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Anionic Trypsins from Crayfish Hepatopancreas: Effects on Protein Degradation of Tail Meat
Author(s) -
KIM H.R.,
MEYERS SAMUEL P.,
GODBER J. SAMUEL
Publication year - 1996
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1996.tb14729.x
Subject(s) - hepatopancreas , crayfish , degradation (telecommunications) , chemistry , biochemistry , food science , biology , fishery , telecommunications , computer science
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.