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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.
