Cloning, expression, and characterization of a novel alkali-tolerant xylanase from alkaliphilic Bacillus sp SN5
文献类型：期刊论文
| 作者 | Bai, Wenqin1,2,3; Xue, Yanfen1; Zhou, Cheng1; Ma, Yanhe1 |
| 刊名 | BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
 |
| 出版日期 | 2015-03-01 |
| 卷号 | 62期号:2页码:208-217 |
| 关键词 | alkali tolerance carbohydrate-binding module catalytic domain xylanase |
| 英文摘要 | A xylanase gene (xyn11A) was cloned from the genomic library of alkalophilic Bacillus sp. SN5. It encoded a polypeptide of 366 amino acids, consisting of a family 11 glycoside hydrolase, a short linker region, and a family 36 carbohydrate-binding module (CBM). The intact xylanase Xyn11A and the CBM-linker-truncated Xyn11A-LC were expressed in Escherichia coli BL21 (DE3). Both purified recombinant proteins exhibited the highest activity at 55 degrees C. The optimal pH for Xyn11A activity was 7.5, whereas Xyn11A-LC showed a broad pH profile (>80% activity at pH 5.5-8.5) with optimal activity at pH 5.5 and 7.5-8.0. They had high alkali tolerance, retaining over 80% residual activity after preincubation at pH 8.5-11.0 at 37 degrees C for 1H. Xyn11A-LC showed better thermal stability, lower affinity, and lower catalytic activity to insoluble xylan than Xyn11A, whereas its specific activity for soluble beechwood xylan (4,511.9U/mg) was greater than that of Xyn11A (3,136.4U/mg). These results implied that the CBM of Xyn11A could change the enzymatic properties and play a role in degrading insoluble xylan. Xyn11A-LC is a family 11 alkali-tolerant cellulase-free xylanase with high specific activity, which qualifies it as a potential candidate for industrial applications, especially in the paper industry. (C) 2014 International Union of Biochemistry and Molecular Biology, Inc. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 关键词[WOS] | CARBOHYDRATE-BINDING MODULES ; PURIFICATION ; FAMILIES ; FUSION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000353164500008 |
| 源URL | [http://124.16.173.210/handle/834782/1457]  |
| 专题 | 天津工业生物技术研究所_酶工程实验室 马延和 _期刊论文 |
| 作者单位 | 1.Chinese Acad Sci, Inst Microbiol, Natl Engn Lab Ind Enzymes, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Natl Engn Lab Ind Enzymes, Tianjin Inst Ind Biotechnol, Tianjin, Peoples R China 3.Shanxi Normal Univ, Coll Life Sci, Linfen, Peoples R China |
| 推荐引用方式 GB/T 7714 | Bai, Wenqin,Xue, Yanfen,Zhou, Cheng,et al. Cloning, expression, and characterization of a novel alkali-tolerant xylanase from alkaliphilic Bacillus sp SN5[J]. BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY,2015,62(2):208-217. |
| APA | Bai, Wenqin,Xue, Yanfen,Zhou, Cheng,&Ma, Yanhe.(2015).Cloning, expression, and characterization of a novel alkali-tolerant xylanase from alkaliphilic Bacillus sp SN5.BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY,62(2),208-217. |
| MLA | Bai, Wenqin,et al."Cloning, expression, and characterization of a novel alkali-tolerant xylanase from alkaliphilic Bacillus sp SN5".BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY 62.2(2015):208-217. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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