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Electrocatalysis of Horseradish Peroxidase Immobilized on Cobalt Nanoparticles Modified ITO Electrode

机译:钴纳米粒子修饰ITO电极固定化辣根过氧化物酶的电催化

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It is the first time that Horseradish peroxidase (HRP) was successively immobilized on the magnetic cobalt nanoparticles modified ITO (indium tin oxide) electrode.Morphologies of electrode surface were featured by the field emission-scanning electron microscope (FSEM).Cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS) were used to characterize the modified process of electrode.Direct electrochemistry and electrocatalysis of HRP immobilized on nano-Co/ITO were investigated.The biosensor exhibited high sensitivity,good stability,and excellent electrocatalytic activity to the reduction of H2O2.Under the optimized experimental conditions,a calibration curve over 2.0 x 10~(-9) ~2.0 x 10~(-8) mol l~(-1) and 2.0 x 10~(-7)~2.0 x 10~(-6) mol l~(-1),with a limit of detection of 1.9 x 10~(-9) mol l~(-1) was obtained.The apparent Michaelis-Menten constant (K_M~(APP)) for HRPano-Co/ITO electrode was calculated to be 0.79 mmol l~(-1),indicating a higher affinity of HRP attached on the modified electrode.
机译:这是首次将辣根过氧化物酶(HRP)固定在磁性钴纳米粒子修饰的ITO(铟锡氧化物)电极上。场发射扫描电子显微镜(FSEM)表征了电极表面的形貌。循环伏安法(CV) )和电化学阻抗谱(EIS)表征电极的修饰过程。研究了直接固定在纳米Co / ITO上的HRP的直接电化学和电催化作用。在最佳实验条件下,在2.0 x 10〜(-9)〜2.0 x 10〜(-8)mol l〜(-1)和2.0 x 10〜(-7)〜2.0 x 10范围内的校准曲线获得〜(-6)mol l〜(-1),检出限为1.9 x 10〜(-9)mol l〜(-1)。表观Michaelis-Menten常数(K_M〜(APP)) HRP / nano-Co / ITO电极的H2O为0.79 mmol l〜(-1),表明HRP的亲和力更高修改后的电极上。

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