Characteristics of extracellular proteases produced by Bacillus laterosporus and Flavobacterium sp. isolated from gelatinfactory effluents Authors
Revised: 05 December 1995 Accepted: 11 December 1995 DOI:
Cite this article as: Sharma, A., Rao, C.L.S.N., Ball, B.K. et al. World Journal of Microbiology & Biotechnology (1996) 12: 615. doi:10.1007/BF00327724 Abstract
Forty bacterial isolates from the effluents of a gelatin factory (Jabalpur, India) were screened for protease activity and the two most potent producers were identified as
Bacillus laterosporus and a Flavobacterium sp. The enzymes of both isolates were optimal at pH 8 and 60°C, with maximum activity after 90 min. The enzyme activity of B. laterosporus was suppressed by Fe 2+, Mg 2+, Mn 2+ and Zn 2+ ions but was enhanced by Ba 2+ and Ca 2+. That of Flavobacterium sp. was suppressed by Mg 2+ and Mn 2+ ions but enhanced by Ba 2+, Ca 2+ and Fe 2+. The enzyme activity of the former was strongly inhibited by KCN, whereas that of the latter was only slightly inhibited by 8-hydroxyquinoline. Key words Bacillus laterosporus Flavobacterium gelatin protease References
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