Purification and preliminary characterization of five serine proteinases produced by Brevibacterium linens

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Abstract
Summary: Five proteinases were purified from culture filtrate of Brevibacterium linens by a series of column chromatography and found to be homogeneous by polyacrylamide gel electrophoresis. All appear to be serine proteinases, being inactivated by phenyl‐methylsulphonyl fluoride and not by EDTA or p‐chloromercuribenzoic acid. They were all active against casein in alkaline pH (pH optimum of 11.0) and specific activity was within the range 2.66–3.23 units mg−1 protein. Proteinases C, D and E were more stable in higher temperature and acidic pH than proteinases A and B. Molecular weights estimated by gel filtration were 37000, 37000, 44000, 127000 and 325000 for proteinases, A, B, C, D and E, respectively.