The denaturation of myof ibrillar protein of bighead carp ( Aristichthys nobilis) during frozen storage at different temperatures ( - 10 e , - 20 e , - 30 e and - 40 e ) was studied by measuring the solubility of actomyosin, ATPase activities and - SH content of myofibrillar protein. The results indicated that the solubility of actomyosin, ATPase activities and-SH content of myofibrillar protein decreased as frozen storage progressed. The temperature of frozen storage can significantly inf luence the rate of denaturation of myofibrillar protein ( P< 0. 01) . The lower the frozen storage temperature, the slower the rate of denaturation of protein is.