PURIFICATION AND PROPERTIES OF PENICILLIUM SPECIES LIPASE IN AQUEOUS-SOLUTIONS AND IN REVERSED MICELLES IN BENZENE

Lipase has been purified from Penicillium sp. using gel filtration on Sephadex G-75 (Superfine). The hydrolytic properties of the purified e nzyme in aqueous solutions and in Triton X-100 reversed micelles in be nzene were investigated. In the reversed micelles the enzyme is 50-fol d more active than in water (maximal rate per mg enzyme) and the pH op timum for hydrolytic activity is shifted towards more acidic pH (from 9.2 and 7.5). The synthetase activity of the enzyme in aqueous solutio ns and in AOT (sulfosuccinic acid diisooctyl ester sodium salt) revers ed micelles in benzene was also investigated. In both systems the enzy me catalyzed glyceride synthesis from glycerol and oleic acid.