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PREPARATION, PURIFICATION AND PROPERTIES OF LIPASE FROM HEPATOPANCREAS OF TRA (PANGASIUS) CATFISH
Author(s) -
Thy Bao Vuong,
Lam Bich Tran,
Duan Luu
Publication year - 2011
Publication title -
science and technology development journal
Language(s) - English
Resource type - Journals
ISSN - 1859-0128
DOI - 10.32508/stdj.v14i3.1959
Subject(s) - chromatography , lipase , catfish , chemistry , size exclusion chromatography , sephadex , hepatopancreas , fractionation , pangasius , enzyme , biochemistry , biology , fishery , fish <actinopterygii>
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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