Physicochemical Properties of Mono- and Diacylglycerol Lipase from Penicillium camembertii

Abstract

In the course of investigations on the enzymatic synthesis of monoglycerides and the partial hydrolysis of glycerides, Yamaguchi and Mase found a newlipase havingstrict specificity to mono- and diacylglycerols but not to triacylglycerols in the culture broth of Penicillium camembertii U-150 (1). The newlipase was purified into four active fractions by a procedure involving ethanol precipitation, ammanium sulfate fractionation, and aminooctyl-Sepharose, hydroxyapatite and concanavalin A-Sepharose (con A Sepharose) column chromatographies. One active fraction, enzyme 1, was not adsorbed on con A-Sepharose but others, enzymes 2- 4, were adsorbed on con A Sepharose and separated into three active fractions by linear gradient elution with Methyl-X-D-glycopyranoside. No significant difference was observed in substrate specificity among enzymes 1-4, but other enzymatic properties, e. g., pH and heatstabilities, and optimum pH and temperature, were clearly different between enzyme 1 and three adsorbed components (three adsorbed components weresimilar to each other)(2). In oder to elusidate multiple forms of this enzyme, the physicochemical properties were compared among four active components.