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题名: Characterization of a new endo-type polyM-specific alginate lyase from Pseudomonas sp.
作者: Zhu, Ben-Wei1, 2;  Huang, Li-Shu-Xin1, 2;  Tan, Hai-Dong1;  Qin, Yu-Qi3;  Du, Yu-Guang1, 4;  Yin, Heng1
关键词: Alginate lyase ;  Oligosaccharides ;  Poly-beta-D-mannuronate lyase ;  Pseudomonas mendocina
刊名: BIOTECHNOLOGY LETTERS
发表日期: 2015-02-01
DOI: 10.1007/s10529-014-1685-0
卷: 37, 期:2, 页:409-415
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine
类目[WOS]: Biotechnology & Applied Microbiology
研究领域[WOS]: Biotechnology & Applied Microbiology
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.
关键词[WOS]: RAW264.7 CELLS ;  OLIGOSACCHARIDES ;  PURIFICATION ;  MANNURONATE ;  GULURONATE ;  INDUCTION ;  LINKAGES
语种: 英语
WOS记录号: WOS:000349230800020
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/145976
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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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

Recommended Citation:
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.
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