Asian Journal of Microbiology, Biotechnology & Environmental Sciences Paper

Vol 6 Issue 2, 2004; Page No.(215-219 )

PRETREATMENT OF LIPASE FROM BACILLUS COAGULANS BTS-1 WITH PROTEASES ENHANCES ITS ACTIVITY

S.S. KANWAR, R.K. KAUSHAL, A. JAWED, S.S. CHIMNI AND V. PUNJ

Abstract

Bacillus coagulans BTS1 produced an extracellular lipase in mineral based medium containing yeast extract (0.5%, v/v) and cottonseed oil (1%). The lipase was extracted from the harvested broth by ammonium sulphate salting out technique. The lipase was pretreated with each one of the proteases viz. pronase-E, proteinase-K, trypsin and a-chymotrypsin at 37°C for 20 min. The pronase-E and proteinase-K strongly quenched the hydrolytic activity of lipase. Trypsin and a-chymotrypsin-treated lipase rapidly hydrolyzed 4-nitro phenyl palmitate. It was observed that proteolytic digestion of B. coagulans BTS-1 lipase with trypsin as well as a-chymotrypsin enhanced hydrolytic activity by approximately 13-43% in comparison to the untreated bacterial lipase. The activity of pancreatic lipase decreased following treatment with proteases. Moreover, PMSF had little effect on the pancreatic lipase.

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