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Studies on electrocatalytical kinetic behavior of horseradish peroxidase and assay for hydrogen peroxide at salt bridge supported bilayer lipid membrane

机译：辣根过氧化物酶的电催化动力学行为及盐桥负载双层脂质膜上过氧化氢的测定

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This article reports on the electrochemical behavior relative to the Fe(III)-Fe(II) conversion, of horseradish peroxidase (HRP) incorporated in a salt bridge-supported bilayer lipid membrane (sb-BLM) modified with lauric acid (LA). The incorporation of HRP was achieved by electrostatic interaction between HRP and LA anion sites in the sb-BLM, which results in the enhancement of the electron exchange between the protein and the electrode surface. A quasireversible electron transfer was observed even in the absence of mediators. A novel and biological compatible biosensor was constructed. The electrocatalytically kinetic behavior of HRP was investigated with this biosensor. Furthermore, the cathodic peak current (I-pc) of HRP was increased in the presence of hydrogen peroxide, the intensity of which is strictly dependent on the concentration of hydrogen peroxide. The relationship is DeltaI(pc)(A)=[1.215 InCH2O2(mmol L-1)+ 1.018]x 10(-7). The effects of the coexisting substances and the pH values on the response of the biosensor were also investigated for optimum analytical performance. [References: 25]
机译：本文报道了辣根过氧化物酶（HRP）相对于Fe（III）-Fe（II）转化的电化学行为，该酶掺入用月桂酸（LA）修饰的盐桥支撑双层脂质膜（sb-BLM）中。 HRP的掺入是通过sb-BLM中HRP和LA阴离子位点之间的静电相互作用实现的，这导致了蛋白质与电极表面之间电子交换的增强。即使在没有介体的情况下，也观察到准可逆的电子转移。构建了一种新型的生物相容的生物传感器。用该生物传感器研究了HRP的电催化动力学行为。此外，HRP的阴极峰值电流（I-pc）在过氧化氢的存在下增加，其强度严格取决于过氧化氢的浓度。关系为：DeltaI（pc）（A）= [1.215 InCH2O2（mmol L-1）+ 1.018] x 10（-7）。为了获得最佳分析性能，还研究了共存物质和pH值对生物传感器响应的影响。 [参考：25]

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