ISSN:
1365-2621
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1990.tb01072.x
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