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INTRACELLULAR PROTEINASE FROM Streptococcus cremoris
Author(s) -
ARORA J. L.,
RAO L. KRISHNA,
SANNABHADTI S. S.,
SRINIVASAN R. A.
Publication year - 1979
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.1365-2621.1979.tb06436.x
Subject(s) - casein , intracellular , enzyme , chemistry , biochemistry , kinetics , specific activity , physics , quantum mechanics
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.