Some properties of protease extracted from the hepatopancreas of crayfish, procambarus clarkii

Crayfish hepatopancreatic protease had consistently high activity between pH 5.8 and 9.0. Temperature optima for hydrolysis of casein was 50℃ at pH 6.8. Proteolytic activity decreased linearly with prolonged incubation time, which indicates the enzyme was not existed as zymogen type. The activity was highest at concentrations of 0.025 to 0.05 mM Ca²⁺ ions. Crude enzyme was inactivated by serine protease inhibitors and inhibition degree was higher N-tosyl-L-lysine-chloromethyl ketone (TLCK) than N-tosyl-L-phynylalanine-chloromethyl ketone (TPCK).

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