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Characterization of a new endo-type polyM-specific alginate lyase from Pseudomonas sp.
Alternative TitleBiotechnol. Lett.
Zhu, Ben-Wei1,2; Huang, Li-Shu-Xin1,2; Tan, Hai-Dong1; Qin, Yu-Qi3; Du, Yu-Guang1,4; Yin, Heng1
2015-02-01
Source PublicationBIOTECHNOLOGY LETTERS
ISSN0141-5492
Volume37Issue:2Pages:409-415
AbstractAn 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.; 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.
KeywordAlginate Lyase Oligosaccharides Poly-beta-d-mannuronate Lyase Pseudomonas Mendocina
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.1007/s10529-014-1685-0
URL查看原文
Indexed BySCI
Language英语
WOS KeywordRAW264.7 CELLS ; OLIGOSACCHARIDES ; PURIFICATION ; MANNURONATE ; GULURONATE ; INDUCTION ; LINKAGES
WOS Research AreaBiotechnology & Applied Microbiology
WOS SubjectBiotechnology & Applied Microbiology
WOS IDWOS:000349230800020
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/11907
Collection研究所(批量导入)
Affiliation1.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
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.
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