An intracellular proteinase from Streatococcus cremoris was isolated, partially purified and characterized. A 40‐fold purification was obtained with retention of 73% of the original activity. The proteinase exhibited normal reaction kinetics with respect to enzyme concentration and reaction rate. Proteinase activity was optimal at pH 7.0 and 37°C. The enzyme showed maximum activity on casein, the alpha casein being preferentially degraded. Effect of metal ions, some inhibitors and reducing agents were studied.
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ARORA et al. (1979) studied this question.
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