Purification and properties of lipase from Tilapia stomach - Digestive enzyme of Tilapia - VII

Lipase of the stomach of Tilapia nilotica was purified by ammonium sulfate precipitation, followed by chromatofocusing (Polyexchanger PBE 94), and gel filtration (Sephadex G-100), The lipase was found to be a single band when examined by electrophoresis. The specific activity of the purified enzyme was 19 times higher than that of the crude extract. The lipase had a molecular weight of 54,000, showed the optimum activity at pH 6.5 and 40 degreesC, and was stable at pH 5.0-7.0 and below 50 degreesC . The Km of the enzyme for olive oil was calculated to be 0.6 mM. Its activ ity was inhibited by Cu2+, Cd2+, Pb2+, Hg2+, Ni2+, PCMB, and EDTA. This enzyme hydrolyzed triacylglycerol more than diacylglycerol and monoacy lglycerol. The enzyme hydrolyzed soybean oil well.