Issue 99, 2014

Simple approach for the immobilization of horseradish peroxidase on poly-l-histidine modified reduced graphene oxide for amperometric determination of dopamine and H2O2

Abstract

In this work, immobilization of horseradish peroxidase (HRP) on poly-L-histidine (P-L-His) modified reduced graphene oxide (RGO) was demonstrated. The HRP/P-L-His-RGO bio-nanocomposite film was prepared through layer-by-layer (LBL) assembly. Scanning electron microscopy, Fourier transform infrared spectroscopy, electrochemical impedance spectroscopy, and UV-Vis spectroscopy were adopted to monitor the uniformity of the LBL assembly of the HRP/P-L-His-RGO bio-nanocomposite film. The immobilized HRP exhibited excellent electrocatalytic activity towards the reduction of hydrogen peroxide (H2O2). The catalysis currents showed a linear relationship with H2O2 concentration, ranging from 0.2 to 5000 μM. The detection limit (S/N = 3) of H2O2 was 0.05 μM. The apparent Michaelis–Menten constant (Km) was calculated to be 1.2 mM. Moreover, the modified electrode displayed a rapid response (5 s) to H2O2 with good stability and reproducibility. Based on the HRP/P-L-His-RGO bio-nanocomposite film, a third-generation reagentless biosensor was constructed for the determination of H2O2.

Graphical abstract: Simple approach for the immobilization of horseradish peroxidase on poly-l-histidine modified reduced graphene oxide for amperometric determination of dopamine and H2O2

Supplementary files

Article information

Article type
Paper
Submitted
21 Aug 2014
Accepted
06 Oct 2014
First published
07 Oct 2014

RSC Adv., 2014,4, 55867-55876

Author version available

Simple approach for the immobilization of horseradish peroxidase on poly-L-histidine modified reduced graphene oxide for amperometric determination of dopamine and H2O2

A. T. E. Vilian and S. Chen, RSC Adv., 2014, 4, 55867 DOI: 10.1039/C4RA09011J

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