Studies on a membrane bound protease from Bacillus pumilus & Escherichia coli
Modi, M.; Wamanacharya, P.; Mehta, B.; Shah, K.; Modi, V.V.
Indian Journal of Experimental Biology 21(11): 611-613
1983
ISSN/ISBN: 0019-5189 PMID: 6373581 Document Number: 206230
The neutral protease activity of particulate fractions from E. coli and B. pumilus decreased gradually with increase in the concentration of penicillin. This enzyme was partially purified and characterized with its MW of .apprx. 48,000. The neutral protease from B. pumilus was inhibited by phenyl methylsulfonyl fluoride (PMSF) and EDTA suggesting that the enzyme required serine group and a divalent cation for its activity. A decline of 57% in Km and 37% in Vmax was observed in the presence of penicillin. The neutral protease from E. coli was inhibited by parachloro mercury benzoate (PCMB) and EDTA, suggesting the involvement of a SH group at the active site and a requirement for a divalent cation. A decline of 84% in Km and 66% in Vmax was observed in the presence of penicillin.