Purification of a Novel Thermophilic Lipase from B. licheniformis MTCC-10498

Lipases have emerged as one of the leading biocatalysts with proven potential for contributing to the multibillion dollar underexploited lipid technology bio-industry and have been used in situ lipid metabolism and ex situ multifaceted industrial applications. For certain applications, such as synthetic reactions in pharmaceutical industry, further purification is needed. Since lipases are known to be hydrophobic in nature, having large hydrophobic surfaces around the active site, the purification of lipases may best be achieved by opting for affinity chromatography, such as hydrophobic interaction chromatography. The purification of bacterial lipase was performed using techniques of ammonium sulphate salting out, dialysis and hydrophobic interaction chromatography (Octyl sepharose) respectively. The analysis of bacterial lipase under reducing and denaturing SDS- PAGE (polyacrylamide gel electrophoresis) revealed that the purified lipase possessed a single band of MW 19kDa as visualized with Coomasie Brilliant Blue R-250.