Frozen storage is one of the most important preservation methods for maintaining microbiological and chemical stability and extending the shelf life of food products. Deteriorations in texture, flavor, and color, resulting from biochemical, enzymatic, and functional changes in proteins, however, are problems associated with freezing and subsequent storage at subfreezing temperatures for many fresh and processed foods. Freeze-induced protein denaturation, enzyme inactivation, and related functionality losses are commonly observed in frozen fish, meat, poultry, egg products, and doughs. Muscle proteins are particularly susceptible to freeze denaturation compared to plant-derived proteins, and this is especially true for fish species. Denaturation of proteins during freezing and frozen storage can be monitored by measuring alterations in protein surface hydrophobicity, amino acid composition, conformational stability, solubility, aggregation, and enzyme activity. Losses in functional properties of proteins are commonly assessed by comparing water-holding ability, viscosity, gelation, emulsification, foaming, and whipping properties.
- Muscle Protein
- Protein Denaturation
- Freeze Storage
- Myofibrillar Protein
- Functionality Loss
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, access via your institution.
Tax calculation will be finalised at checkout
Purchases are for personal use onlyLearn about institutional subscriptions
Unable to display preview. Download preview PDF.
Ang, J.F. and Hultin, H.O. 1989. Denaturation of cod myosin during freezing after modification with formaldehyde. J. Food Sci. 54:814–818.
Awad, A., Powrie, W.D., and Fennema, O. 1968. Chemical deterioration of frozen bovine muscle at −4°C. J. Food Sci. 33:227–235.
Berglund, P.T., Shelton, D.R., and Freeman, T.P. 1991. Frozen bread dough ultrastructure as affected by duration of frozen storage and freeze-thaw cycles. Cereal Chem. 68:105–107.
Buttkus, H. 1970. Accelerated denaturation of myosin in frozen solution. J. Food Sci. 35:558–562.
Careche, M. and Tejada, M. 1994. Hake natural actomyosin interaction with free fatty acids during frozen storage. J. Sci. Food Agric. 64:501–507.
Castrillón, A.M., Alvarez-Pontes, E., Arias, M.T.G., and Navarro, P. 1996. Influence of frozen storage and defrosting on the chemical and nutritional quality of sardine (Clupea pilchardus). J. Sci. Food Agric. 70:29–34.
Cotterill, O.J. 1990. Freezing egg products. In Egg Science and Technology, 3d ed. (Stadelman, W.J. and Cotterill, O.J., eds.) pp. 217–242, Haworth Press, Binghamton, New York.
Davies, J.R., Ledward, D.A., Bardsley, R.G., and Poulter, R.G. 1994. Species dependence of fish myosin stability to heat and frozen storage. Int. J. Food Sci. Technol. 29:287–301.
Dyer, W.J. and Dingle, J.R. 1961. Fish proteins with special reference to freezing. In Fish as Food. I. Biochemistry and Microbiology. (Borgstrom, G., ed.) pp. 275–327, Academic Press, New York.
Feeney, R.E. and Yeh, Y. 1993. Antifreeze proteins: Properties, mechanism of action, and possible applications. Food Technol. 47(1):82, 84–88, 90.
Fennema, O. 1982. Behavior of proteins at low temperatures. In Food Protein Deterioration Mechanisms and Functionality. (Cherry, J.P., ed.) pp. 109–133, ACS Symposium Series 206, American Chemical Society, Washington, D.C.
Franks, F. 1995. Protein destabilization at low temperatures. Adv. Protein Chem. 46:105–139.
Herald, T.J., Osorio, F.A., and Smith, D.M. 1989. Rheological properties of pasteurized liquid whole egg during frozen storage. J. Food Sci. 54:35–38, 44.
Huidobro, A. and Tejada, M. 1992. Foaming capacity of fish minces during frozen storage. J. Sci. Food Agric. 60:263–270.
Huidobro, A. and Tejada, M. 1993. Emulsifying capacity of fish mince from several species during frozen storage. J. Sci. Food Agric. 61:333–338.
Huidobro, A. and Tejada, M. 1995. Alteration of the electrophoretic pattern of myofibrillar proteins in fish mince during frozen storage. Z. Lebensm. Unters. Forsch. 200:247–251.
Inoue, N., Takatori, K., Motoshige, T., and Shinano, H. 1992. Effect of storage temperature on the freeze denaturation of fish myosin B. Nippon Suisan Gakkaishi 58:2357–2360.
Inoue, Y., Sapirstein, H.D., Takayanagi, S., and Bushuk, W. 1994. Studies on frozen doughs. III. Some factors involved in dough weakening during frozen storage and thaw-freeze cycles. Cereal Chem. 71:118–121.
Jarenbäck, L. and Liljemark, A. 1975. Ultrastructural changes during frozen storage of cod. III. Effects of linoleic acid and linolenic acid hydroperoxides on myofibrillar proteins. J. Food Technol. 10:437–452.
Jiang, S.-T., Hwang, B.-S., Moody, M.W., and Chen, H.-C. 1991. Thermostability and freeze denaturation of grass prawn (Penaeus monodon) muscle proteins. J. Agric. Food Chem. 39:1998–2001.
Jiménez-Colmenero, F., Tejada, M., and Borderias, A.J. 1988. Effect of seasonal variations on protein functional properties of fish during frozen storage. J. Food Biochem. 12:159–170.
Kang, J.O., Ito, T., and Fukazawa, T. 1983. Effect of frozen storage on the structure and enzymatic activities of myofibrillar proteins of rabbit skeletal muscle. Meat Sci. 9:131–144.
Kim, B.Y., Hamann, D.D., Lanier, T.C., and Wu, M.C. 1986. Effects of freeze-thaw abuse on the viscosity and gel-forming properties of surimi from two species. J. Food Sci. 51:951–956, 1004.
Kinsella, J.E. 1976. Functional properties of proteins in foods: a survey. CRC Crit. Rev. Food Sci. Nutr. 7:219–280.
Lawrie, R.A. 1991. Meat Science, 5th ed. Pergamon Press, New York.
LeBlanc, E.L. and LeBlanc, R.J. 1992. Determination of hydrophobicity and reactive groups in proteins of cod (Gadus morhua) muscle during frozen storage. Food Chem. 43:3–11.
Li-Chan, E., Nakai, S., and Wood, D.F. 1985. Relationship between functional (fat binding, emulsifying) and physicochemical properties of muscle proteins: effects of heating, freezing, pH, and species. J. Food Sci. 50:1034–1040.
Love, R.M. 1968. Ice formation in frozen muscle. In Low Temperature Biology of Foodstuffs. (Hawthorn, J. and Rolfe, E.J., eds.) pp. 105–124, Pergamon Press, Oxford.
Love, R.M. and Lavéty, J. 1972. The connective tissues of fish. VII. Postmortem hydration and ice crystal formation in myocommata and their influence on gaping. J. Food Technol. 7:431–441.
Montera, P. and Borderías, J. 1990. Behavior of myofibrillar proteins and collagen in hake (Merluccius merluccius L.) muscle during frozen storage and its effect on texture. Z Lebensm. Unters. Forsch. 190:112–117.
Nambudiri, D.D. and Gopakumar, K. 1992. ATPase and lactate dehydrogenase activity in frozen stored fish muscle as indices of cold storage deterioration. J. Food Sci. 57:72–76.
Olley, J., Pirie, R., and Watson, H. 1962. Lipase and phospholipase activity in fish skeletal muscle and its relationship to protein denaturation. J. Sci. Food Agric. 13:501–516.
Park, J.W., Lanier, T.C., and Pilkington, D.H. 1993. Cryostabilization of functional properties of prerigor and postrigor beef by dextrose polymer and/or phosphates. J. Food Sci. 58:467–472.
Payne, S.R. and Young, O.A. 1995. Effects of pre-slaughter administration of antifreeze proteins on frozen meat quality. Meat Sci. 41:147–155.
Privalov, P.L., Griko, Y.V., Venyaminov, Y.S., and Kutyshenko, VP. 1986. Cold denaturation of myoglobin. J. Mol. Biol. 190:487–497.
Privalov, P.L. and Makhatadze, G.I. 1993. Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration. J. Mol. Biol. 232:660–679.
Rahelic, S., Gawwad, A.H., and Puac, S. 1985. Structure of beef longissimus dorsi muscle frozen at various temperatures. Part 2: Ultrastructure of muscle frozen at −10, −22, −33, −78, and −115°C. Meat Sci. 14:73–81.
Reddy, G.VS., Srikar, L.N., and Sudhara, N.S. 1992. Deteriorative changes in pink perch mince during frozen storage. Int. J. Food Sci. Technol. 27:271–276.
Shenouda, S.Y.K. 1980. Theories of protein denaturation during frozen storage of fish flesh. Adv. Food Res. 26:275–311.
Smith, D.M. 1987. Functional and biochemical changes in deboned turkey due to frozen storage and lipid oxidation. J. Food Sci. 52:22–27.
Sotelo, C.G., Piñeir, C., and Pérez-Martin, R.I. 1995. Denaturation of fish proteins during frozen storage: role of formaldehyde. Z Lebensm. Unters. Forsch. 200:14–23.
Sych, J., Lacroix, C., Adambounou, L.T., and Castaigne, F. 1990. Cryoprotective effects of lactitol, palatinit, and polydextrose on cod surimi proteins during frozen storage. J. Food Sci. 55:356–360.
Sych, J., Lacroix, C., Adambounou, L.T., and Castaigne, F. 1991. The effect of low-and non-sweet additives on the stability of protein functional properties of frozen cod surimi. Int. J. Food Sci. Technol. 26:185–197.
Takahashi, K., Inoue, N., and Shinano, H. 1993. Effect of storage temperature on freeze denaturation of carp myofibrils with KC1 or NaCl. Nippon Suisan Gakkaishi 59:519–527.
Wagner, J.R. and Añón, M.C. 1985. Effect of freezing rate on the denaturation of myofibrillar proteins. J. Food Technol. 20:735–744.
Wagner, J.R. and Añón, M.C. 1986. Effect of frozen storage on protein denaturation in bovine muscle. 1. Myofibrillar ATPase activity and differential scanning calorimetric studies. J. Food Technol. 21:9–18.
Wootton, M., Hong, N.T., and Thi, H.A.P. 1981. A study of the denaturation of egg white proteins during freezing using differential scanning calorimetry. J. Food Sci. 46:1336–1338.
Xiong, Y.L., Decker, E.A., Robe, G.H., and Moody, W.G. 1993. Gelation of crude myofibrillar protein isolated from beef heart under antioxidative conditions. J. Food Sci. 58:1241–1244.
Yamamoto, K., Samejima, K., and Yasui, T. 1977. A comparative study of the changes in hen pectoralis muscle during storage at 4°C and −20°C. J. Food Sci. 42:1642–1645.
Yoon, K.S., Lee, CM., and Hufnagel, L.A. 1991. Effect of washing on the texture and microstructure of frozen fish mince. J. Food Sci. 56:294–298.
Editors and Affiliations
© 1997 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Xiong, Y.L. (1997). Protein Denaturation and Functionality Losses. In: Erickson, M.C., Hung, YC. (eds) Quality in Frozen Food. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5975-7_8
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-7738-2
Online ISBN: 978-1-4615-5975-7
eBook Packages: Springer Book Archive