These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Biochemical characterization of a novel GH43 family β-xylosidase from Bacillus pumilus. Author: Liu Y, Huang L, Zheng D, Xu Z, Li Y, Shao S, Zhang Y, Ge X, Lu F. Journal: Food Chem; 2019 Oct 15; 295():653-661. PubMed ID: 31174809. Abstract: Although β-xylosidases have a wide range of applications, cold-active β-xylosidases have been poorly studied. In this study, a cold active β-xylosidase gene (xyl) from Bacillus pumilus TCCC 11,350 was cloned and overexpressed in Escherichia coli. The recombinant XYL (rXYL) was revealed to be a bifunctional enzyme with both β-xylosidase and α-l-arabinofuranosidase activities. Purified rXYL was most active at 30 °C, demonstrating 26% and 18% of its maximum activity at 4 °C and 0 °C, respectively. Meanwhile, rXYL showed a 52% activity in 200 mM xylose, indicating a relatively strong tolerance to xylose. Moreover, rXYL exhibited a high synergistic effect (11.14-fold and 16.21-fold) with endo-xylanase to degrade beechwood xylan in both sequential and simultaneous reactions at low temperatures. As the first report on the novel cold-adapted β-xylosidase from B. pumilus, these results suggested rXYL had attractive properties for food industrial utilizations.[Abstract] [Full Text] [Related] [New Search]