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Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-beta-Xylanase from Caldicellulosiruptor owensensis
Liu, Xin1; Liu, Tengfei2; Zhang, Yuebin3; Xin, Fengjiao1; Mi, Shuofu4; Wen, Boting1; Gu, Tianyi1; Shi, Xinyuan2; Wang, Fengzhong1; Sun, Lichao1
2018-01-10
Source PublicationJOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
ISSN0021-8561
Volume66Issue:1Pages:187-193
AbstractXylanases (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.
KeywordGh10 Xylanase Caldicellulosiruptor Owensensis Thermostability Crystal Structure Loop 7
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1021/acs.jafc.7b03607
Indexed BySCI
Language英语
WOS KeywordGH10 XYLANASE ; ALCOHOL-DEHYDROGENASE ; CRYSTAL-STRUCTURE ; BESCII ; THERMOSTABILITY ; STABILITY ; RESIDUES ; FEATURES ; INDUSTRY ; BIOMASS
WOS Research AreaAgriculture ; Chemistry ; Food Science & Technology
WOS SubjectAgriculture, Multidisciplinary ; Chemistry, Applied ; Food Science & Technology
Funding Organizationnational key research and development plan "modern food processing and food storage and transportation technology and equipment"(2017YFD0400200) ; National Natural Science Foundation of China(31571963)
WOS IDWOS:000419999900022
Citation statistics
Cited Times:4[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/24090
Collection生化工程国家重点实验室
Affiliation1.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
Recommended Citation
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.
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