Purification and characterization of an extracellular lipase from a newly <span style="font-size:14.0pt;line-height:115%;font-family:"Times New Roman"; mso-fareast-font-family:"Times New Roman";color:black;mso-ansi-language:EN-IN; mso-fareast-language:EN-IN;mso-bidi-language:HI" lang="EN-IN">isolated thermophilic <i>Bacillus pumilus</i></span>

Abstract

1213-1217An extracellular lipase was isolated and purified from a bacterium and is the first report on the isolation and purification of lipase from the species B.pumilus. Effect of temperature, pH and composition of culture medium were     optimized for maximum lipase production. The enzyme was purified and the purity was found to be 98%. The Km value of the enzyme was 1.75 x10-2 mg. and it was found to be a monomer by SDS PAGE. This lipase was found to be alkaline and thermostable and was not a metalloprotein as evidenced from EDTA treatment. Immobilized whole cells were found to be more stable than the pure enzyme.</span