Abstract
Lipase from the hepatopancreas of Tra (Pangasius) catfish was purified by ammonium sulfate fractionation, followed by ion-exhange chromatography on DEAE Cellulose and gel filtration Sephadex G-75. The preparation was homogeneous on polyacrylamide disc gel electrophoresis. The specific activity of the purified enzyme was 37.95 times higher than that of the crude extract. The enzyme showed a molecular weight of 57000 Da. The pH and temperature optima of purified lipase were 8 and 500C respectively. Enzyme activity was enhanced by Ca2+ but inhibited by heavy metals Zn2+, Cd2+, Mg2+.
Highlights
Lipases are enzymes that catalyze the hydrolysis of triacylglycerols at the oil-water interface to release glycerol and free fatty acids
The present paper focuses on the purification of Tra (Pangasius) pancreatic lipase and the effects of temperature, pH and metal ions on the enzyme activity
The pure enzyme has a molecular weight of 57 Kda
Summary
3.1.1.3) are enzymes that catalyze the hydrolysis of triacylglycerols at the oil-water interface to release glycerol and free fatty acids. Lipases are finding increasing uses as food and other industrial processing aids, there is growing interest in discovering new sources of these enzymes with appropriate characteristics to suit particular applications. The few lipases that have been studied from fish and other aquatic animals include lipases from the leopard shark (Patton et al, 1977), Atlantic cod (Lie and Lambersten, 1985; Gjellesvik et al, 1992), dog fish (Raso and Hultin, 1988), sardine (Mukundan et al, 1985), anchovy, striped bas and salmon (Lager et al, 1977). The present paper focuses on the purification of Tra (Pangasius) pancreatic lipase and the effects of temperature, pH and metal ions on the enzyme activity
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