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, beta-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 beta-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 degrees C and pH 8.5. In addition, supplementation of 1 M salt and 300 mM glucose enhanced the beta-glucosidase activity. Most of the metal ions and organic solvents tested did not affect the beta-glucosidase activity. However, Cu2+ and Mn2+ ions, Mercaptoethanol and Triton X-100 reduce the activity of the enzyme. The studied beta-glucosidase enzyme has multiple industrially desirable properties including thermostability, and alkaline, salt, and glucose tolerance.

Keywords

Beta-glucosidase; Glycoside hydrolase family 3 (GH3); Soda lakes; Enzyme characterisation

Published in

Scientific Reports
2024, Volume: 14, number: 1, article number: 10012
Publisher: NATURE PORTFOLIO

SLU Authors

• Oumer, Oliyad Jeilu

  • Department of Plant Breeding, Swedish University of Agricultural Sciences
    
  • Ambo University
  • Northwestern University

• Alexandersson, Erik

  • Department of Plant Breeding, Swedish University of Agricultural Sciences
    

• Johansson, Eva

  • Department of Plant Breeding, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Biocatalysis and Enzyme Technology


Publication identifier

DOI: https://doi.org/10.1038/s41598-024-60645-y

Permanent link to this page (URI)

https://res.slu.se/id/publ/130220