Insight into Glycoside Hydrolases for Debranched Xylan Degradation from Extremely Thermophilic Bacterium Caldicellulosiruptor lactoaceticus
文献类型：期刊论文
| 作者 | Jia, Xiaojing1; Mi, Shuofu1; Wang, Jinzhi2; Qiao, Weibo1,3; Peng, Xiaowei1; Han, Yejun1 |
| 刊名 | PLOS ONE
 |
| 出版日期 | 2014-09-03 |
| 卷号 | 9期号:9页码:12 |
| 关键词 | CELLULASE-FREE XYLANASE HIGHLY THERMOSTABLE XYLANASE ALPHA-GLUCURONIDASE BIOCHEMICAL-CHARACTERIZATION SCHIZOPHYLLUM-COMMUNE STRUCTURAL INSIGHTS NEUTRAL XYLANASE WHEAT-STRAW PURIFICATION HYDROLYSIS |
| ISSN号 | 1932-6203 |
| 其他题名 | PLoS One |
| 中文摘要 | 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. |
| 英文摘要 | 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. |
| WOS标题词 | Science & Technology |
| 类目[WOS] | Multidisciplinary Sciences |
| 研究领域[WOS] | Science & Technology - Other Topics |
| 关键词[WOS] | CELLULASE-FREE XYLANASE ; HIGHLY THERMOSTABLE XYLANASE ; ALPHA-GLUCURONIDASE ; BIOCHEMICAL-CHARACTERIZATION ; SCHIZOPHYLLUM-COMMUNE ; STRUCTURAL INSIGHTS ; NEUTRAL XYLANASE ; WHEAT-STRAW ; PURIFICATION ; HYDROLYSIS |
| 收录类别 | SCI |
| 原文出处 | |
| 语种 | 英语 |
| WOS记录号 | WOS:000341257700078 |
| 公开日期 | 2014-11-02 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/11644]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | 1.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 |
| 推荐引用方式 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. |
入库方式： OAI收割
来源：过程工程研究所
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