A. Taniguchi et al., Purification and properties of lipase from Tilapia intestine - Digestive enzyme of Tilapia - VI, NIP SUIS G, 67(1), 2001, pp. 78-84
Lipase of the intestine of Tilapia nilotica was purified by ammonium sulfat
e precipitation, followed by ion-exchange chromatography (DEAE-cellulose),
chromatofocusing (Polyexchanger PBE 94 ), and gel filtration (Sephadex G-10
0).
The lipase was found to be a single band when examined by electrophoresis.
The specific activity of the purified enzyme was 177 times higher than that
of the crude extract.
The lipase had a molecular weight of 46,000, showed the highest activity at
pH 7.5 and 35 degreesC, and was stable at pH 6.5-8.5 and below 40 degreesC
. The Km of the enzyme for olive oil was calculated to be 0.7 mM. Its activ
ity was inhibited by Cu2+, Cd2+, Ni2+, Hg2+, PCMB, and CH2ICOOH.
This enzyme specifically digested Tributyrin and Tricaproin, whereas it dig
ested 1,2-diolein and 1-monoolein more than 1,3-diolein and 2-monoolein. Th
e enzyme well decomposed soybean oil and coconut oil.