Candida rugosa lipase immobilized on diethylaminoethyl-cellulose (Deae) for esterification of butyl oleate

Abstract

Lipase from Candida rugosa was immobilized onto diethylaminoethyl-cellulose (DEAE) through physical adsorption method with high percentage of protein absorption obtained at 84%. The lipase-DEAE was used to catalyze the enzymatic esterification of butyl oleate by reacting oleic acid and butanol in hexane. Butyl oleate, an alkylic ester of long-chain fatty acid is now in high demand to produce biodiesel. The effect of reaction temperature, thermostability of the immobilization lipase, stability in organic solvent, leaching with hexane and storage studies under various conditions of immobilized lipase were investigated. The optimum esterification was found to be up to 90% yield. Only a slight of lipase leached out after being washed by 20 mL of hexane. This showed that lipases were strongly attached to the DEAE support via physical adsorption method, and it could be used as industrial biocatalyst.