Abstract
ABSTRACTThe denaturation of croaker actomyosin was studied with respect to the important role of coagulation and gelation phenomena in the manufacture of gel‐type meat and fish products. Measurements of turbidity (A600), viscosity, calcium ATPase activity, total sulfhydryl groups and protein coagulation of croaker actomyosin solutions during heating at a constant temperature increase of 1°C/min revealed no loss of enzymic activity nor evidence of protein aggregation prior to reaching a temperature of 37–40°C, at which point the protein coagulated with corresponding loss of ATPase activity and sulfhydryl groups and an increase in turbidity. The degree of protein coagulation was highly dependent on the protein concentration. An observed increase in the apparent viscosity over the 30–35°C temperature range was postulated to result from interaction of protein molecules due to noncovalent forces.
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