Functional immobilization of lipase eliminating lipolysis product inhibition.

Lipase from Pseudomonas fluorescens biotype I was immobilized on macroporous anion exchange resin using glutaraldehyde to enhance the adsorption. The immobilization method was selected, because it provided the highest extent of hydrolysis of beef tallow at high substrate concentrations. The immobilized lipase was not substantially inhibited by oleic acid or sodium oleate, but the soluble lipase was strongly inhibited by both substances. The optimum pH of lipolysis was pH 4 for the immobilized lipase and pH 6 for the soluble one. These results indicate that the microenvironment created around the lipase molecule by immobilization eliminates product inhibition. In addition, the immobilization on the support enhances the stability of the lipase against chemical denuaturation. (c) 1992 John Wiley & Sons, Inc.