Biochemical characterization of extra- and intracellular endoxylanse from thermophilic bacterium Caldicellulosiruptor kronotskyensis

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	Biochemical characterization of extra- and intracellular endoxylanse from thermophilic bacterium Caldicellulosiruptor kronotskyensis
	Jia, Xiaojing 1,2; Qiao, Weibo 1; Tian, Wenli 3; Peng, Xiaowei 1; Mi, Shuofu 1; Su, Hong 1,2; Han, Yejun 1
刊名	SCIENTIFIC REPORTS
	2016-02-22
卷号	6 期号:FEB 页码:1-12
关键词	CARBOHYDRATE-BINDING MODULES GEOBACILLUS-STEAROTHERMOPHILUS STRUCTURAL INSIGHTS XYLAN UTILIZATION PLANT BIOMASS SPECIFICITY ENZYMES PROTEIN SERVER THERMOSTABILIZATION
ISSN号	2045-2322
通讯作者	Han, YJ (reprint author), Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China.
英文摘要	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.
学科主题	Multidisciplinary Sciences ; Science & Technology - Other Topics
WOS标题词	Science & Technology
类目[WOS]	Multidisciplinary Sciences
研究领域[WOS]	Science & Technology - Other Topics
关键词[WOS]	CARBOHYDRATE-BINDING MODULES ; GEOBACILLUS-STEAROTHERMOPHILUS ; STRUCTURAL INSIGHTS ; XYLAN UTILIZATION ; PLANT BIOMASS ; SPECIFICITY ; ENZYMES ; PROTEIN ; SERVER ; THERMOSTABILIZATION
收录类别	SCI
原文出处	NATURE PUBLISHING GROUP
语种	英语
WOS记录号	WOS:000370508800001
内容类型	期刊论文
源URL	[http://ir.ipe.ac.cn/handle/122111/20713]
专题	过程工程研究所_研究所（批量导入）
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
推荐引用方式 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.