PRETREATMENT OF LIPASE FROM BACILLUS COAGULANS BTS-1 WITH PROTEASES ENHANCES ITS ACTIVITYS.S. KANWAR, R.K. KAUSHAL, A. JAWED, S.S. CHIMNI AND V. PUNJ
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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