ArticleScientific reports2024
A novel GH3-β-glucosidase from soda lake metagenomic libraries with desirable properties for biomass degradation.
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 14 citations in OpenAlex.
- Exploration of Alkaliphilic Bacteria Alkalitalea saponilacus Identifies Glycoside Hydrolases With Biotechnological Potential.Microbial biotechnology · 2026Article
- Synthesis and Glycosidase Inhibition Studies of Novel Exoglycals Targeting GH3 Family Enzymes: Insights from Comparative Analysis with Macrolide Antibiotics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Characterization of a Novel GH3 β-Glucosidase with Alkali-Tolerant and Halophilic Properties from Pontixanthobacter luteolus SW-109.Applied biochemistry and biotechnology · 2026Article
- CAZyme fold architecture is conserved between disparate environments despite extreme sequence divergence.mSystems · 2026Article
- Metagenomic insights into mangrove lignocellulolytic bacteria and functional analysis of a glucose-tolerant GH 1 β-glucosidase.3 Biotech · 2026Article
- Microorganisms and functional genes in an aerobic-anoxic integrated gold mine wastewater treatment system.World journal of microbiology & biotechnology · 2026Article
- Characterization, thermostable mechanism, and molecular docking of a novel glucose-tolerantFrontiers in microbiology · 2025Article
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Authors and funding
5 authors at 2 institutions in 3 countries.
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No grant is acknowledged in the PubMed record.
Abstract
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
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