The effects of frozen storage temperatures on the formation of disulfides and the denaturation of actomyosin (AM), extracted from milk‐fish ( Chanos chanos ) dorsal muscle, were investigated. The activities of Ca‐ATPase and Mg(Ca)‐ATPase, Ca‐sensitivity and AM solubility in 0.6M KCl decreased at a higher rate at −20°C than at −35°C. The total NaBH 4 ‐soluble and insoluble proteins increased at a much higher rate at −20°C than at −35°C. During the freezing process, the total SHs decreased significantly; the total SHs decreased with a faster note at −20°C than at −35°C, suggesting that more disulfides formed in samples at −20°C than at −35°C. During storage, disulfides formed at −20°C but not at −35°C.
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Jiang et al. (1988) studied this question.
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