Stability of immobilized α‐chymotrypsin

Abstract

Abstract The thermal of free and immobilized α‐chymotrypsin was investigated experimentally and theoretically. The inactivation process of free α‐chymotrypsin was analyzed with a kinetic model which included a first‐ order reaction process and autolysis. The effects of ionic strength, Ca 2+ concentration, and temperature are discussed here in terms of the estimated kinetic parameters included in this model. The inactivation process of α‐chymotrypsin immobilized onto various supports by several methods was investigated. The Contribution of thermal denaturation and autolysis to the inactivation depended upon the method of immobilization. To interpret quantitatively the non‐first‐order thermal denaturation process of the immobilized enzyme, a model in which the heterogeneity of the immobilized enzyme was taken into account is proposed.