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PRODUCTION AND CHARACTERIZATION OF AN EXTRACELLULAR THERMOSTABLE LIPASE FROM A THERMOPHILIC BACILLUS SP.

The objective of this study was to isolate and characterize thermostable microbial lipases. An enrichment culture technique was used to enrich for thermophiles capable of utilizing olive oil as a carbon source. Out of 44 initial isolates, strain H1, which exhibits the highest lipase activity, was chosen for further characterization. Strain H1 was a spore forming rod, capable of growing at 65°C and was assigned as a Bacillus sp. Optimal lipase production was on medium containing 1 % Tween 80. Lipase H1 was partially purified by acetone precipitation, anion exchange chromatography and gel filtration. The enzyme has a molecular weight of 20,000 (based on gel filtration) and is most active at pH 7.0 at 70°C with a half-life of 50 h at 60°C. Lipase H1 had no apparent requirement for cofactors and its activity was completely inhibited in the presence of 1 mm HgCl 2 . The best substrates for the enzyme were short-chain fatty acid esters. With β-naphthyl caprylate as a substrate, the enzyme has a K m of 0.02 mM