Supramolecular immobilization of redox enzymes on cyclodextrin-coated magnetic nanoparticles for biosensing applications

J Colloid Interface Sci. 2012 Nov 15;386(1):181-8. doi: 10.1016/j.jcis.2012.07.050. Epub 2012 Jul 26.

Abstract

Mono-6-formyl-β-cyclodextrin moieties were attached to (3-aminopropyl)triethoxysilane-coated superparamagnetic Fe(3)O(4) nanoparticles by reductive alkylation with NaBH(3)CN. The oligosaccharide-capped core-shell nanoparticles were employed as support for the supramolecular immobilization of two different adamantane-modified enzymes, tyrosinase and xanthine oxidase, through host-guest interactions. The enzyme-modified nanomaterial was further used to magnetically modify carbon paste electrodes for constructing amperometric biosensors toward cathecol and xanthine. The tyrosinase and xanthine oxidase based biosensors showed excellent electroanalytical behaviours, with linear ranges of 100 nM-12 μM cathecol and 5.0-120 μM xanthine, sensitivities of 12 mA/M and 130 mA/M, and low detection limits of 22 nM and 2.0 μM, respectively. The supramolecular nature of the immobilization approach was confirmed by electroanalytical methods.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biosensing Techniques*
  • Enzymes, Immobilized / chemistry*
  • Magnetics*
  • Metal Nanoparticles / chemistry*
  • Oxidation-Reduction
  • beta-Cyclodextrins / chemistry*

Substances

  • Enzymes, Immobilized
  • beta-Cyclodextrins