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PREPARATION, PURIFICATION AND PROPERTIES OF LIPASE FROM HEPATOPANCREAS OF TRA (PANGASIUS) CATFISH

Thy Bao Vuong 1, *
Lam Bich Tran 2
Duan Luu 3
  1. Cuu Long University
  2. University of Technology, VNU-HCM
  3. Saigon Technology University
Correspondence to: Thy Bao Vuong, Cuu Long University. Email: pvphuc@hcmuns.edu.vn.
Volume & Issue: Vol. 14 No. 3 (2011) | Page No.: 5-11 | DOI: 10.32508/stdj.v14i3.1959
Published: 2011-09-30

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Copyright The Author(s) 2023. This article is published with open access by Vietnam National University, Ho Chi Minh city, Vietnam. This article is distributed under the terms of the Creative Commons Attribution License (CC-BY 4.0) which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. 

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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