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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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Article Details
Issue: Vol 14 No 3 (2011)
Page No.: 5-11
Published: Sep 30, 2011
Section: Engineering and Technology - Research article
DOI: https://doi.org/10.32508/stdj.v14i3.1959
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Copyright: The Authors. This is an open access article distributed under the terms of the Creative Commons Attribution License CC-BY 4.0., which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
How to Cite
Vuong, T., Tran, L., & Luu, D. (2011). PREPARATION, PURIFICATION AND PROPERTIES OF LIPASE FROM HEPATOPANCREAS OF TRA (PANGASIUS) CATFISH. Science and Technology Development Journal, 14(3), 5-11. https://doi.org/https://doi.org/10.32508/stdj.v14i3.1959
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