[Lipolytic complex of Penicillium sp]

By gel filtration on Sephadex G-75 it has been demonstrated that the lipolytic complex of Penicillium sp. contains two active components--a high molecular weight (lipase-1) and low molecular weight component (lipase-2). Both components have been isolated by Sephadex gel-filtration and DEAE-cellulose chromatography. It has been shown by discelectrophoresis and isoelectric focusing that lipase-2 is a highly purified protein with the molecular weight of 30,000 (gel-filtration) or 29,000 (electrophoresis) and isoelectric point at pH 4.8 Lipase-1 has been found to contain large quantities of lipids. The conditions of deaggregation of a high molecular weight component have been identified to yield a new active component corresponding to lipase-2 in its gel-filtration and disc-electrophoresis properties. It has been shown that pH 7.5-8.0 and temperature 37-40 degrees are optimal for both lipase-1 and lipase-2. Activities of the two components are inhibited by Na deoxycholate and remain unchanged in the presence of Na cholate and dehydrocholate. On the basis of these findings it is concluded that lipase-1 and lipase-2 are two forms of the same enzyme.