Biochemical Characterization of Two Thermostable Xylanolytic Enzymes Encoded by a Gene Cluster of Caldicellulosiruptor owensensis
文献类型：期刊论文
| 作者 | Mi, Shuofu1; Jia, Xiaojing1; Wang, Jinzhi2; Qiao, Weibo1,3; Peng, Xiaowei1; Han, Yejun1 |
| 刊名 | PLOS ONE
 |
| 出版日期 | 2014-08-15 |
| 卷号 | 9期号:8页码:12 |
| 关键词 | GH39 BETA-XYLOSIDASE PLANT BIOMASS THERMOANAEROBACTERIUM-SACCHAROLYTICUM INDUSTRIAL APPLICATIONS GLYCOSIDE HYDROLASE STRUCTURAL INSIGHTS MICROBIAL XYLANASES ESCHERICHIA-COLI BACTERIUM CLONING |
| ISSN号 | 1932-6203 |
| 其他题名 | PLoS One |
| 中文摘要 | 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. |
| 英文摘要 | 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. |
| WOS标题词 | Science & Technology |
| 类目[WOS] | Multidisciplinary Sciences |
| 研究领域[WOS] | Science & Technology - Other Topics |
| 关键词[WOS] | GH39 BETA-XYLOSIDASE ; PLANT BIOMASS ; THERMOANAEROBACTERIUM-SACCHAROLYTICUM ; INDUSTRIAL APPLICATIONS ; GLYCOSIDE HYDROLASE ; STRUCTURAL INSIGHTS ; MICROBIAL XYLANASES ; ESCHERICHIA-COLI ; BACTERIUM ; CLONING |
| 收录类别 | SCI |
| 原文出处 | |
| 语种 | 英语 |
| WOS记录号 | WOS:000340879300099 |
| 公开日期 | 2014-09-30 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/11494]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | 1.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 |
| 推荐引用方式 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. |
入库方式： OAI收割
来源：过程工程研究所
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