Sharma, A., Rao, C.L.S.N., Ball, B.K. et al. World Journal of Microbiology & Biotechnology (1996) 12: 615. doi:10.1007/BF00327724
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 Fe2+, Mg2+, Mn2+ and Zn2+ ions but was enhanced by Ba2+ and Ca2+. That of Flavobacterium sp. was suppressed by Mg2+ and Mn2+ ions but enhanced by Ba2+, Ca2+ and Fe2+. The enzyme activity of the former was strongly inhibited by KCN, whereas that of the latter was only slightly inhibited by 8-hydroxyquinoline.