Immobilization of lipase on a hydrophobic zeolite type Y

Abstract

Lipase from Candida cylindracea was immobilized by adsorption on a hydrophobic zeolite type Y. The maximal amount of bound protein of 8.2 mg g(-1) and an immobilization efficiency of 33% were achieved under optimum conditions. The kinetics of lipase binding to the zeolite were assessed using a general model of topochemical reactions. Based on the values of the parameters of the specific kinetic model, we propose that the adsorption process is controlled by surface kinetics. This was later experimentally confirmed. The activation energy for lipase adsorption on the zeolite is 43 kJ mol(-1).