A. Taniguchi et al., Purification and properties of lipase from Tilapia stomach - Digestive enzyme of Tilapia - VII, NIP SUIS G, 67(1), 2001, pp. 96-101
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.