Colloidal gold as a biocompatible immobilization matrix suitable for the fabrication of enzyme electrodes by electrodeposition.

Published

Journal Article

Glucose oxidase, horseradish peroxidase, xanthine oxidase, and carbonic anhydrase have been adsorbed to colloidal gold sols with good retention of enzymatic activity. Adsorption of xanthine oxidase on colloidal gold did not result in a change in enzymatic activity as determined by active site titration with the stoichiometric inhibitor pterin aldehyde and by measurement of the apparent Michaelis constant (K'(M)). Gold sols with adsorbed glucose oxidase, horseradish peroxidase, and xanthine oxidase have also been electrodeposited onto conducting matrices (platinum gauze and/or glassy carbon) to make enzyme electrodes. These electrodes retained enzymatic activity and, more importantly, gave an electrochemical response to the enzyme substrate in the presence of an appropriate electron transfer mediator. Our results demonstrate the utility of colloidal gold as a biocompatible enzyme immobilization matrix suitable for the fabrication of enzyme electrodes.

Full Text

Duke Authors

Cited Authors

  • Crumbliss, AL; Perine, SC; Stonehuerner, J; Tubergen, KR; Zhao, J; Henkens, RW; O'Daly, JP

Published Date

  • August 1992

Published In

Volume / Issue

  • 40 / 4

Start / End Page

  • 483 - 490

PubMed ID

  • 18601142

Pubmed Central ID

  • 18601142

Electronic International Standard Serial Number (EISSN)

  • 1097-0290

International Standard Serial Number (ISSN)

  • 0006-3592

Digital Object Identifier (DOI)

  • 10.1002/bit.260400406

Language

  • eng