Lipase immobilized by adsorption: effect of support hydrophobicity on the reaction rate of ester synthesis in cyclohexane

Candida cylindracea lipase was immobilized by adsorption to various hydrophilic and hydrophobic supports and studied with respect to the esterification rates of a primary and a secondary alcohol, respectively, in organic media. The reaction rates were compared with the rate of esterification with "free lipase". When the secondary alcohol, (R,S)-1-phenylethanol, was used the highest reaction rates were measured for lipase adsorbed to the hydrophobic supports. When the primary alcohol, heptanol, was used "free lipase" exhibited the highest reaction rate. A kinetic explanation of these results in proposed.