ABSTRACT Alkaline protease in croaker exists not only in the sarcoplasmic fraction of skeletal muscle but also in the skin and internal organs. As characterized by optimal pH, thermal stability, and column chromatography, the alkaline proteases obtained from different fish tissues such as muscle, skin, kidney, and alimentary canal exhibit similar enzymatic properties. An experiment using chloramphenicol to inhibit bacterial growth suggests that the heat‐stable alkaline protease present in the minced (mechanically separated) croaker is likely not of bacterial origin. The high specific activity of alkaline protease from kidney, liver, and visceral tissue in comparison to that of skin and muscle suggests that inclusion of residual tissue in even small amounts from the former sources could contribute greatly to the total activity measured in fish mince.
Journal of Food Science – Wiley
Published: Nov 1, 1981
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