Search. Read. Cite.

Easy to search. Easy to read. Easy to cite with credible sources.

Asian Journal of Biochemistry

Year: 2008  |  Volume: 3  |  Issue: 4  |  Page No.: 243 - 255

Isolation, Purification and Characterization of Lipase from Grey Mullet (Liza parsia Hamilton, 1822)

M.A. Islam, N. Absar and Abdus Salam Bhuiyan

Abstract

Two lipases designated as Lip-1 and Lip-2 were purified from dorsal part of grey mullet (Liza parsia) to homogeneity by 85% (NH4)2SO4 fractionation followed by simultaneous desalting and concentration by ultrafiltration and Sephadex G-50 and DEAE-cellulose chromotography and CM-cellulose chromotography. The molecular weight of two lipases was determined by SDS-PAGE and gel filtration about 46.5 and 41.2 KDa, respectively. Both the enzymes were dimer in nature remained unchanged the presence and absence of reducing agent under SDA-PAGE. The Lip-1 and Lip-2 lipases were active within the pH range of 7-8.5, with an optimum pH of 8 and 8.5.0 and were stable from 2.0-10.5. The enzyme was active within the temperature range of 30-60°C and maximum activities were observed around 33 and 35°C, respectively and beyond which it lost activity progressively. The hydrolytic activity was enhanced by Ca+ and EDTA (concentration 0.001-0.003 M) but strongly inhibited by heavy metal s Cd++, Zn++ and Hg++. The presence of Zn++ and Hg++ potently inhibited lipolytic activities of the lipases from grey mullet, while activities were slightly inhibited in the presence of Cu++ salts.

Cited References Fulltext