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首页> 外文期刊>Journal of Food Science >ANIONIC TRYPSINS FROM CRAYFISH HEPATOPANCREAS - EFFECTS ON PROTEIN DEGRADATION OF TAIL MEAT
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ANIONIC TRYPSINS FROM CRAYFISH HEPATOPANCREAS - EFFECTS ON PROTEIN DEGRADATION OF TAIL MEAT

机译:小龙虾肝胰蛋白酶中的胰蛋白酶-对尾肉蛋白质降解的影响

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摘要

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 degrees C for A and B, and 50 degrees 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.
机译:从小龙虾肝胰脏中分离得到的四种阴离子胰蛋白酶(暂定标记为胰蛋白酶A,B,C和D)在pH 5.5至10.0之间具有较高的酪蛋白活性。酪蛋白水解的最佳温度是A和B为45摄氏度,C和D为50摄氏度。与其他胰蛋白酶在pH 6.8相比,胰蛋白酶D酪蛋白反应的底物周转数(V-max)最高。胰蛋白酶A和D对小龙虾尾肉的肌原纤维和肌浆蛋白的活性高于B和C。结果表明,与目前存在的其他胰蛋白酶相比,胰蛋白酶A和D在小龙虾尾肉的粘稠性发展中很重要。

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