Premium
Purification and preliminary characterization of five serine proteinases produced by Brevibacterium linens
Author(s) -
HAYASHI K.,
CLIFFE A. J.,
LAW B. A.
Publication year - 1990
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.1990.tb01072.x
Subject(s) - brevibacterium , chemistry , chromatography , size exclusion chromatography , casein , serine , polyacrylamide gel electrophoresis , electrophoresis , enzyme , biochemistry , bacteria , biology , microorganism , genetics
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.