Characterization of Recombinant GH 43 β-Xylosidases and a GH 3 β-Glucosidase from Levilactobacillus brevis for the Hydrolysis of Lignocellulose-Derived Substrates
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-nitrophenyl-β-D-glucopyranoside, with optimal activity at pH 9.0 and 45°C. The LbBgl3 demonstrated thermal stability at up to 45°C. It showed high activity towards cellobiose. Structural analysis of the three GH enzymes confirmed the presence of hallmark domains in their respective GH families and conserved catalytic residues. This study aims to contribute to the understanding of LAB-derived GH enzymes through genomic surveys and recombinant protein expression and their potential use in industrial applications.
Fields of Study & Subjects
Enzyme Production and Characterization
Biofuel production and bioconversion
Enzyme Catalysis and Immobilization
Publication details
- Journal / source
- Journal of Microbiology and Biotechnology
- Volume
- 36
- Pages
- e2601031–e2601031
- Publication date
- 13 March 2026
- Language
- EN