title: Increased enzymatic hydrolysis of sugarcane bagasse by a novel glucose- and xylose-stimulated β-glucosidase from Anoxybacillus flavithermus subsp. yunnanensis E13T.
abstract: β-Glucosidase is claimed as a key enzyme in cellulose hydrolysis. The cellulosic fibers are usually entrapped with hemicelluloses containing xylose. So there is ongoing interest in searching for glucose- and xylose-stimulated β-glucosidases to increase the efficiency of hydrolysis of cellulosic biomass.
  
  
  
  A thermostable β-glucosidase gene (Bglp) was cloned from Anoxybacillus flavithermus subsp. yunnanensis E13Tand characterized. Optimal enzyme activity was observed at 60 °C and pH 7.0. Bglp was relatively stable at 60 °C with a 10-h half-life. The kinetic parameters Vmaxand Kmfor p-nitrophenyl-β-D-glucopyranoside (pNPG) were 771 ± 39 μmol/min/mg and 0.29 ± 0.01 mM, respectively. The activity of Bglp is dramatically stimulated by glucose or xylose at concentrations up to 1.4 M. After Bglp was added to Celluclast® 1.5 L, the conversion of sugarcane bagasse was 48.4 ± 0.8%, which was much higher than of Celluclast® 1.5 L alone. Furthermore, Bglp showed obvious advantages in the hydrolysis when initial concentrations of glucose and xylose are high.
  
  
  
  The supplementation of BglP significantly enhanced the glucose yield from sugarcane bagasse, especially in the presence of high concentrations of glucose or xylose. Bglp should be a promising candidate for industrial applications.
authors.affiliation: Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis. School of Life Sciences, Anhui University, Hefei, Anhui, China.|College of Biological and Food Engineering, Chuzhou University, Chuzhou, Anhui, China.
authors.forename: Yang
authors.initials: Y
authors.lastname: Liu
authors.affiliation: Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis. School of Life Sciences, Anhui University, Hefei, Anhui, China.
authors.forename: Rui
authors.initials: R
authors.lastname: Li
authors.affiliation: Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis. School of Life Sciences, Anhui University, Hefei, Anhui, China.
authors.forename: Jing
authors.initials: J
authors.lastname: Wang
authors.affiliation: Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis. School of Life Sciences, Anhui University, Hefei, Anhui, China.
authors.forename: Xiaohan
authors.initials: X
authors.lastname: Zhang
authors.affiliation: Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis. School of Life Sciences, Anhui University, Hefei, Anhui, China.
authors.forename: Rong
authors.initials: R
authors.lastname: Jia
authors.affiliation: Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis. School of Life Sciences, Anhui University, Hefei, Anhui, China.
authors.forename: Yi
authors.initials: Y
authors.lastname: Gao
authors.affiliation: Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis. School of Life Sciences, Anhui University, Hefei, Anhui, China. pph0259@126.com.
authors.forename: Hui
authors.initials: H
authors.lastname: Peng
mesh_terms: D058677:Anoxybacillus / Q000201:enzymology*; D002482:Cellulose / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects*; D004795:Enzyme Stability; D005947:Glucose / Q000494:pharmacology*; D006868:Hydrolysis / Q000187:drug effects; D007700:Kinetics; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D031786:Saccharum / Q000378:metabolism*; D013696:Temperature; D014994:Xylose / Q000494:pharmacology*; D001617:beta-Glucosidase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins; D002482:Cellulose; D014994:Xylose; D001617:beta-Glucosidase; D005947:Glucose
keywords: Conversion of sugarcane bagasse; Glucose-stimulated; Thermostability; Xylose-stimulated; β-Glucosidase