PURIFICATION AND BIOCHEMICAL CHARACTERIZATION OF LIPASE FROM BACILLUS PUMILUS DGLU12DEVASENA KANNAN, BADDIREDDI SUBHADRA LAKSHMI AND USHA ANTONY
Lipase from B. pumilus strain DGLU12 was purified and its enzymatic characteristics were studied. The molecular weight of the enzyme was 34 kDa and it showed a single band on SDS-PAGE. The purification steps involved 70 % ammonium sulphate saturation, dialysis and gel filtration chromatography using Sephadex G-100. A purification fold of 36 was achieved following this three step purification that yielded a specific activity of 95.02 U/mg. The purified lipase was analyzed by RP-HPLC to confirm its homogeneity. The pH and temperature for optimum activity of the enzyme was 8 and 30° C respectively. The enzyme exhibited significant stability in nonpolar organic solvents and was found to maintain activity in the presence of polyols especially sorbitol (% RA - 112). The storage stability was better at 4° C and retained its activity for 40 days (RA 95%).
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