摘要
用电化学方法将黄嘌呤氧化酶固定在聚苯胺中以制成聚苯胺黄嘌呤氧化酶电极.该电极呈现典型的酶催化反应动力学特性.且具有快速的生物电化学响应.固定化黄嘌呤氧化酶的表观米氏常数为21×10^(-6)mol·dm^(-3),最适pH为8,4,酶催化反应的活化能为85.1kJ·mol^(-1).酶电极具有较高的稳定性.使用聚苯胺黄嘌呤氧化酶电极能可靠地测定较低的底物浓度,如2×10^(-6)mol·dm^(-3)黄瞟呤.
The catalytic action of the polyaniline xanthine oxidase electrode, which was formed by immobilization of xanthine oxidase on the polyaniline film using the electrochemical method, has kinetic characteristics of the typical enzyme-catalyzed reaction. The enzyme electrode has a very fast bioelectrochemical response and high stability. The apparent Michaelis constant, optimum pH and activation energy for the immobilized xanthine oxidase are 21× 10-6mol· dm-3, 8.4 and 85.1kJ · mol-1, respectively. At a very low concentration of the substrate, such as 2×10-6mol·dm-3, xanthine can be determined reliably by using a polyaniline oxidase electrode.
出处
《化学学报》
SCIE
CAS
CSCD
北大核心
1995年第6期521-525,共5页
Acta Chimica Sinica
