PREPARATION, PURIFICATION AND PROPERTIES OF LIPASE FROM HEPATOPANCREAS OF TRA (PANGASIUS) CATFISH
2011 ◽
Vol 14
(3)
◽
pp. 5-11
Keyword(s):
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+.
1981 ◽
Vol 27
(10)
◽
pp. 1053-1059
◽
1973 ◽
Vol 51
(11)
◽
pp. 1551-1555
◽
1979 ◽
Vol 34
(9-10)
◽
pp. 726-737
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