Electrochemical and biosensing properties of an FAD-dependent glucose dehydrogenase from Trichoderma virens.
Amperometry
FAD-dependent glucose dehydrogenase
GMC oxidoreductases
Maltose biosensor
Osmium polymer
Trichoderma virens
Journal
Bioelectrochemistry (Amsterdam, Netherlands)
ISSN: 1878-562X
Titre abrégé: Bioelectrochemistry
Pays: Netherlands
ID NLM: 100953583
Informations de publication
Date de publication:
Oct 2023
Oct 2023
Historique:
received:
25
03
2023
revised:
20
05
2023
accepted:
24
05
2023
medline:
24
7
2023
pubmed:
4
6
2023
entrez:
3
6
2023
Statut:
ppublish
Résumé
We investigated the bioelectrochemical properties of an FAD-dependent glucose dehydrogenase from Trichoderma virens (TvGDH) and its electrochemical behaviour when immobilized on a graphite electrode. TvGDH was recently shown to have an unusual substrate spectrum and to prefer maltose over glucose as substrate, and hence could be of interest as recognition element in a maltose sensor. In this study, we determined the redox potential of TvGDH, which is -0.268 ± 0.007 V vs. SHE, and advantageously low to be used with many redox mediators or redox polymers. The enzyme was entrapped in, and wired by an osmium redox polymer (poly(1-vinylimidazole-co-allylamine)-{[Os(2,2'-bipyridine)
Identifiants
pubmed: 37269684
pii: S1567-5394(23)00117-2
doi: 10.1016/j.bioelechem.2023.108480
pii:
doi:
Substances chimiques
Glucose 1-Dehydrogenase
EC 1.1.1.47
Graphite
7782-42-5
Maltose
69-79-4
Glucose
IY9XDZ35W2
Polymers
0
Enzymes, Immobilized
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
108480Informations de copyright
Copyright © 2023 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.