Glucose oxidase 효소 전극 제조 : 물리적 방법에 의한 효소의 고정화

Abstract

Purified glucose oxidase from Penicillium verruculosum was immobilized by physical methods such as physical entrapment in a polyacrylamide gel or adsorption onto insoluble matrix. Construction of the enzyme electrode was carried out using the immobilized glucose oxidase, and catalytic parameters as well as functional stability of the immobilized enzyme were monitored by oxygen electrode. Due to diffusional restriction of substrate, the observed $K_m$ values of immobilized enzyme by physical entrapment were higher than that of soluble enzyme. However, in case of immobilized enzymes by physical adsorption, the $K_m$ values were lowered compared to that of soluble enzyme. Optimal pH for the glucose oxidase activity was shifted toward acidic or neutral side with more extended pH range as a result of immobilization and thermal stability of the catalytic function was also greatly improved after immobilization of the enzyme.