IMMOBILIZATION OF HYDROPHOBIC LIPASE DERIVATIVES ON TO ORGANIC POLYMER BEADS

A simple and effective method of lipase immobilization is described. L ipase from Candida rugosa was first modified with several hydrophobic modifiers before being adsorbed on to organic polymer beads. The solub le hydrophobic lipase derivatives adsorbed more strongly on to the var ious polymers as compared with the native lipase. The optimal adsorpti on temperature of the native and modified lipases on all the polymers was 40 degrees C. The optimal pH of adsorption was between 6 and 7. Li pase immobilized in this manner produced high catalytic recoveries whi ch were affected by the type of modifiers, degree of modification and type of supports used. Monomethoxypolyethylene glycol (1900) activated with p-nitrophenyl chloroformate was found to be the best modifier of the enzyme at 95% modification, for adsorption to the polymers. Incre asing the degree of modification of the enzyme increased the activity which was immobilized. Generally, both native and hydrophobic lipase d erivatives showed higher specific activities when immobilized on polar polymers compared with non-polar polymers.