Characterization of a novel cold-active β-Xylosidase from Parabacteroides distasonis and its synergistic hydrolysis of beechwood xylan.

Although β-xylosidases have broad applications in fields such as food and medicine, there is limited research on cold-active β-xylosidases. This study cloned a novel cold-active β-xylosidase XYL13 from Parabacteroides distasonis. The purified XYL13 exhibited the highest activity at 40 °C, with 42 % and 25 % of its maximum activity at 4 °C and 0 °C, respectively. Meanwhile, XYL13 predominantly produces X1 while degrading X2-X6. Additionally, XYL13 showed a significant synergistic effect (18.5-fold) with endo-xylanase for degrading beechwood xylan at low temperatures. Moreover, the site-directed mutagenesis assay indicated that Ile269 and Glu621 are essential catalytic sites of XYL13. Finally, molecular docking showed that XYL13 has an excellent binding effect with X2-X6, verifying that XYL13 can effectively cut X2-X6 to produce xylose. These results highlight the potential of cold-adapted XYL13 from P. distasonis for application in the food industry.