A novel GH3-β-glucosidase from soda lake metagenomic libraries with desirable properties for biomass degradation.
Beta-glucosidase
Enzyme characterisation
Glycoside hydrolase family 3 (GH3)
Soda lakes
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
01 05 2024
01 05 2024
Historique:
received:
16
11
2023
accepted:
25
04
2024
medline:
2
5
2024
pubmed:
2
5
2024
entrez:
1
5
2024
Statut:
epublish
Résumé
Beta-glucosidases catalyze the hydrolysis of the glycosidic bonds of cellobiose, producing glucose, which is a rate-limiting step in cellulose biomass degradation. In industrial processes, β-glucosidases that are tolerant to glucose and stable under harsh industrial reaction conditions are required for efficient cellulose hydrolysis. In this study, we report the molecular cloning, Escherichia coli expression, and functional characterization of a β-glucosidase from the gene, CelGH3_f17, identified from metagenomics libraries of an Ethiopian soda lake. The CelGH3_f17 gene sequence contains a glycoside hydrolase family 3 catalytic domain (GH3). The heterologous expressed and purified enzyme exhibited optimal activity at 50 °C and pH 8.5. In addition, supplementation of 1 M salt and 300 mM glucose enhanced the β-glucosidase activity. Most of the metal ions and organic solvents tested did not affect the β-glucosidase activity. However, Cu
Identifiants
pubmed: 38693138
doi: 10.1038/s41598-024-60645-y
pii: 10.1038/s41598-024-60645-y
doi:
Substances chimiques
beta-Glucosidase
EC 3.2.1.21
Cellulose
9004-34-6
Glucose
IY9XDZ35W2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
10012Informations de copyright
© 2024. The Author(s).
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