Characterization of crude lipase from Rhizopus arrhizus and purification of multiplicity forms of the enzyme

Abstract

Some of the biochemical properties of a crude lipase enzyme from Rhizopus arrhizus were determined. The enzyme displayed maximal catalytic activity at pH9.0 and temperature of 35°C. It was stable at basic values of pH and 40°C and in the presence of detergents. Lipase showed substrate specificity against different plant oils. Three multiplicity forms of the enzyme (Lip I, Lip II and Lip III) were isolated by gel chromatography. They differed in their molecular weight (Lip I- 80 000 Da, Lip II- 39 700 Da and Lip III- 6 900 Da) and degree of glycosylation (51.61% for Lip I, 74.17% for Lip II and 55.60% for Lip III). Some of the specific biochemical properties of the multiplicity forms were established. No synergistic effect of the three multiplicity forms of lipase in hydrolysis of olive oil was observed.