Characterization of a recombinant β-xylosidase of GH43 family from Bacteroides ovatus strain ATCC 8483

• Published in: Biocatalysis and biotransformation Vol. 38; no. 1; pp. 46 - 52
• Main Authors: Zhou, Andong, Hu, Yanbo, Li, Jingjing, Wang, Weiyang, Zhang, Mengshan, Guan, Shuwen
• Format: Journal Article
• Language: English
• Published: Taylor & Francis 02.01.2020
• Subjects: Bacteroides ovatus; GH family 43; β-1,4-xylosidase
• ISSN: 1024-2422; 1029-2446
• DOI: 10.1080/10242422.2019.1631813

A novel β-1,4-xylosidase was identified from the genome of Bacteroides ovatus strain ATCC 8483 and overexpressed in Escherichia coli BL21 (DE3) cells. The molecular weight of recombinant enzyme named BoXyl43A was calculated to be 37.1 kDa. Using p-nitrophenyl-β-D-xylopyranoside (pNPβXyl) as substrate, BoXyl43A was most active at pH 7.0 and 35 °C. The enzyme could be activated by Mg 2+ and Mn 2+ . The K m and V max of BoXyl43A against pNPβXyl were 1.71 ± 0.21 mM, 7.41 ± 0.81 μmol/min/mg, respectively. BoXyl43A hydrolyzed xylooligosaccharide to produce D-xylose as main product, indicating that BoXyl43A acted as an exo-β-1,4-xylosidase. The mixture of BoXyl43A and PoAbf62A (α-L-arabinofuranosidase) exhibited significant synergistic effects on the degradation of arabinoxylan. Therefore, BoXyl43A would be a useful tool to degrade hemicellulose.