STUDY OF A LIPASE FROM CANDIDA-RUGOSA DIDDENS AND LODDER

Lipasic system of Candida rugosa (CBS 613) strain was studied. The enz yme was purified in one step by hydrophobic chromatography. The proper ties of this lipase were determined. It is an oligomeric enzyme compos ed of five identical monomers of 46 kg . mol-1. Its optimum reaction c onditions are pH = 7 and temperature = 40-degrees-C. This enzyme prese nts a rapid thermal denaturation and then a more stable form. It is a cell-bound lipase which is induced by triacyl glycerols. This enzyme p resents a high specificity for external positions on glycerol.