Abstract
A novel extra-cellular lipase from Bacillus coagulans MTCC-6375 was purified 76.4-fold by DEAE anion exchange and Octyl Sepharose chromatography. The purified enzyme was found to be electrophoretically pure by denaturing gel electrophoresis and possessed a molecular mass of approximately 103 kDa. The lipase was optimally active at 45 °C and retained approximately 50% of its original activity after 20 min of incubation at 55 °C. The enzyme was optimally active at pH 8.5. Mg 2+, Cu 2+, Ca 2+, Hg 2+, Al 3+, and Fe 3+ at 1 mM enhanced hydrolytic activity of the lipase. Interestingly, Hg 2+ ions resulted in a maximal increase in lipase activity but Zn 2+ and Co 2+ ions showed an antagonistic effect on this enzyme. EDTA at 150 mM concentration inhibited the activity of lipase but Hg 2+ or Al 3+ (10 mM) restored most of the activity of EDTA-quenched lipase. Phenyl methyl sulfonyl fluoride (PMSF, 15 mM) decreased 98% of original activity of lipase. The lipase was more specific to p-nitrophenyl esters of 8 ( pNPC) and 16 ( pNPP) carbon chain length esters. The lipase had a V max and K m of 0.44 mmol mg −1 min −1 and 28 mM for hydrolysis of pNPP, and 0.7 mmol mg −1 min −1 and 32 mM for hydrolysis of pNPC, respectively.
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