Characterization of a novel salt-, xylose- and alkali-tolerant GH43 bifunctional β-xylosidase/α-l-arabinofuranosidase from the gut bacterial genome.

@article{Xu2019CharacterizationOA,
  title={Characterization of a novel salt-, xylose- and alkali-tolerant GH43 bifunctional $\beta$-xylosidase/$\alpha$-l-arabinofuranosidase from the gut bacterial genome.},
  author={Bo Xu and Liming Dai and Wenhong Zhang and Yunjuan Yang and Qian Wu and Junjun Li and Xianghua Tang and Junpei Zhou and Junmei Ding and Nanyu Han and Zunxi Huang},
  journal={Journal of bioscience and bioengineering},
  year={2019}
}
A GH43 bifunctional β-xylosidase encoding gene (XylRBM26) was cloned from Massilia sp. RBM26 and successfully expressed in Escherichia coli. Recombinant XylRBM26 exhibited β-xylosidase and α-l-arabinofuranosidase activities. When 4-nitrophenyl-β-d-xylopyranoside was used as a substrate, the enzyme reached optimal activity at pH 6.5 and 50°C and remained stable at pH 5.0-10.0. Purified XylRBM26 presented good salt tolerance and retained 96.6% activity in 3.5 M NaCl and 77.9% initial activity… 
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Results indicate that CoXyl43 exhibits unique enzymatic properties useful for biomass saccharification.
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