Four anionic trypsins, tentatively labeled trypsin A, B, C, and D, isolated from crayfish hepatopancreas, had high casein activity between pH 5.5 and 10.0. Temperature optima for hydrolysis of casein were 45°C for A and B, and 50°C for C and D. Trypsin D had the highest substrate turnover number (V max ) for casein reaction compared with the other trypsins at pH 6.8. Trypsins A and D had higher activities against myofibrilla and sarcoplasmic proteins from crayfish tail meat than did B and C. Results suggested that trypsins A and D are important in development of mushiness in crayfish tail meat compared with other trypsins present.
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Kim et al. (1996) studied this question.
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