Purification and properties of thermostable xylanase and beta-xylosidase produced by a newly isolated Bacillus stearothermophilus strain

J Bacteriol. 1990 Dec;172(12):6669-72. doi: 10.1128/jb.172.12.6669-6672.1990.

Abstract

We isolated a thermophilic bacterium that produces both xylanase and beta-xylosidase. Based on taxonomical research, this bacterium was identified as Bacillus stearothermophilus. Each extracellular enzyme was separated by hydrophobic chromatography by using a Toyopearl HW-65 column, followed by gel filtration with a Sephacryl S-200 column. Each enzyme in the culture was further purified to homogeneity (62-fold for xylanase and 72-fold for beta-xylosidase) by using a fast protein liquid chromatography system with a Mono Q HR 5/5 column. The optimum temperatures were 60 degrees C for xylanase and 70 degrees C for beta-xylosidase. The isoelectric points and molecular masses were 5.1 and 39.5 kDa for xylanase and 4.2 and 150 kDa for beta-xylosidase, respectively. Heat treatment at 60 degrees C for 1 h did not cause inhibition of the activities of these enzymes. The action of the two enzymes on xylan gave only xylose.

MeSH terms

  • Geobacillus stearothermophilus / enzymology*
  • Geobacillus stearothermophilus / metabolism
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / isolation & purification*
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Isoelectric Point
  • Molecular Weight
  • Xylan Endo-1,3-beta-Xylosidase
  • Xylans / metabolism
  • Xylosidases / chemistry
  • Xylosidases / isolation & purification*

Substances

  • Xylans
  • Glycoside Hydrolases
  • Xylosidases
  • Xylan Endo-1,3-beta-Xylosidase
  • exo-1,4-beta-D-xylosidase