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Official Journal of the Japan Wood Research Society

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

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Abstract

β-Glucosidase (β-1,4-D-glucoside glucohydrolase: EC.3.2.1.21) 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%.

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Author information

Correspondence to Hyeun-Jong Bae.

Additional information

Part of this study was presented at the 57th Annual Meeting of the Japan Wood Research Society, Hiroshima, August 2007

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Choi, I.S., Wi, S.G., Jung, S.R. et al. Characterization and application of recombinant β-glucosidase (BglH) from Bacillus licheniformis KCTC 1918. J Wood Sci 55, 329–334 (2009) doi:10.1007/s10086-009-1044-2

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Key words

  • Cellulose
  • Cellulose degradation
  • β-Glucosidase