Solvent concentration at 50% protein unfolding may reform enzyme stability ranking and process window identification.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
26 Jun 2024
26 Jun 2024
Historique:
received:
19
07
2023
accepted:
19
06
2024
medline:
27
6
2024
pubmed:
27
6
2024
entrez:
26
6
2024
Statut:
epublish
Résumé
As water miscible organic co-solvents are often required for enzyme reactions to improve e.g., the solubility of the substrate in the aqueous medium, an enzyme is required which displays high stability in the presence of this co-solvent. Consequently, it is of utmost importance to identify the most suitable enzyme or the appropriate reaction conditions. Until now, the melting temperature is used in general as a measure for stability of enzymes. The experiments here show, that the melting temperature does not correlate to the activity observed in the presence of the solvent. As an alternative parameter, the concentration of the co-solvent at the point of 50% protein unfolding at a specific temperature T in short
Identifiants
pubmed: 38926341
doi: 10.1038/s41467-024-49774-0
pii: 10.1038/s41467-024-49774-0
doi:
Substances chimiques
Solvents
0
Oxidoreductases
EC 1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
5420Informations de copyright
© 2024. The Author(s).
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