CAS OpenIR  > 研究所(批量导入)
Biochemical Characterization of Two Thermostable Xylanolytic Enzymes Encoded by a Gene Cluster of Caldicellulosiruptor owensensis
Alternative TitlePLoS One
Mi, Shuofu1; Jia, Xiaojing1; Wang, Jinzhi2; Qiao, Weibo1,3; Peng, Xiaowei1; Han, Yejun1
2014-08-15
Source PublicationPLOS ONE
ISSN1932-6203
Volume9Issue:8Pages:12
AbstractThe xylanolytic extremely thermophilic bacterium Caldicellulosiruptor owensensis provides a promising platform for xylan utilization. In the present study, two novel xylanolytic enzymes, GH10 endo-beta-1,4-xylanase (Coxyn A) and GH39 beta-1,4-xylosidase (Coxyl A) encoded in one gene cluster of C. owensensis were heterogeneously expressed and biochemically characterized. The optimum temperature of the two xylanlytic enzymes was 75 degrees C, and the respective optimum pH for Coxyn A and Coxyl A was 7.0 and 5.0. The difference of Coxyn A and Coxyl A in solution was existing as monomer and homodimer respectively, it was also observed in predicted secondary structure. Under optimum condition, the catalytic efficiency (k(cat)/K-m) of Coxyn A was 366 mg ml(-1) s(-1) on beechwood xylan, and the catalytic efficiency (k(cat)/K-m) of Coxyl A was 2253 mM(-1) s(-1) on pNP-beta-D-xylopyranoside. Coxyn A degraded xylan to oligosaccharides, which were converted to monomer by Coxyl A. The two intracellular enzymes might be responsible for xylooligosaccharides utilization in C. owensensis, also provide a potential way for xylan degradation in vitro.; The xylanolytic extremely thermophilic bacterium Caldicellulosiruptor owensensis provides a promising platform for xylan utilization. In the present study, two novel xylanolytic enzymes, GH10 endo-beta-1,4-xylanase (Coxyn A) and GH39 beta-1,4-xylosidase (Coxyl A) encoded in one gene cluster of C. owensensis were heterogeneously expressed and biochemically characterized. The optimum temperature of the two xylanlytic enzymes was 75 degrees C, and the respective optimum pH for Coxyn A and Coxyl A was 7.0 and 5.0. The difference of Coxyn A and Coxyl A in solution was existing as monomer and homodimer respectively, it was also observed in predicted secondary structure. Under optimum condition, the catalytic efficiency (k(cat)/K-m) of Coxyn A was 366 mg ml(-1) s(-1) on beechwood xylan, and the catalytic efficiency (k(cat)/K-m) of Coxyl A was 2253 mM(-1) s(-1) on pNP-beta-D-xylopyranoside. Coxyn A degraded xylan to oligosaccharides, which were converted to monomer by Coxyl A. The two intracellular enzymes might be responsible for xylooligosaccharides utilization in C. owensensis, also provide a potential way for xylan degradation in vitro.
KeywordGh39 Beta-xylosidase Plant Biomass Thermoanaerobacterium-saccharolyticum Industrial Applications Glycoside Hydrolase Structural Insights Microbial Xylanases Escherichia-coli Bacterium Cloning
SubtypeArticle
WOS HeadingsScience & Technology
DOI10.1371/journal.pone.0105264
URL查看原文
Indexed BySCI
Language英语
WOS KeywordGH39 BETA-XYLOSIDASE ; PLANT BIOMASS ; THERMOANAEROBACTERIUM-SACCHAROLYTICUM ; INDUSTRIAL APPLICATIONS ; GLYCOSIDE HYDROLASE ; STRUCTURAL INSIGHTS ; MICROBIAL XYLANASES ; ESCHERICHIA-COLI ; BACTERIUM ; CLONING
WOS Research AreaScience & Technology - Other Topics
WOS SubjectMultidisciplinary Sciences
WOS IDWOS:000340879300099
Citation statistics
Cited Times:13[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/11494
Collection研究所(批量导入)
Affiliation1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing, Peoples R China
2.Chinese Acad Agr Sci, Inst Agrofood Sci & Technol, Beijing 100193, Peoples R China
3.Shenyang Agr Univ, Shenyang 110161, Peoples R China
Recommended Citation
GB/T 7714
Mi, Shuofu,Jia, Xiaojing,Wang, Jinzhi,et al. Biochemical Characterization of Two Thermostable Xylanolytic Enzymes Encoded by a Gene Cluster of Caldicellulosiruptor owensensis[J]. PLOS ONE,2014,9(8):12.
APA Mi, Shuofu,Jia, Xiaojing,Wang, Jinzhi,Qiao, Weibo,Peng, Xiaowei,&Han, Yejun.(2014).Biochemical Characterization of Two Thermostable Xylanolytic Enzymes Encoded by a Gene Cluster of Caldicellulosiruptor owensensis.PLOS ONE,9(8),12.
MLA Mi, Shuofu,et al."Biochemical Characterization of Two Thermostable Xylanolytic Enzymes Encoded by a Gene Cluster of Caldicellulosiruptor owensensis".PLOS ONE 9.8(2014):12.
Files in This Item:
File Name/Size DocType Version Access License
Biochemical Characte(4713KB) 限制开放CC BY-NC-SAApplication Full Text
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Mi, Shuofu]'s Articles
[Jia, Xiaojing]'s Articles
[Wang, Jinzhi]'s Articles
Baidu academic
Similar articles in Baidu academic
[Mi, Shuofu]'s Articles
[Jia, Xiaojing]'s Articles
[Wang, Jinzhi]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Mi, Shuofu]'s Articles
[Jia, Xiaojing]'s Articles
[Wang, Jinzhi]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.