Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-beta-Xylanase from Caldicellulosiruptor owensensis

doi:10.1021/acs.jafc.7b03607

CORC > 过程工程研究所 > 中国科学院过程工程研究所 > 生化工程国家重点实验室

	Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-beta-Xylanase from Caldicellulosiruptor owensensis
	Liu, Xin 1; Liu, Tengfei 2; Zhang, Yuebin 3; Xin, Fengjiao 1; Mi, Shuofu 4; Wen, Boting 1; Gu, Tianyi 1; Shi, Xinyuan 2; Wang, Fengzhong 1; Sun, Lichao 1
刊名	JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
	2018-01-10
卷号	66 期号:1 页码:187-193
关键词	Gh10 Xylanase Caldicellulosiruptor Owensensis Thermostability Crystal Structure Loop 7
ISSN号	0021-8561
DOI	10.1021/acs.jafc.7b03607
文献子类	Article
英文摘要	Xylanases (EC 3.2.1.8) are a kind of enzymes degrading xylan to xylooligosaccharides (XOS) and have been widely used in a variety of industrial applications. Among them, xylanases from thermophilic microorganisms have distinct advantages in industries that require high temperature conditions. The CoXynA gene, encoding a glycoside hydrolase (GH) family 10 xylanase, was identified from thermophilic Caldicellulosiruptor owensensis and was overexpressed in Escherichia coli. Recombinant CoXynA showed optimal activity at 90 degrees C with a half-life of about 1 h at 80 degrees C and exhibited highest activity at pH 7.0. The activity of CoXynA activity was affected by a variety of cations. CoXynA showed distinct substrate specificities for beechwood xylan and birchwood xylan. The crystal structure of CoXynA was solved and a molecular dynamics simulation of CoXynA was performed. The relatively high thermostability of CoXynA was proposed to be due to the increased overall protein rigidity resulting from the reduced length and fluctuation of Loop 7.
WOS关键词	GH10 XYLANASE ; ALCOHOL-DEHYDROGENASE ; CRYSTAL-STRUCTURE ; BESCII ; THERMOSTABILITY ; STABILITY ; RESIDUES ; FEATURES ; INDUSTRY ; BIOMASS
WOS研究方向	Agriculture ; Chemistry ; Food Science & Technology
语种	英语
WOS记录号	WOS:000419999900022
资助机构	national key research and development plan "modern food processing and food storage and transportation technology and equipment"(2017YFD0400200) ; National Natural Science Foundation of China(31571963)
内容类型	期刊论文
源URL	[http://ir.ipe.ac.cn/handle/122111/24090]
专题	过程工程研究所_生化工程国家重点实验室
作者单位	1.Chinese Acad Agr Sci, Inst Food Sci & Technol, Lab Biomfg & Food Engn, Beijing 100193, Peoples R China 2.Beijing Univ Chinese Med, Sch Chinese Mat Med, Beijing 100102, Peoples R China 3.Chinese Acad Sci, Dalian Inst Chem Phys, State Key Lab Mol React Dynam, 457 Zhongshan Rd, Dalian 116023, Peoples R China 4.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
推荐引用方式 GB/T 7714	Liu, Xin,Liu, Tengfei,Zhang, Yuebin,et al. Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-beta-Xylanase from Caldicellulosiruptor owensensis[J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY,2018,66(1):187-193.
APA	Liu, Xin.,Liu, Tengfei.,Zhang, Yuebin.,Xin, Fengjiao.,Mi, Shuofu.,...&Sun, Lichao.(2018).Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-beta-Xylanase from Caldicellulosiruptor owensensis.JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY,66(1),187-193.
MLA	Liu, Xin,et al."Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-beta-Xylanase from Caldicellulosiruptor owensensis".JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 66.1(2018):187-193.