Characterization and utilization of Candida rugosa lipase immobilized on controlled pore silica

Candida rugosa lipase was immobilized by covalent binding on controlled por e silica (CPS) using glutaraldehyde as cross-linking agent under aqueous an d nonaqueous conditions. The immobilized C. rugosa was more active when the coupling procedure was performed in the presence of a nonpolar solvent, he xane. Similar optima pH (7.5-8.0) was found for both free and immobilized l ipase. The optimum temperature for the immobilized lipase was about 10 degr ees C higher than that for the free lipase. The thermal stability of the CP S lipase was also greater than the original lipase preparation. Studies on the operational stability of CPS lipase revealed good potential for recycli ng under aqueous (olive-oil hydrolysis) and nonaqueous (butyl butyrate synt hesis) conditions.