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Insight into Glycoside Hydrolases for Debranched Xylan Degradation from Extremely Thermophilic Bacterium Caldicellulosiruptor lactoaceticus
Alternative TitlePLoS One
Jia, Xiaojing1; Mi, Shuofu1; Wang, Jinzhi2; Qiao, Weibo1,3; Peng, Xiaowei1; Han, Yejun1
2014-09-03
Source PublicationPLOS ONE
ISSN1932-6203
Volume9Issue:9Pages:12
AbstractCaldicellulosiruptor lactoaceticus 6A, an anaerobic and extremely thermophilic bacterium, uses natural xylan as carbon source. The encoded genes of C. lactoaceticus 6A for glycoside hydrolase (GH) provide a platform for xylan degradation. The GH family 10 xylanase (Xyn10A) and GH67 alpha-glucuronidase (Agu67A) from C. lactoaceticus 6A were heterologously expressed, purified and characterized. Both Xyn10A and Agu67A are predicted as intracellular enzymes as no signal peptides identified. Xyn10A and Agu67A had molecular weight of 47.0 kDa and 80.0 kDa respectively as determined by SDS-PAGE, while both appeared as homodimer when analyzed by gel filtration. Xyn10A displayed the highest activity at 80 degrees C and pH 6.5, as 75 degrees C and pH 6.5 for Agu67A. Xyn10A had good stability at 75 degrees C, 80 degrees C, and pH 4.5-8.5, respectively, and was sensitive to various metal ions and reagents. Xyn10A possessed hydrolytic activity towards xylo-oligosaccharides (XOs) and beechwood xylan. At optimum conditions, the specific activity of Xyn10A was 44.6 IU/mg with beechwood xylan as substrate, and liberated branched XOs, xylobiose, and xylose. Agu67A was active on branched XOs with methyl-glucuronic acids (MeGlcA) sub-chains, and primarily generated XOs equivalents and MeGlcA. The specific activity of Agu67A was 1.3 IU/mg with aldobiouronic acid as substrate. The synergistic action of Xyn10A and Agu67A was observed with MeGlcA branched XOs and xylan as substrates, both backbone and branched chain of substrates were degraded, and liberated xylose, xylobiose, and MeGlcA. The synergism of Xyn10A and Agu67A provided not only a thermophilic method for natural xylan degradation, but also insight into the mechanisms for xylan utilization of C. lactoaceticus.; Caldicellulosiruptor lactoaceticus 6A, an anaerobic and extremely thermophilic bacterium, uses natural xylan as carbon source. The encoded genes of C. lactoaceticus 6A for glycoside hydrolase (GH) provide a platform for xylan degradation. The GH family 10 xylanase (Xyn10A) and GH67 alpha-glucuronidase (Agu67A) from C. lactoaceticus 6A were heterologously expressed, purified and characterized. Both Xyn10A and Agu67A are predicted as intracellular enzymes as no signal peptides identified. Xyn10A and Agu67A had molecular weight of 47.0 kDa and 80.0 kDa respectively as determined by SDS-PAGE, while both appeared as homodimer when analyzed by gel filtration. Xyn10A displayed the highest activity at 80 degrees C and pH 6.5, as 75 degrees C and pH 6.5 for Agu67A. Xyn10A had good stability at 75 degrees C, 80 degrees C, and pH 4.5-8.5, respectively, and was sensitive to various metal ions and reagents. Xyn10A possessed hydrolytic activity towards xylo-oligosaccharides (XOs) and beechwood xylan. At optimum conditions, the specific activity of Xyn10A was 44.6 IU/mg with beechwood xylan as substrate, and liberated branched XOs, xylobiose, and xylose. Agu67A was active on branched XOs with methyl-glucuronic acids (MeGlcA) sub-chains, and primarily generated XOs equivalents and MeGlcA. The specific activity of Agu67A was 1.3 IU/mg with aldobiouronic acid as substrate. The synergistic action of Xyn10A and Agu67A was observed with MeGlcA branched XOs and xylan as substrates, both backbone and branched chain of substrates were degraded, and liberated xylose, xylobiose, and MeGlcA. The synergism of Xyn10A and Agu67A provided not only a thermophilic method for natural xylan degradation, but also insight into the mechanisms for xylan utilization of C. lactoaceticus.
KeywordCellulase-free Xylanase Highly Thermostable Xylanase Alpha-glucuronidase Biochemical-characterization Schizophyllum-commune Structural Insights Neutral Xylanase Wheat-straw Purification Hydrolysis
SubtypeArticle
WOS HeadingsScience & Technology
DOI10.1371/journal.pone.0106482
URL查看原文
Indexed BySCI
Language英语
WOS KeywordCELLULASE-FREE XYLANASE ; HIGHLY THERMOSTABLE XYLANASE ; ALPHA-GLUCURONIDASE ; BIOCHEMICAL-CHARACTERIZATION ; SCHIZOPHYLLUM-COMMUNE ; STRUCTURAL INSIGHTS ; NEUTRAL XYLANASE ; WHEAT-STRAW ; PURIFICATION ; HYDROLYSIS
WOS Research AreaScience & Technology - Other Topics
WOS SubjectMultidisciplinary Sciences
WOS IDWOS:000341257700078
Citation statistics
Cited Times:6[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/11644
Collection研究所(批量导入)
Affiliation1.Chinese Acad Sci, Natl Key Lab Biochem Engn, Inst Proc Engn, Beijing, Peoples R China
2.Chinese Acad Agr Sci, Inst Agrofood Sci & Technol, Beijing 100193, Peoples R China
3.Shenyang Agr Univ, Coll Biosci & Biotechnol, Shenyang 110161, Peoples R China
Recommended Citation
GB/T 7714
Jia, Xiaojing,Mi, Shuofu,Wang, Jinzhi,et al. Insight into Glycoside Hydrolases for Debranched Xylan Degradation from Extremely Thermophilic Bacterium Caldicellulosiruptor lactoaceticus[J]. PLOS ONE,2014,9(9):12.
APA Jia, Xiaojing,Mi, Shuofu,Wang, Jinzhi,Qiao, Weibo,Peng, Xiaowei,&Han, Yejun.(2014).Insight into Glycoside Hydrolases for Debranched Xylan Degradation from Extremely Thermophilic Bacterium Caldicellulosiruptor lactoaceticus.PLOS ONE,9(9),12.
MLA Jia, Xiaojing,et al."Insight into Glycoside Hydrolases for Debranched Xylan Degradation from Extremely Thermophilic Bacterium Caldicellulosiruptor lactoaceticus".PLOS ONE 9.9(2014):12.
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