Fisheries and Aquatic Sciences

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
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Optimal Conditions for the Distribution of Cryoprotectant into the Intact Fish Muscle of Oncorhynchus mykiss during Freeze/Thaw Cycling

  • Kong Chang Suk (Department of Food Science and Nutrition, Pusan National University) ;
  • Park Kun Young (Department of Food Science and Nutrition, Pusan National University)
  • Published : 2005.03.01
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Abstract

Conditions for sufficient and rapid distribution of a cryoprotectant (sorbitol solution) into intact fish muscle (Oncorhynchus mykiss) were studied as changing in the residual Ca2+ ATPase activity during freeze/thaw cycling. Chunks of the fish muscle were immersed in 4 concentrations of sorbitol solutions ($20\%$, $30\%$, $45\%$, and $60\%$) by a shaker mechanism at 5$^${circ}C. Whole immersion samples (W) showed a higher value of the residual Ca2+ ATPase activity than those in the untreated controls (C), except in the treated controls (TC), while less effect of immersion concentration could be found. Comparing the extent of penetration of sorbitol into the surface layer to inner layer of immersed fish chunks, outer portion samples achieved excellent cryoprotection with $100\%$ of the residual ATPase activity values or more. For the inner portion samples, $30\%$ and $45\%$ sorbitol solution treatments indicated a higher ATPase activity than $60\%$ treatment. At high concentrations, mass transfer rates during osmotic dehydration might berapid and it causes faster surface drying by dewatering at surface solute layer. Periodically immersed and relaxed samples, W (5-3-1), led to good cryoprotection effect: W (5-3-1) indicated high residual Ca2+ ATPase activity values and the residual ATPase activity values excess $100\%$ in immersion of $30\%$ and $45\%$ sorbitol solutions.

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References

  1. Arakawa, T. and S.N. Timasheff. 1982. Stabilization of protein structure by sugars. Biochemistry, 21, 6536-6544 https://doi.org/10.1021/bi00268a033
  2. Back, J.F., D. Oakenfull and M.B. Smith. 1979. Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry, 18, 5191-5196 https://doi.org/10.1021/bi00590a025
  3. Bolin. H.R., C.C. Huxsoll, R. Jackson and K.C. Ng. 1983. Effect of osmotic agents and concentration on fruit quality. J. Food Sci., 48, 202-205 https://doi.org/10.1111/j.1365-2621.1983.tb14823.x
  4. Carpenter, J.F. and J.H. Crowe. 1988. The mechanism of cryoprotection of proteins by solutes. Cryobiology, 25, 244-255 https://doi.org/10.1016/0011-2240(88)90032-6
  5. Carvajal, P.A., G.A. MacDonald and T.C. Lanier. 1999. Cryostabilization mechanism of fish muscle proteins by maltodextrins. Cryobiology, 38, 16-26 https://doi.org/10.1006/cryo.1998.2142
  6. Connell, J.J. 1961. The relative stabilities of the skeletal muscle myosins of some animals. Biochem. J., 80, 503-509 https://doi.org/10.1042/bj0800503
  7. Fiskke, C.H. and Y. Subbarow. 1925. The colorimetric determination of phosphorus. J. Biol. Chem., 66, 375-400
  8. Franks. F., J.R. Ravenhill and D.S. Reid. 1972. Thermodynamic studies of dilute aqueous solutions of cyclic ethers and simple carbohydrates. J. Sol. Chem., 1, 3
  9. Fukuda, Y., Z. Tarakita and K. Arai. 1984. Effect of freshness of chub mackerel on the freeze denaturation of myofibrillar protein. Bull. Jap. Soc. Sci. Fish., 50, 845-852 https://doi.org/10.2331/suisan.50.845
  10. Haard, N.F.1992. Biochemical reactions in fish muscle during frozen storage. In: Seafood Science and Technology. Bligh, E.G., ed. Fishing New Books, Oxford, pp. 176-209
  11. Hashimoto, A., A. Kobayashi and K. Arai. 1982. Thermostability of fish myofibrillar Ca-ATPase and adaptation to environmental temperature. Bull. Jap. Soc. Sci. Fish., 48, 671-684 https://doi.org/10.2331/suisan.48.671
  12. Kawashima, T., K. Arai and T. Saito. 1973. Studies on muscular proteins of fish-IX. An attempt on quantitative determination of actomyosin in frozen 'surimi' from Alaska pollack. Bull. Jap. Soc. Sci. Fish., 39, 207-214 https://doi.org/10.2331/suisan.39.207
  13. Lee, J.C. and S.N. Timasheff. 1981. The stabilization of proteins by sucrose. J. Biol. Chem., 256, 7193-7201
  14. MacDonard, G.A., N.D.C. Wilson and T.C. Lanier. 1990. Stabilized mince: an alternative to the traditional surimi process. In: Chilling and Freezing of New Fish Products. Intl, Inst. Refrig., 69-76
  15. MacDonard, G.A. and T.C. Lanier. 1994. Actomyosin stabilization to freeze-thaw and heat denaturation by lactate salts. J. Food Sci., 59, 101-105 https://doi.org/10.1111/j.1365-2621.1994.tb06907.x
  16. MacDonald, G.A., T.C. Lanier, H.E. Swaisgood and D.D. Hamann. 1996. Mechnism for stabilization of fish actomyosin by sodium lactate. J. Agr. Food Chem., 44, 106-112 https://doi.org/10.1021/jf940698y
  17. Matsumoto, J.J. 1979. Denaturation of fish muscle proteins during frozen storage. In: Proteins at Low Temperature, Fennema, O., ed. American Chemical Society, Washington DC, pp. 206-224
  18. Matsumoto, J.J. and S. Noguchi. 1992. Cryostabilization of protein in Surimi. In: Surimi Technology, Lanier, T.C. and C.M. Lee, cds. Marcel Dekker, Inc., New York, pp. 357-388
  19. Niwa, E. 1992. The chemistry of surimi gelation. In: Surimi Technology, Lanier, T.C. and C.M. Lee, eds. Marcel Dekker, Inc., New York, pp. 389-428
  20. Noguchi, S. and J.J. Matsmoto. 1970. Studies on the control of the denaturation of the fish muscle proteins during frozen storage. I. Preventive effect of Na-glutamate. Bull. Jap. Soc. Sci. Fish., 36, 1078-1087 https://doi.org/10.2331/suisan.36.1078
  21. Noguchi, S. 1974. The control of denaturation of fish muscle proteins during frozen storage. Ph.D. Thesis, Sophia University, Tokyo, Japan, pp. 138
  22. Noguchi, S. and J.J. Matsumoto. 1975. Studies on the control of the denaturation of the fish muscle proteins during frozen storage. IV. Preventive effect of carboxylic acids. Bull. Jap. Soc. Sci. Fish., 41, 329-335 https://doi.org/10.2331/suisan.41.329
  23. Okada, M. 1992. History of surimi technology in Japan. In: Surimi Technology, Lanier, T.C. and C.M. Lee, eds. Marcel Dekkar, Inc., New York, Dekker, New York, pp. 3-22
  24. Park, J.W., T.C. Lanier and D.P. Green. 1988. Cryoprotective effects of sugars, polyols, and/or phosphates on Alaska pollock surimi. J. Food Sci., 53, 1-3 https://doi.org/10.1111/j.1365-2621.1988.tb10163.x
  25. Rastogi, N.K., A. Angersbach and D. Knorr. 2000. Evaluation of mass transfer mechanisms during osmostic trearment of plant materials. J. Food Sci., 65, 1016-1019 https://doi.org/10.1111/j.1365-2621.2000.tb09409.x
  26. Salvatori, D., A. Andres, A. Albors, A. Chiralt and P. Fito. 1998. Structural and compositional profiles in osmotically dehydrated apple. J. Food Sci., 63, 606-610
  27. Sych, J., C. Lacroix, L.T. Adambounou and F. Castigne. 1991a. The effect of low- or non-sweet additives on the stability of protein functional properties of frozen cod. Int. J. Food Sci. Technol., 26, 185-197
  28. Sych, J., C. Lacroix and M. Carrier. 1991b. Determination of optimal level of lactitol for surimi. J. Food Sci., 56, 285-290 https://doi.org/10.1111/j.1365-2621.1991.tb05263.x
  29. Tait, M.J., A. Suggett, F. Franks, S. Ablett and P.A. Quickenden. 1972. Hydration of monosaccharides: a study by dielectric and nuclear magnetic relaxation. J. Sol. Chem., 1, 131-151 https://doi.org/10.1007/BF01028450
  30. Uedeira, H. 1980. The effect of sugars on the thermal denaturation of lysozyme. Bull. Chem. Soc. Jap., 532, 2451-2455