Characterization of a new endo-type polyM-specific alginate lyase from Pseudomonas sp.
文献类型：期刊论文
| 作者 | Zhu, Ben-Wei1,2; Huang, Li-Shu-Xin1,2; Tan, Hai-Dong1; Qin, Yu-Qi3; Du, Yu-Guang1,4; Yin, Heng1 |
| 刊名 | BIOTECHNOLOGY LETTERS
 |
| 出版日期 | 2015-02-01 |
| 卷号 | 37期号:2页码:409-415 |
| 关键词 | Alginate lyase Oligosaccharides Poly-beta-D-mannuronate lyase Pseudomonas mendocina |
| ISSN号 | 0141-5492 |
| 其他题名 | Biotechnol. Lett. |
| 中文摘要 | An alginate lyase gene, algA, encoding a new poly beta-d-mannuronate (polyM)-specific alginate lyase AlgA, was cloned from Pseudomonas sp. E03. The recombinant AlgA with (His)(6)-tag, consisting of 364 amino acids (40.4 kDa),was purified using Ni-NTA Sepharose. The purified lyase had maximal activity (222 EU/mg) at pH 8 and 30 A degrees C and also maintained activity between pH 7-9 and below 45 A degrees C. It exclusively and endolytically depolymerized polyM by beta-elimination into oligosaccharides with degrees of polymerization (DP) of 2-5. Due to its high substrate specificity, AlgA could be a valuable tool for production of polyM oligosaccharides with low DP and for determining the fine structure of alginate. |
| 英文摘要 | An alginate lyase gene, algA, encoding a new poly beta-d-mannuronate (polyM)-specific alginate lyase AlgA, was cloned from Pseudomonas sp. E03. The recombinant AlgA with (His)(6)-tag, consisting of 364 amino acids (40.4 kDa),was purified using Ni-NTA Sepharose. The purified lyase had maximal activity (222 EU/mg) at pH 8 and 30 A degrees C and also maintained activity between pH 7-9 and below 45 A degrees C. It exclusively and endolytically depolymerized polyM by beta-elimination into oligosaccharides with degrees of polymerization (DP) of 2-5. Due to its high substrate specificity, AlgA could be a valuable tool for production of polyM oligosaccharides with low DP and for determining the fine structure of alginate. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biotechnology & Applied Microbiology |
| 研究领域[WOS] | Biotechnology & Applied Microbiology |
| 关键词[WOS] | RAW264.7 CELLS ; OLIGOSACCHARIDES ; PURIFICATION ; MANNURONATE ; GULURONATE ; INDUCTION ; LINKAGES |
| 收录类别 | SCI |
| 原文出处 | |
| 语种 | 英语 |
| WOS记录号 | WOS:000349230800020 |
| 公开日期 | 2015-04-01 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/11907]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | 1.Chinese Acad Sci, Nat Prod & Glycobiotechnol Res Grp, Liaoning Prov Key Lab Carbohydrates, Dalian Inst Chem Phys, Dalian 116023, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.Natl Glycoengn Res Ctr, Jinan 250100, Peoples R China 4.Chinese Acad Sci, Inst Proc Engn, Beijing 100190, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhu, Ben-Wei,Huang, Li-Shu-Xin,Tan, Hai-Dong,et al. Characterization of a new endo-type polyM-specific alginate lyase from Pseudomonas sp.[J]. BIOTECHNOLOGY LETTERS,2015,37(2):409-415. |
| APA | Zhu, Ben-Wei,Huang, Li-Shu-Xin,Tan, Hai-Dong,Qin, Yu-Qi,Du, Yu-Guang,&Yin, Heng.(2015).Characterization of a new endo-type polyM-specific alginate lyase from Pseudomonas sp..BIOTECHNOLOGY LETTERS,37(2),409-415. |
| MLA | Zhu, Ben-Wei,et al."Characterization of a new endo-type polyM-specific alginate lyase from Pseudomonas sp.".BIOTECHNOLOGY LETTERS 37.2(2015):409-415. |
入库方式： OAI收割
来源：过程工程研究所
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