Tirkeş S, Toppare L, Alkan S, Bakir U, Onen A, Yağci Y
Department of Chemistry, Middle East Technical University, Ankara, Turkey.
Int J Biol Macromol. 2002 Apr 8;30(2):81-7. doi: 10.1016/s0141-8130(02)00011-9.
Glucose oxidase (GOD) was immobilized in four different conducting polymer matrices, namely: polypyrrole, (PPy), poly(pyrrole-graft-polytetrahydrofuran), (1) and (3); and poly(pyrrole-graft-polystyrene/polytetrahydrofuran), (2). The kinetic parameters V(max) and K(m), and the optimum temperature were determined for both immobilized and native enzymes. The effect of electrolysis time and several supporting electrolytes, p-toluenesulfonic acid, p-toluene sulfonic acid (PTSA), sodium p-toluene sulfonate, sodium p-toluene sulfonate (NaPTS), and sodium dodecyl sulfate, sodium dodecyl sulfate (SDS), on enzyme immobilization were investigated. The high K(m) value (59.9 mM) of enzyme immobilized in PPy was decreased via immobilization in graft copolymer matrices of pyrrole. V(max), which was 2.25 mM/min for pure PPy, was found as 4.71 mM/min for compound (3).
葡萄糖氧化酶（GOD）被固定在四种不同的导电聚合物基质中，即：聚吡咯（PPy）、聚（吡咯接枝聚四氢呋喃）（1）和（3）；以及聚（吡咯接枝聚苯乙烯/聚四氢呋喃）（2）。测定了固定化酶和天然酶的动力学参数V(max)和K(m)以及最适温度。研究了电解时间和几种支持电解质对甲苯磺酸、对甲苯磺酸钠（NaPTS）和十二烷基硫酸钠（SDS）对酶固定化的影响。固定在PPy中的酶的高K(m)值（59.9 mM）通过固定在吡咯的接枝共聚物基质中而降低。纯PPy的V(max)为2.25 mM/min，化合物（3）的V(max)为4.71 mM/min。
