Biochemical characterization of a novel GH43 family β-xylosidase from Bacillus pumilus.


State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, The College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, PR China. Electronic address: [Email]


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.


Bacillus pumilus,Characterization,Cold adaptation,Xylan degradation,β-Xylosidase,

OUR Recent Articles