A single residue affects the dynamics and shape of a tetrameric GH43 β-1,4-d-xylosidase from Levilactobacillus brevis DSM1269.

ABSTRACT: Lignocellulosic materials (e.g., straw and bran) are gaining interest as feedstocks for the manufacture of higher value products, recognizing xylooligosaccharides (XOS) as interesting prebiotic compounds, and putting enzymes converting xylooligosaccharides into focus. In this work, we are investigating a XOS converting enzyme from the probiotic bacterium Levilactobacillus brevis (formerly Lactobacillus brevis). Growth of multiple L. brevis strains, recognized as probiotics, is promoted by the presence of XOS. This study elucidates the 3D structure of an intracellular L. brevis β-xylosidase, LbXyn43B from glycoside hydrolase family 43 (GH43), resolving it to 1.9 Å resolution. Functional analysis identified LbXyn43B as a mediator for XOS utilization in L. brevis DSM1269. The enzyme, featurin

SUBMITTER: Linares-Pasten JA 

PROVIDER: S-EPMC12432433 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature