Abstract
Crude proteolytic enzyme extracts were prepared from the muscle tissues of two fish species, blue fish and sheephead, and subjected to high hydrostatic pressure treatments (from 1,000–3,000 atm), and monitored for residual activity for cathepsin C., collagenase, chymotrypsin-like and trypsin-like enzymes versus homologous enzymes from bovine. The fish enzymes were more sensitive to hydrostatic pressure than the mammalian enzymes. The extent of enzyme inactiva-tion achieved depended on both the amount of pressure applied, the duration of pressurization, and on the source material. Pressure treatment of fresh fish flesh formed products whose color deteriorated (cooked appearance) with increasing pressure as well as holding time. Application of pressure also improved tissue firmness or strength of fresh fish up to 2,000 atm and a holding time of 10 min, beyond which texture generally deteriorated. The combined use of pressure in combination with the broad spectrum protease inhibitor, α2-macroglobulin, enhanced the capacity of the hydrostatic pressure technology to achieve a more lasting inactivation of endogenous enzymes to form stable fish gels.
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References
Ashie, I.N.A.; Simpson, B.K. Effects of hydrostatic pressure on alpha-Macroglobulin and selected proteases. J. Food Biochem. 1995, 18, 377–391.
Ashie, I.N.A.; Simpson, B.K.; Smith, J.R Spoilage and shelf-life extension of fresh fish and shellfish. CRC Crit. Rev. Fd. Sci. Nutr. 1996a, 36, 1–30.
Ashie, I.N.A.; Simpson, B.K.; Ramaswamy, H.S. Control of endogenous enzyme activity by inhibitors and hydrostatic pressure using RSM. J. Food Sci. 1996b, 61, 350–356.
Baranowski, J.D.; Nip, W.K.; Moy, J.H. Partial characterization of a crude enzyme extract from the freshwater prawn, (Marcobrachium rosenbergii), J. Food Sci. 1984, 49, 1494–1495.
Bourne, M.C. Interpretation of force curves from instrumental texture measurements. In Rheology and Texture in Food Quality; Deman, et al., Eds; AVI Publishing Company Inc. Wesport, CN, 1976; pp 244–274.
Bridgman, P.W. The coagulation of albumen by pressure. J. Biol. Chem. 1914, 19, 511–512.
Curl, L.A.; Jansen, E.F. Effect of high pressures on trypsin and chymotrypsin. J. Biol. Chem. 1950, 184, 45–54.
Erlanger, B.F.; Kokowsky, N.; Cohen, W. The preparation and properties of two new chromogenic substrates of trypsin. Archs. Biochem. Biophys. 1961, 95, 271–278.
Farkas, D.F. Novel Processes — Ultra High Pressure Processing. In Food Protection Technology; Felix, C.W., Ed.; Lewis Pub., Inc. Chelsea, Michigan, 1987.
Farr, D. High pressure technology in the food industry. Trends Food Sci. Technol. 1990, 1, 14–16.
Fletcher, G.C.; Statham, J.A. Shelf-life of sterile yellow-eyed mullet (Aldrichetta forsten) at 4°C. J. Food Sci. 1988, 53, 1030–1035.
Flick, G.J.; Lovell R. T. Postmortem degradation of nucleotides and glycogen in Gulf shrimp. Dissert. Abst. Int. Section B. Science and Engineering. 1970, 30, 1743.
Francis, F. J.; Clydesdale, F. M. Food Colorimetry: Theory and Applications. AVI Publishing Co., Inc. Westport, CT, 1975.
Guizani, N.; Marshall, M.R.; Wei, C.I. Purification and characterization of a trypsin-like enzyme from the hepa-topancreas of crayfish (Procambarus clarkii). Comp. Biochem. Physiol. 1992, 103B, 809–815.
Haard, N.F.; Martins, I.; Newbury, R.; Botta, R. Hypobaric storage of Atlantic herring and cod. Can. Inst. Food Sci. Technol. J. 1979, 12, 84–87.
Hartree, E.F. Determination of protein: a modification of the Lowry method that gives a linear photometric response. Anal. Biochem. 1972, 48, 422–427.
Hayakawa, I.; Kanno, T.; Tomita, M.; Fujio, Y. Application of high pressure for spore inactivation and protein de-naturation. J. Food Sci. 1994, 59, 159–163.
Hite, B.H.; Giddings, N.J.; Weakly, C.E. The effects of pressure on certain microorganisms encountered in the preservation of fruits and vegetables. Bull. 146, W. Va. Univ. Agric. Exp. Sta. Morgantown, USA, 1994.
Hochachka, P.W.; Storey, K.B.; Baldwin, J. Gill citrate synthase from an abyssal fish. Comp. Biochem. Physiol. 1975, 52B, 43–49.
Hultin, H.; McDonald, R.; Kelleher, S. Lipid oxidation in fish muscle microsome. In Chemistry & Biochemistry of Marine Food Products; Martin et al., Eds.; AVI, Westport, Connecticut, 1982; pp 1–9.
Hummel, B.C.W. A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin. Can. J. Biochem. Physiol. 1950, 37, 1393–1399.
Konagaya, S. Proteases responsible for softening or lysing of meat of chum salmon caught during spawning migration. Bull. Tokai Reg. Fish. Res. Lab. 1985, 116, 39–47.
Lakidos, D.; Lougovois, V. Lipid oxidation in muscle foods. Food Chem. 1990, 35, 295–314.
Lanier, T.C.. High pressure processing effects on fish products. In Int. Chem. Congress of Pacific Basin Societies; Dec. 1995, 17–22.
Lee, H-J.; LaRue, J. N.; Wilson, I. B. A simple spectrophotometric assay for amino acyl arylamidases (naphtylami-dases, aminopeptidases). Anal. Biochem. 1971, 41, 397–401.
Lindner, P.; Angel, S.; Weinberg, Z.G.; Granit, R. Factors inducing mushiness in stored prawns. Food Chemistry. 1988, 29, 119–132.
Nagashima, Y.; Ebina, H.; Tanaka, M.; Taguchi, T. Effect of high hydrostatic pressure on the thermal gelation of squid mantle meat. Food Res. Int. 1993, 26, 119–123.
Nip, W.K.; Lan, C. Y.; Moy, J.H. Partial characterization of a collagenolytic enzyme fraction from the hepatopan-creas of the freshwater prawn, (Macrobrachium rosenbergii.) J. Food Sci. 1985, 50, 1187–1188.
Ogawa, H.; Fukuhisa, K.; Kubo, Y; Fukumoto, H. Pressure inactivation of yeasts, molds, and pectinesterase in Satsuma Mandarin juice: effects of juice concentration, pH, and organic acids, and comparison with heat sanitation. Agric. Biol. Chem. 1990, 54, 1219–1225.
Okamoto, M.; Kawamura, Y; Hayashi, R. Application of high pressure to food processing: textural comparison of pressure- and heat-induced gels of meat proteins. Agric. Biol. Chem. 1990, 54, 183–189.
Ohshima, T.; Ushio, H.; Koizumi, C. High pressure processing of fish and fish products. Trends Food Sci. Technol. 1993, 4, 370–375.
Sareevoravitkul, R.; Simpson, B.; Ramaswamy, H. Comparative properties of bluefish (Pomatomus saltatrix) gels formulated by high hydrostatic pressure and heat. J. Aquat. Food Prod. Tech. 1996, (In press).
Shoji, I.; Saeki, H.; Wakameda, 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: 2069–2076
Simpson, M.V.; Haard, N.F. Temperature acclimation of Atlantic cod (Gadus morhua) and its influence on freezing point and biochemical damage of postmortem muscle during storage at 0°C and-3°C. J. Food Biochem. 1987a, 11, 69–93
Simpson, B.K.; Haard, N.F. Cold-adapted enzymes from fish. In Food Biotechnology; Knorr, D., Ed.; Marcel Dekker, Inc, 1987b; pp 495–527.
Steel, R.J.D.; Torrie, J.H. Principles and Procedures of Statistics — A Biometrie Approach. (Steel, R.J.D., and Torrie, J.H., eds.). McGraw Hill Pub. Co., 1980, pp 173–175.
Toyomizu, M.; Hanaoka, K.; Yamaguchi, K. Effect of release of free fatty acids by enzymatic hydrolysis of phospholipids on lipid oxidation during storage of fish at-5°C. Nippon Suisan Gakkaishi. 1988, 47, 615–620.
Tsukuda, N. Studies on the discoloration of red fishes. VI. Bull. Jpn. Soc. Sci. Fish. 1970, 36, 725–730.
Wasson, D.H. Fish muscle proteases and heat-induced myofibrillar degradation: A Review. J. Aquat. Food Prod. Technol 1992, 1(2), 23–41.
Wunsch, E.; Heidrich, H-G. Quantitative determination of collagenase. Biochem. J. 1963, 333, 149–151.
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Simpson, B.K. (1998). High Pressure Processing of Fresh Seafoods. 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_7
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DOI: https://doi.org/10.1007/978-1-4899-1925-0_7
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