ENZYMATIC-SYNTHESIS OF FATTY ESTERS BY HYDROPHOBIC LIPASE DERIVATIVESIMMOBILIZED ON ORGANIC POLYMER BEADS

Lipase from Candida rugosa was modified with several hydrophobic modif iers before being adsorbed onto organic polymer beads. The effects of different enzyme modifiers, supports, solvents, reaction temperatures, fatty acids, and alcohols on the activity of the immobilized enzyme w ere investigated. The immobilized lipases were good biocatalysts for e sterification reactions in organic solvents. They exhibited high activ ities in all solvents tested, including polar solvents. The activity s eemed to depend on the type of support rather than on the modifier of the enzyme. The medium polar support, XAD7, appeared to be the best fo r the modified lipases. The immobilized lipase favored the medium-chai n fatty acids rather than the long-chain fatty acids as acyl donors. T he alcohol selectivity of the enzyme was unchanged upon immobilization . The native and immobilized lipases favored the short-chain and terpe ne alcohols as nucleophiles.