98
Views
11
CrossRef citations to date
0
Altmetric
Chemical and Biosensors

Electrocatalysis of Horseradish Peroxidase Immobilized on Cobalt Nanoparticles Modified ITO Electrode

, , &
Pages 3182-3194 | Received 24 Aug 2006, Accepted 10 Sep 2007, Published online: 04 Feb 2008
 

Abstract

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 2.0×10−9∼2.0×10−8 mol l−1 and 2.0×10−7∼2.0×10−6 mol l−1, with a limit of detection of 1.9×10−9 mol l−1 was obtained. The apparent Michaelis‐Menten constant (K M app ) for HRP/nano‐Co/ITO electrode was calculated to be 0.79 mmol l−1, indicating a higher affinity of HRP attached on the modified electrode.

The National Natural Science Foundation of China (Nos. 20275007) is gratefully acknowledged.

Log in via your institution

Log in to Taylor & Francis Online

PDF download + Online access

  • 48 hours access to article PDF & online version
  • Article PDF can be downloaded
  • Article PDF can be printed
USD 61.00 Add to cart

Issue Purchase

  • 30 days online access to complete issue
  • Article PDFs can be downloaded
  • Article PDFs can be printed
USD 768.00 Add to cart

* Local tax will be added as applicable

Related Research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.