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