Novel enzyme biosensor for hydrogen peroxide via supramolecular associations

Biosens Bioelectron. 2009 Mar 15;24(7):2028-33. doi: 10.1016/j.bios.2008.10.008. Epub 2008 Oct 22.

Abstract

A polythiolated-beta-cyclodextrin polymer was synthesized and used as a coating material for gold electrodes. The functionalized electrodes were employed for immobilizing adamantane-modified horseradish peroxidase via supramolecular associations. The enzyme-containing electrode was used as an amperometric biosensor device with 1mM hydroquinone as electrochemical mediator. The biosensor exhibited a fast amperometric response (10s), a good linear response toward H(2)O(2) concentrations between 28 microM and 5.5 mM, and a low detection limit of 7 microM. The biosensor showed a sensitivity of 109 microA/Mcm(2) and retained 98% of its initial electrocatalytic activity after 40 days of storage at 4 degrees C in 50mM sodium phosphate buffer pH 7.0. The host-guest supramolecular nature of the immobilization method was confirmed by cyclic voltammetry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biosensing Techniques / instrumentation*
  • Electrochemistry / instrumentation*
  • Electrodes*
  • Enzymes, Immobilized / chemistry
  • Equipment Design
  • Equipment Failure Analysis
  • Horseradish Peroxidase / chemistry*
  • Hydrogen Peroxide / analysis*
  • Hydrogen Peroxide / chemistry
  • Macromolecular Substances / analysis
  • Macromolecular Substances / chemistry
  • Reproducibility of Results
  • Sensitivity and Specificity

Substances

  • Enzymes, Immobilized
  • Macromolecular Substances
  • Hydrogen Peroxide
  • Horseradish Peroxidase