A Cold- and Salt-Tolerant GH43-1 β-Xylosidase from Cellulomonas bogoriensis 69B4^T: Biochemical Characterization and Subfamily Functional Diversity.

Authors

Xueting Qu, Shuyan Wang, Shanshan Gao, Yuchi Zhou, Ye Yuan, Yao Di, Hongmei Xia, Fan Li

Published in

Applied biochemistry and biotechnology. Jul 01, 2026. Epub Jul 01, 2026.

Abstract

The β-xylosidase Cbxyl1 of GH43-1 subfamily from Cellulomonas bogoriensis 69B4^T was expressed in Escherichia coli. It showed optimal activity at 30 °C and pH 7.0, retaining 40% of its activity at 10 °C. It displayed Ca²⁺-dependent activity and remarkable salt tolerance, maintaining 87% activity in the presence of 4 M KCl. Cbxyl1 hydrolyzed p-nitrophenyl-β-D-xylopyranoside, p-nitrophenyl-α-L-arabinofuranoside, and xylooligosaccharides, but could not cleave arabinose from arabinoxylan oligosaccharides. Structural analysis reveals that Cbxyl1 adopts a five-bladed β-propeller fold characteristic of the GH43 family, with Asp5, Asp125, and Glu212 as the catalytic residues, along with a high proportion of random coils and a low number of salt bridges and hydrogen bonds. Phylogenetic analysis and comparison with other GH43-1 enzymes suggest functional diversity within this subfamily, including both strict β-xylosidases and bifunctional enzymes. Collectively, these results establish Cbxyl1 as a cold- and salt-tolerant β-xylosidase with strict substrate selectivity, thereby providing a candidate enzyme together with experimental information for further investigation and potential application, and contributing to a refined understanding of the substrate specificity landscape within the GH43-1 subfamily.

PMID:
42384251
Bibliographic data and abstract were imported from PubMed on 01 Jul 2026.

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