans, K.; Masson, P., Eds.; Colloque INSERM, John Libbey Eurotext Ltd., 1992; Vol. 224, pp 353–355.
Dumay, E.M.; Kalichevsky, M.T.; Cheftel, J.C. High-pressure unfolding and aggregation of lactoglobulin and the baroprotective effects of sucrose. J. Agric. Food Chem. 1994, 42, 1861–1868.
Farr, D. High pressure technology in the food industry. Trends in Food Sci. Technol. 1990, 1, 14–16.
Fennema, O.R. Water and ice. In Low-Temperature Preservation of Foods and Living Matter; Fennema, O.R.; Powrie, W.D.; Marth, E.H., Eds.; Marcel Dekker, Inc., N.Y., 1973; pp 3–78.
Fennema, O.R. Water and ice. In Food Chemistry, 3rd edition; Fennema, O.R., Ed.; Marcel Dekker, Inc., N.Y., 1996; pp 17–94.
Gilleland, M.G.; Lanier, T.C. Investigation into the mechanism of gelation of surimi pastes treated by high isostatic pressures. Food Sci. 1997, 4, 1–5
Hashimoto, A.; Kobayashi, A; Arai, K. Thermostability of fish myofibrillar Ca-ATPase and adaption to environmental temperature. Bull. Japan. Soc. Sci. Fish. 1982, 48, 671–684.
Heremans, L.; Heremans, K. Raman spectroscopic study of the changes in secondary structure of chymotrypsin: Effect of pH and pressure on the salt bridge. Biochim. Biophys. Acta. 1989, 999, 192–197.
Heremans, K. Pressure behavior of proteins: infrared studies in the diamond anvil cell. Abst. Int. Conf. High Press. Biosci. Biotechnol., Kyoto, Japan, 1995.
Homma, N.; Ikeuchi, Y.; Suzuki, A. Effects of high pressure treatment on the proteolytic enzymes in meat. Meat Sci. 1994, 55, 219–228.
Ikeuchi, Y; Tanji, H.; Kim, K.; Takeda, N.; Kakimoto, T.; Suzuki, A. Dynamic rheological behavior and biochemical properties of pressurized actomyosin. Abst. Int. Conf High Press. Biosci. Biotechnol. Kyoto, Japan, 1995.
Jiang, S.T.; Hwang, B.O.; Tsao, C.T. Protein denaturation and changes in nucleotides of fish muscle during frozen storage. J. Agric. Food Chem. 1987a, 35, 22–27.
Jiang, S.T.; Hwang, B.O.; Tsao, C.T. Effect of adenosine-nucleotides and their derivatives on denaturation of myofibrillar proteins in vitro during frozen storage at-20°C. J. Food Sci. 1987b, 52, 117–123.
Joseph, D.; Lanier, T.; Hamann, D. Temperature and pH affect transglutaminase-catalyzed setting of crude fish actomyosin. J. Food Sci. 1994, 59(5), 1019–1027.
Kalichevsky, M.T.; Knorr, D.; Lilliford, P.J. Potential food applications of high-pressure effects on ice-water transitions. Trends in Food Sci. & Technol. 1995, 6, 253–259.
Kamath, G.; Lanier, T.; Foegedin, E.; Hamann, 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.
Kumazawa, Y; Numazawa, T.; Motoki, M.; Takamura, M. Participation of transglutaminase in the manufacturing process of “kamaboko”. Abstr. Ann. Meet., Inst. Food Technol, Chicago, IL, 1993.
Lanier, T. C. Functional properties of surimi. Food Technol. 1986, 40, 107–124.
Lee, H. Lanier, T. The role of covalent crosslinking in the texturizing of muscle protein sols. J. Muscle Foods 1995, 6, 125–138.
Lee, H.G.; Lanier, T.C; Hamann, D.D.; Knopp, J. A. Investigation of the role of transglutaminase in the low temperature gelation of fish protein sols. J. Food Sci. 1997, 62, 20–24.
Levine, H.; Slade, L. A polymer physico-chemical approach to the study of commercial starch hydrolysis products (SEPs). Carbohydr. Polym. 1986, 6, 213.
Levine, H.; Slade, L. A food polymer science approach to the practice of cryostabilization technology. Comments Agric. Food Chem. 1988, 1, 315–395.
Loomis, S.H.; Carpenter, T.J.; Anchordoguy, T.J.; Crowe, J.H., Branchini, B.R. Cryoprotective capacity of end products of anaerobic metabolism. J. Exp. Zoo. 1989, 252, 9–15.
Love, R. M. New factors involved in the denaturation of frozen cod muscle protein. J. Food Sci. 1962, 27, 544–550.
Love, R. M. The Food Fishes: Their Intrinsic Variation and Practical Implications. Van Nostrand Reinhold, New York, 1988; pp. 130–140.
Low, P.; Somero, G. Pressure effects on enzyme structure and function in vitro and under simulated in vivo conditions. Comp. Biochem. Physiol. 1975, 52B, 67–74.
Martino, M.N.; Zaritzky, N.E. Ice crystal size modifications during frozen beef storage. J. Food Sci. 1988, 53, 1631–1637.
Murakami, T.; Kimura, I.; Yamagishi, T.; Yamashita, M.; Sugimoto, M.; Satake, M. Thawing of frozen fish by hydrostatic pressure. In High Pressure and Biotechnology; Balny, C; Hayashi, R.; Heremans K.; Masson, P.; Eds.; Colloque INSERM, John Libbey Eurotext Ltd., 1992; Vol. 224, pp 329–331.
Nielsen, P.M. Reactions and potential industrial applications of transglutaminase. Review of literature and patents. Food Biotechnology 1995, 9, 119–156.
Ohmori, T.; Shigehiza, T.; Taji, S.; Hayashi, R. Effect of high pressure on the protease activities in meat. Agric. Biol. Chem. 1991, 55, 357–361.
Ohshima, T.; Ushio, H.; Koizumi, C. High-pressure processing of fish and fish products. Trends Food Sci. Technol. 1993, 4(11), 1370–375.
Okamoto, M.; Kawamura, Y; Hayashi, R. Application of high pressure to food processing: Textural comparison of pressure and heat induced gels of food proteins. Agric. Biol. Chem. 1990, 54(1), 183–189.
Parker, R.; Ring, S.G. A theoretical analysis of diffusion-controlled reactions in frozen solutions. Cryo-Letters 1995, 6, 197–208.
Powrie, W.D. Characteristics of food myosystems and their behavior during freezepreservation. In Low-Temperature Preservation of Foods and Living Matter; Fennema, O.R.; Powrie, W.D.; Marth, E.H., Eds.; Marcel Dekker, Inc., N.Y, 1973; pp 282–353.
Rubinsky, B.; Arav, A.; Hong, J.-S.; Lee, C.Y. Freezing of mammalian livers with glycerol and antifreeze proteins. Biochem. Biophys. Res. Comm. 1994, 200, 732–741.
Shenouda, S.Y. Theories of protein denaturation during frozen storage of fish flesh. Adv. Food Res. 1980, 26, 275–311.
Shoji, T.; Saeki, H.; Wakarneda, A.; Nakamura, M.; Nonaka, M. Gelation of salted paste of Alaska pollock by high hydrostatic pressure and change in myofibrillar protein in it. Nippon Suisan Gakkaishi 1990, 56(12), 2069–2076.
Shoji, T.; Saeki, H., Wakarneda, A., Nonaka, M. Muence of ammonium salt on the formation of pressure-induced gel from Walleye pollock suiimi. Nippon Suisan Gakkaishi 1994, 60(1), 101–109.
Sikorski, Z.; Olley, J.; Kostuch, S. Protein changes in frozen fish. Crit. Rev. Food Sci. Nutri. 1976, 8, 97.
Yamamoto, K. Changes in myosin molecule and its proteolytic subfragments induced by high hydrostatic pressure. Abst. Int. Conf High Press. Biosci. Biotechnol. Kyoto, Japan, 1995.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Lanier, T.C. (1998). High Pressure Processing Effects on Fish Proteins. 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_5
Download citation
DOI: https://doi.org/10.1007/978-1-4899-1925-0_5
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-1927-4
Online ISBN: 978-1-4899-1925-0
eBook Packages: Springer Book Archive