Frozen muscle during

Jarenback and Liljemark (75,76) found similar changes in cod actomyosin solution and cod muscle during frozen storage. The denatured myosin was not extracted with salt solution. 

Owusu-Ansah, Y.L. and Hultin, H.O. 1987. Effect of in situ formaldehyde production on solubility and cross-linking of proteins of minced red hake muscle during frozen storage. Journal of Food Biochemistry 11 17-39. 

Thanonkaew, A., Benjakul, S., Visessanguan, V, and Decker, E.A. 2008. The effect of antioxidants on the quality changes of cuttlefish (Sepia pharaonis) muscle during frozen storage. FWT-Food Science and Technology 41 161-169. 

Ueng, Y.E. and Chow, C.J. 1998. Textural and histological changes of different squid mantle muscle during frozen storage. Journal of Agricultural and Food Chemistry 46 4728 733. 

Femandez-Reiriz, M.J., Pastoriza, L., Sampedro, G., and Herrera, J.J., 1995, Changes in lipids of whole and minced rayfish (Raja clavata) muscle during frozen storage, Z. Lebensm. Unters. Forsch., 200, 420. 

Haard, N.F., 1992, Biochemical reactions in fish muscle during frozen storage, in Seafood Science and Technology, Bligh, E.G., Ed., Fishing News Books, London, Chapter 20. 

Several fluorescence techniques have been used to investigate oxidation products in animal tissues, in frozen fish muscle during storage, in freeze-dried meats, and in oxidatively damaged soybeans. Mixtures of tissues are extracted with chloroform-methanol (2 1, by volume), homogenized, mixed with water and centrifuged. The chloroform layer is analysed for fluorescence using... 

LeBlanc E. LeBlanc, R. Determination of hydrophobicity and reactive groups in proteins of cod (Gadus morhua) muscle during frozen storage. Food Chem. 1992, 43, 3—11. 

Jiang, S.T. Hwang, B.O. Tsao, CT. Protein denaturation and changes in nucleotides of fish muscle during frozen storage. J. Agric. Food Chem. 1987a, 35, 22-27. 

Torres-Arreola, W., Soto-Valdez, H., Peralta, E., Cardenas-Lopez, J.L. and Ezquerra-Brauer, J.M. (2007). Effect of a low-density polyethylene film containing butylated hydroxytoluene on hpid oxidation and protein quaUty of sierra fish (Scomberomorus sierra) muscle during frozen storage. Journal of Agricultural and Food Chemistry, 55,6140-6146. 

Aldrin has been administered in vivo by injection into the posterior adductor muscle and by topical application to tissues (primarily gill). During the test period, animals have been left undisturbed in the ocean surf, confined in retrievable traps, or held in beakers at the study site and in the laboratory. Study periods have varied from 2 to 24 hours. Animals frozen and later homogenized and extracted yielded homogenates which contained aldrin and dieldrin and no other electron-capturing metabolites compared to controls. 

Shrimp samples held at 5°C showed increasing I-values during storage compared to frozen samples presumably due to increased breakdown of muscle tissue by inherent enzymes and/or increased microbial action. 

Sugar alcohols have also found application in foods containing sugars. Sorbitol is an effective cryoprotectant in surimi, preventing denaturation of the muscle protein during frozen storage. 

Chemical Deterioration of Muscle Proteins During Frozen Storage... 

Actomyosin. At high salt concentrations ( . . 0.6 M KC1), actin and myosin combine to form actomyosin filaments giving a highly viscous solution. Actomyosin retains the ATPase activity of myosin and demonstrates "super-precipitation" on the addition of ATP (24,34). As expected, there are differences between actomyosins of rabbit and fish with respect to solubility (10,22,35,36), viscosity (46) and ultracentrifugal behavior (477. Since actomyosin is the most readily available form of myofibrillar proteins from fish muscle, its behavior relative to deterioration during frozen storage has been most frequently studied. 

Information on the molecular changes occurring during frozen storage of whole muscle or of isolated protein preparations will be reviewed here. 

Connell has proposed that insolubilization of actomyosin during frozen storage of cod muscle is attributable to the denaturation of myosin rather than actin (89). During 40 weeks storage at -14°C, extractability of actomyosin and myosin decreased in parallel, while that of actin appeared to remain constant. The decrease in extractability of myosin was biphasic, while that of actomyosin followed an exponential curve. 

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