Characterization of a new endo-type polyM-specific alginate lyase from Pseudomonas sp.

被引：50

作者：

Zhu, Ben-Wei ^{[1
,2
]}

Huang, Li-Shu-Xin ^{[1
,2
]}

Tan, Hai-Dong ^{[1
]}

Qin, Yu-Qi ^{[3
]}

Du, Yu-Guang ^{[1
,4
]}

Yin, Heng ^{[1
]}

机构：

[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

来源：

BIOTECHNOLOGY LETTERS | 2015年 / 37卷 / 02期

基金：

中国国家自然科学基金;

关键词：

Alginate lyase; Oligosaccharides; Poly-beta-D-mannuronate lyase; Pseudomonas mendocina; RAW264.7; CELLS; OLIGOSACCHARIDES; PURIFICATION; MANNURONATE; GULURONATE; INDUCTION; LINKAGES;

D O I：

10.1007/s10529-014-1685-0

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

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.

引用

页码：409 / 415

页数：7

共 50 条

[1] Characterization of a new endo-type polyM-specific alginate lyase from Pseudomonas sp.
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[J]. Biotechnology Letters, 2015, 37 : 409 - 415
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