KINETIC-PROPERTIES OF SOLUBLE AND IMMOBILIZED CANDIDA-RUGOSA LIPASE

Immobilized lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) from Candida rugosa has been immobilized on commercially available micropor ous polypropylene and used for the batch hydrolysis of different anima l fats. The effect of the reaction products at concentrations similar to those obtained at 90% hydrolysis, both on soluble and immobilized l ipase, was studied. Glycerol showed low inhibitory effect but oleic ac id caused 50% inhibition. A mixture of free fatty acids present in the complete hydrolysis of beef tallow inhibited lipase activity more tha n 70%. The stability of the enzyme (both soluble and immobilized) was highest in the presence of 20% isooctane. The apparent Michaelis const ant for each substrate for the soluble enzyme did not change on immobi lization.