Anionic Trypsins from Crayfish Hepatopancreas: Effects on Protein Degradation of Tail Meat |
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Authors: | H.R. KIM SAMUEL P. MEYERS J. SAMUEL GODBER |
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Affiliation: | Authors Meyers and Godber are with the Dept. of Food Science, Louisiana Agricultural Experimental Station, Louisiana Agricultural Experimental Station and LSU Agricultural Center, Baton Rouge, LA 70803.;Author Kim's present address: Yosu National Fisheries Univ., Dept. of Food Science &Nutrition, Yosu-si, Chun-Nam, Korea, 550-749. |
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Abstract: | 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 (Vmax) 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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Keywords: | crayfish trypsin hepatopancreas protein-degradation tail meat |
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