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Biochemical characterization of extra- and intracellular endoxylanse from thermophilic bacterium Caldicellulosiruptor kronotskyensis
Jia, Xiaojing1,2; Qiao, Weibo1; Tian, Wenli3; Peng, Xiaowei1; Mi, Shuofu1; Su, Hong1,2; Han, Yejun1
2016-02-22
发表期刊SCIENTIFIC REPORTS
ISSN2045-2322
卷号6期号:FEB页码:1-12
摘要

Caldicellulosiruptor kronotskyensis grows on lignocellulosic biomass by the catalysis of intrinsic glycoside hydrolase, and has potential application for consolidated bioprocessing. In current study, two predicted extra-(Xyn10A) and intracellular (Xyn10B) xylanase from C. kronotskyensis were comparatively characterized. Xyn10A and Xyn10B share GH10 catalytic domain with similarity of 41%, while the former contains two tandem N-terminus CBM22s. Xyn10A showed higher hydrolytic capability than Xyn10B on both beechwood xylan (BWX) and oat spelt xylan (OSX). Truncation mutation experiments revealed the importance of CBMs for hydrolytic activity, substrate binding and thermostability of Xyn10A. While the quantity of CBM was not directly related to bind and thermostability. Although CBM was considered to be crucial for substrate binding, Xyn10B and Xyn10A as well as truncations performed similar binding affinity to insoluble substrate OSX. Analysis of point mutation revealed similar key residues, Glu493, Glu601 and Trp658 for Xyn10A and Glu139, Glu247 and Trp305 for Xyn10B. Both Xyn10A and Xyn10B exhibited hydrolytic activity on the mechanical pretreated corncob. After pre-digested by Xyn10A or Xyn10B, the micropores in the the mechanical pretreated corncob were observed, which enhanced the accessibility for cellulase. Compared with corncob hydrolyzed with cellulase alone, enhanced hydrolytic performance of was observed after predigestion by Xyn10A or Xyn10B.

关键词Carbohydrate-binding Modules Geobacillus-stearothermophilus Structural Insights Xylan Utilization Plant Biomass Specificity Enzymes Protein Server Thermostabilization
文章类型Article
学科领域Multidisciplinary Sciences ; Science & Technology - Other Topics
WOS标题词Science & Technology
DOI10.1038/srep21672
URL查看原文
收录类别SCI
语种英语
关键词[WOS]Carbohydrate-binding Modules ; Geobacillus-stearothermophilus ; Structural Insights ; Xylan Utilization ; Plant Biomass ; Specificity ; Enzymes ; Protein ; Server ; Thermostabilization
WOS研究方向Science & Technology - Other Topics
WOS类目Multidisciplinary Sciences
项目资助者National High Technology Research and Development Program of China (863 Project)(2014AA021905) ; 100 Talents Program of institute of process engineering, Chinese Academy of Sciences
WOS记录号WOS:000370508800001
引用统计
被引频次:7[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ipe.ac.cn/handle/122111/20713
专题研究所(批量导入)
通讯作者Han, Yejun
作者单位1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Chinese Acad Agr Sci, Inst Apicultural Res, Beijing 100093, Peoples R China
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GB/T 7714
Jia, Xiaojing,Qiao, Weibo,Tian, Wenli,et al. Biochemical characterization of extra- and intracellular endoxylanse from thermophilic bacterium Caldicellulosiruptor kronotskyensis[J]. SCIENTIFIC REPORTS,2016,6(FEB):1-12.
APA Jia, Xiaojing.,Qiao, Weibo.,Tian, Wenli.,Peng, Xiaowei.,Mi, Shuofu.,...&Han, Yejun.(2016).Biochemical characterization of extra- and intracellular endoxylanse from thermophilic bacterium Caldicellulosiruptor kronotskyensis.SCIENTIFIC REPORTS,6(FEB),1-12.
MLA Jia, Xiaojing,et al."Biochemical characterization of extra- and intracellular endoxylanse from thermophilic bacterium Caldicellulosiruptor kronotskyensis".SCIENTIFIC REPORTS 6.FEB(2016):1-12.
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