Preparation, purification and properties of lipase from hepatopancreas of Tra (pangasius) catfish.

  • Vương Bảo Thy
  • Trần Bích Lam
  • Lưu Duẩn

Abstract

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+.

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Published
2012-12-06
Issue
Vol. 14 No. 3K (2011)
Section
ARTILES
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