Bovine pancreatic lipase: Purification and applications in immobilized form for transesterification reactions

The purification of lipase from bovine pancreas is described The final prod uct was homogeneous as determined by electrophoresis in denaturing polyacry lamide gels showing a single protein band with a molecular weight of 47 kDa The procedure involves the preparation of acetone powder from fresh pancre as, ammonium sulphate precipitation, chromatography on DEAE-Sephadex and ge l filtration on Sephadex G-100. Optimal activity occurred at pH 9.0 using p -nitrophenyl laurate as a substrate emulsified with polyvinylalcohol for th e assay of enzyme activity. The purified lipase is immobilized on phenolic resin and utilized for transesterification reactions in dry pyridine.