Lipase immobilized by adsorption

Summary Candida cylindraceae 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 explantation of these results is proposed.