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Insights into the mechanism for the high-alkaline activity of a novel GH43 β-xylosidase from Bacillus clausii with a promising application to produce xylose
- Source :
- Bioorganic Chemistry. 126:105887
- Publication Year :
- 2022
- Publisher :
- Elsevier BV, 2022.
-
Abstract
- Nowadays, alkali-tolerant β-xylosidases and their molecular mechanism of pH adaptability have been poorly studied. Here, a novel GH43 β-xylosidase (XYLO) was isolated from Bacillus clausii TCCC 11004, and the recombinant β-xylosidase (rXYLO) was most active at pH 8.0 and stable in a broad pH range (7.0-11.0), exhibiting superior alkali tolerance. Molecular dynamics simulation indicated that XYLO showed a notable overall structural stability and an enlargement of substrate binding pocket under alkaline condition, resulting in the formation of a new hydrogen bond between substrate and Arg286 of XYLO, and the tight binding played a key role in improving the XYLO activity with the increasing pH. Moreover, rXYLO with an endo-xylanase resulted in high xylose yields by hydrolyzing alkali-extracted xylan from agricultural wastes. This work would provide an alkali-tolerant β-xylosidase, enhance the understanding for the relationship of structure and activity adapted to the high-alkaline environment, and promote its application in xylose production.
Details
- ISSN :
- 00452068
- Volume :
- 126
- Database :
- OpenAIRE
- Journal :
- Bioorganic Chemistry
- Accession number :
- edsair.doi.dedup.....04f63b56c403097a2c2359543c802ef1