The University of Southampton
University of Southampton Institutional Repository

There is no evidence to support literature claims of direct electron transfer (DET) for native glucose oxidase (GOx) at carbon nanotubes or graphene

There is no evidence to support literature claims of direct electron transfer (DET) for native glucose oxidase (GOx) at carbon nanotubes or graphene
There is no evidence to support literature claims of direct electron transfer (DET) for native glucose oxidase (GOx) at carbon nanotubes or graphene
It is widely claimed that native GOx undergoes direct electron transfer (DET) at nanostructured electrodes. In this paper we argue that the vast majority, if not all, of these claims are incorrect. We present results for GOx adsorbed on MWCNTs, a typical nanostructured electrode. We show that the surface redox peaks usually attributed to DET to GOx actually arise from flavin, and possibly catalase, impurities present in the as supplied commercial enzyme that are adsorbed at the electrode surface. We show that the observed response to glucose is due to enzymatic activity, but not electroactivity, of adsorbed GOx that catalyses the reaction of D-glucose with dissolved oxygen leading to a decrease in the oxygen reduction current that correlates with the glucose concentration.
Enzyme electrochemistry, glucose oxidase, direct electron transfer
1572-6657
26-37
Bartlett, Philip N.
d99446db-a59d-4f89-96eb-f64b5d8bb075
Al-Lolage, Firas A.
83184275-ce0e-4887-aee4-4b4c81bf7c06
Bartlett, Philip N.
d99446db-a59d-4f89-96eb-f64b5d8bb075
Al-Lolage, Firas A.
83184275-ce0e-4887-aee4-4b4c81bf7c06

Bartlett, Philip N. and Al-Lolage, Firas A. (2018) There is no evidence to support literature claims of direct electron transfer (DET) for native glucose oxidase (GOx) at carbon nanotubes or graphene. Journal of Electroanalytical Chemistry, 819, 26-37. (doi:10.1016/j.jelechem.2017.06.021).

Record type: Article

Abstract

It is widely claimed that native GOx undergoes direct electron transfer (DET) at nanostructured electrodes. In this paper we argue that the vast majority, if not all, of these claims are incorrect. We present results for GOx adsorbed on MWCNTs, a typical nanostructured electrode. We show that the surface redox peaks usually attributed to DET to GOx actually arise from flavin, and possibly catalase, impurities present in the as supplied commercial enzyme that are adsorbed at the electrode surface. We show that the observed response to glucose is due to enzymatic activity, but not electroactivity, of adsorbed GOx that catalyses the reaction of D-glucose with dissolved oxygen leading to a decrease in the oxygen reduction current that correlates with the glucose concentration.

Text
GOx_DET_18_5_17_docx - Accepted Manuscript
Download (1MB)
Text
GOx DET Table Final
Restricted to Repository staff only
Request a copy

More information

Accepted/In Press date: 12 June 2017
e-pub ahead of print date: 13 June 2017
Published date: 15 June 2018
Keywords: Enzyme electrochemistry, glucose oxidase, direct electron transfer

Identifiers

Local EPrints ID: 412283
URI: http://eprints.soton.ac.uk/id/eprint/412283
ISSN: 1572-6657
PURE UUID: 5679b6a8-6867-486d-b9ea-996cb301c7c3
ORCID for Philip N. Bartlett: ORCID iD orcid.org/0000-0002-7300-6900

Catalogue record

Date deposited: 17 Jul 2017 13:26
Last modified: 16 Mar 2024 05:27

Export record

Altmetrics

Contributors

Author: Firas A. Al-Lolage

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×