Glucose oxidase converted into a general sugar-oxidase.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
23 06 2022
23 06 2022
Historique:
received:
14
02
2022
accepted:
15
06
2022
entrez:
23
6
2022
pubmed:
24
6
2022
medline:
28
6
2022
Statut:
epublish
Résumé
Entrapment of glucose oxidase (GOx) within metallic gold converts this widely used enzyme into a general saccharide oxidase. The following sugar molecules were oxidized by the entrapped enzyme (in addition to D-glucose): fructose, xylose, L-glucose, glucose-6-phosphate, sucrose, lactose, methylglucoside, and the tri-saccharide raffinose. With the exception of raffinose, none of these sugars have a natural specific oxidase. The origin of this generalization of activity is attributed to the strong protein-gold 3D interactions and to the strong interactions of the co-entrapped CTAB with both the gold, and the protein. It is proposed that these interactions induce conformational changes in the channel leading to the active site, which is located at the interface between the two units of the dimeric GOx protein. The observations are compatible with affecting the specific conformation change of pulling apart and opening this gate-keeper, rendering the active site accessible to a variety of substrates. The entrapment methodology was also found to increase the thermal stability of GOx up to 100 °C and to allow its convenient reuse, two features of practical importance.
Identifiants
pubmed: 35739181
doi: 10.1038/s41598-022-14957-6
pii: 10.1038/s41598-022-14957-6
pmc: PMC9226012
doi:
Substances chimiques
Sugars
0
Gold
7440-57-5
Oxidoreductases
EC 1.-
Glucose Oxidase
EC 1.1.3.4
Glucose
IY9XDZ35W2
Raffinose
N5O3QU595M
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
10716Informations de copyright
© 2022. The Author(s).
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