Issue 2, 1993

Enzyme catalysis at hydrogel-modified electrodes with redox polymer mediator

Abstract

Direct electrical communication between a new acrylamide–acrylic acid ferrocence copolymer and the enzyme cofactor FADH2 of glucose oxidase is demonstrated. Subsequent catalysis for the anaerobic oxidation of glucose at the co-reticulated enzyme–polymer-modified electrode is shown for polymer-coated glassy carbon and for a composite carbon-paste electrode. A theoretical framework for the kinetic analysis of the reagentless amperometric enzyme electrode is outlined and the model is validated with experimental results. Based on this analysis, kinetic data for the ping-pong glucose oxidase mechanism are discussed for the immobilized enzyme. A comparison of immobilized enzyme electrodes is presented with a redox polymer and soluble substituted-ferrocene redox mediator of similar formal redox potential.

Article information

Article type
Paper

J. Chem. Soc., Faraday Trans., 1993,89, 377-384

Enzyme catalysis at hydrogel-modified electrodes with redox polymer mediator

E. J. Calvo, C. Danilowicz and L. Diaz, J. Chem. Soc., Faraday Trans., 1993, 89, 377 DOI: 10.1039/FT9938900377

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements