Characterization and application of recombinant β-glucosidase (BglH) from <Emphasis Type="Italic">Bacillus licheniformis</Emphasis> KCTC 1918 |
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| Authors: | In Seong Choi Seung Gon Wi Se Ra Jung Darshan H Patel Hyeun-Jong Bae |
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| Institution: | (1) National Engineering Laboratory for High-efficiency Enzyme Expression, Fuzhou, China;(2) College of Biological Science and Technology, Fuzhou University, Fuzhou, China;(3) School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China;(4) 3/f, Building No. 3, No. 7, JinZhou Road North, JinShan Industrial Zone, Fuzhou, Fujian, 350002, People’s Republic of China; |
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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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