Purification and characterization of a low molecular mass alkaliphilic lipase of Bacillus cereus MTCC 8372
Verma, M. L. and Kanwar, S. S. 2010, Purification and characterization of a low molecular mass alkaliphilic lipase of Bacillus cereus MTCC 8372, Acta microbiologica et immunologica hungarica, vol. 57, no. 3, pp. 191-207.
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A low molecular mass alkaliphilic extra-cellular lipase of Bacillus cereus MTCC 8372 was purified 35-fold by hydrophobic interaction (Octyl-Sepharose) chromatography. The purified enzyme was found to be electrophoretically pure by denaturing gel electrophoresis and possessed a molecular mass of approximately 8 kDa. It is a homopentamer of 40 kDa as revealed by native-PAGE. The lipase was optimally active at 55 °C and retained approximately half of its original activity after 40 min incubation at 55 °C. The enzyme was maximally 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 synergized and Zn 2+ and Co 2+ ions antagonized the lipase activity. Among surfactants, Tween 80 promoted the lipase activity. Phenyl methyl sulfonyl fluoride (PMSF, 15 mM) decreased 98% of original activity of lipase. The lipase was highly specific towards p -nitrophenyl palmitate and showed a Vmax and Km of 0.70 mmol.mg −1 .min −1 and 32 mM for hydrolysis of p NPP.
Field of Research
069999 Biological Sciences not elsewhere classified
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