Specific anion effects on urease activity: A Hofmeister study.
Chaotropicity
Enzymatic activity
Hofmeister series
Kosmotropicity
Urease
Journal
Colloids and surfaces. B, Biointerfaces
ISSN: 1873-4367
Titre abrégé: Colloids Surf B Biointerfaces
Pays: Netherlands
ID NLM: 9315133
Informations de publication
Date de publication:
Apr 2024
Apr 2024
Historique:
received:
19
12
2023
revised:
24
01
2024
accepted:
04
02
2024
pubmed:
17
2
2024
medline:
17
2
2024
entrez:
17
2
2024
Statut:
ppublish
Résumé
The effects of a range of electrolytes on the hydrolysis of urea by the enzyme urease is explored. The autocatalytic behavior of urease in unbuffered solutions and its pH clock reactions are studied. The concentration dependence of the experimental variables is analyzed in terms of specific ion-enzyme interactions and hydration. The results offer insights into the molecular mechanisms of the enzyme, and on the nature of its interactions with the electrolytes. We found that urease can tolerate mild electrolytes in its environment, while it is strongly inhibited by both strong kosmotropic and strong chaotropic anions. This study may cast light on an alternative therapy for Helicobacter pylori infections and contribute to the design of innovative materials and provide new approaches for the modulation of the enzymatic activity.
Identifiants
pubmed: 38367291
pii: S0927-7765(24)00047-X
doi: 10.1016/j.colsurfb.2024.113789
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
113789Informations de copyright
Copyright © 2024 The Authors. Published by 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.