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Official Journal of the Japan Wood Research Society

Journal of Wood Science Cover Image
  • Original Article
  • Open Access

Characterization and application of recombinant β-glucosidase (BglH) from Bacillus licheniformis KCTC 1918

  • 1,
  • 2,
  • 1,
  • 2 and
  • 1, 2Email author
Journal of Wood ScienceOfficial Journal of the Japan Wood Research Society200955:1044

  • Received: 14 January 2009
  • Accepted: 10 June 2009
  • Published:


β-Glucosidase (β-1,4-D-glucoside glucohydrolase: EC. catalyzes the hydrolysis of β-glucosidic bonds between saccharides and aryl or alkyl groups. A gene encoding β-glucosidase from Bacillus licheniformis KCTC 1918, an anaerobic spore-forming soil bacterium, was cloned and characterized. The structural gene for the β-glucosidase consists of 1410 bp encoding 469 amino acid residues, and has a molecular weight of 53.4 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis with 12% separating gel. The enzyme activity was determined against pNPG as a substrate. The enzyme was optimally active at pH 6.0 (citrate-phosphate buffer) and 47°C. β-Glucosidase retained 100% of its original activity for 24 h. The activity of the enzyme was stimulated by glycerol and urea and was decreased by Ca2+, Cu2+, Hg2+, Mg2+, and Mn2+. In particular, Cu2+ had the strongest negative effect on β-glucosidase activity. The purified β-glucosidase was active against pNPG and cellobiose. When the β-glucosidase was tested for cellulose hydrolysis, the supplement of β-glucosidase with cellulose increased the glucose yield from pine wood powder by 139.8%.

Key words

  • Cellulose
  • Cellulose degradation
  • β-Glucosidase