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

Ben Wei Zhu; Li Shu Xin Huang; Hai Dong Tan; Yu Qi Qin; Yu Guang Du; Heng Yin

doi:10.1007/s10529-014-1685-0

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

Ben Wei Zhu, Li Shu Xin Huang, Hai Dong Tan, Yu Qi Qin, Yu Guang Du, Heng Yin

Research output: Contribution to journal › Article › peer-review

55 Scopus citations

Abstract

An alginate lyase gene, algA, encoding a new poly β-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 °C and also maintained activity between pH 7–9 and below 45 °C. It exclusively and endolytically depolymerized polyM by β-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.

Original language	English
Pages (from-to)	409-415
Number of pages	7
Journal	Biotechnology Letters
Volume	37
Issue number	2
DOIs	https://doi.org/10.1007/s10529-014-1685-0
State	Published - Feb 2015
Externally published	Yes

Keywords

Alginate lyase
Oligosaccharides
Poly-β-d-mannuronate lyase
Pseudomonas mendocina

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10.1007/s10529-014-1685-0

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title = "Characterization of a new endo-type polyM-specific alginate lyase from Pseudomonas sp",

abstract = "An alginate lyase gene, algA, encoding a new poly β-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 °C and also maintained activity between pH 7–9 and below 45 °C. It exclusively and endolytically depolymerized polyM by β-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.",

keywords = "Alginate lyase, Oligosaccharides, Poly-β-d-mannuronate lyase, Pseudomonas mendocina",

author = "Zhu, {Ben Wei} and Huang, {Li Shu Xin} and Tan, {Hai Dong} and Qin, {Yu Qi} and Du, {Yu Guang} and Heng Yin",

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doi = "10.1007/s10529-014-1685-0",

language = "英语",

volume = "37",

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T1 - Characterization of a new endo-type polyM-specific alginate lyase from Pseudomonas sp

AU - Zhu, Ben Wei

AU - Huang, Li Shu Xin

AU - Tan, Hai Dong

AU - Qin, Yu Qi

AU - Du, Yu Guang

AU - Yin, Heng

PY - 2015/2

Y1 - 2015/2

N2 - An alginate lyase gene, algA, encoding a new poly β-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 °C and also maintained activity between pH 7–9 and below 45 °C. It exclusively and endolytically depolymerized polyM by β-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.

AB - An alginate lyase gene, algA, encoding a new poly β-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 °C and also maintained activity between pH 7–9 and below 45 °C. It exclusively and endolytically depolymerized polyM by β-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.

KW - Alginate lyase

KW - Oligosaccharides

KW - Poly-β-d-mannuronate lyase

KW - Pseudomonas mendocina

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U2 - 10.1007/s10529-014-1685-0

DO - 10.1007/s10529-014-1685-0

M3 - 文章

C2 - 25257600

AN - SCOPUS:84925482907

SN - 0141-5492

VL - 37

SP - 409

EP - 415

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 2

ER -

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

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Keywords

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