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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
Source PublicationSCIENTIFIC REPORTS
ISSN2045-2322
Volume6Issue:FEBPages:1-12
Abstract

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.

KeywordCarbohydrate-binding Modules Geobacillus-stearothermophilus Structural Insights Xylan Utilization Plant Biomass Specificity Enzymes Protein Server Thermostabilization
SubtypeArticle
Subject AreaMultidisciplinary Sciences ; Science & Technology - Other Topics
WOS HeadingsScience & Technology
DOI10.1038/srep21672
URL查看原文
Indexed BySCI
Language英语
WOS KeywordCarbohydrate-binding Modules ; Geobacillus-stearothermophilus ; Structural Insights ; Xylan Utilization ; Plant Biomass ; Specificity ; Enzymes ; Protein ; Server ; Thermostabilization
WOS Research AreaScience & Technology - Other Topics
WOS SubjectMultidisciplinary Sciences
Funding OrganizationNational High Technology Research and Development Program of China (863 Project)(2014AA021905) ; 100 Talents Program of institute of process engineering, Chinese Academy of Sciences
WOS IDWOS:000370508800001
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/20713
Collection研究所(批量导入)
Corresponding AuthorHan, Yejun
Affiliation1.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
Recommended Citation
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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