Characterization of a new endo-type alginate lyase from Vibrio sp. W13

Benwei Zhu; Haidong Tan; Yuqi Qin; Qingsong Xu; Yuguang Du; Heng Yin

doi:10.1016/j.ijbiomac.2015.01.053

Characterization of a new endo-type alginate lyase from Vibrio sp. W13

Benwei Zhu, Haidong Tan, Yuqi Qin, Qingsong Xu, Yuguang Du, Heng Yin

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

75 Scopus citations

Abstract

A gene, encoding a new alginate lyase Algb, was identified and cloned from marine bacterium Vibrio sp. W13. The recombinant alginate lyase was characterized followed by being purified on Ni-NTA Sepharose. It exhibited the highest activity (457U/mg) at pH 8.0 and 30°C. Interestingly, Algb possessed broader substrate specificity. It showed activities toward both polyM (poly β-d-mannuronate) and polyG (poly α-l-guluronate). Furthermore, K_m values of Algb toward alginate (0.67mg/ml) and polyMG (0.50mg/ml) are lower than those toward polyG (1.04mg/ml) and polyM (6.90mg/ml). The TLC and ESI-MS analysis suggested that Algb mainly released oligosaccharides with DP of 2-5 from the four kinds of substrates in an endolytic manner. Therefore, it may be a potent tool to produce alginate oligosaccharides with low DP.

Original language	English
Pages (from-to)	330-337
Number of pages	8
Journal	International Journal of Biological Macromolecules
Volume	75
DOIs	https://doi.org/10.1016/j.ijbiomac.2015.01.053
State	Published - 1 Apr 2015
Externally published	Yes

Keywords

Alginate lyase
Polysaccharide lyase family 7
Vibrio sp

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/j.ijbiomac.2015.01.053

Cite this

@article{8bc8cca5df4849bab4ac5ee95a177896,

title = "Characterization of a new endo-type alginate lyase from Vibrio sp. W13",

abstract = "A gene, encoding a new alginate lyase Algb, was identified and cloned from marine bacterium Vibrio sp. W13. The recombinant alginate lyase was characterized followed by being purified on Ni-NTA Sepharose. It exhibited the highest activity (457U/mg) at pH 8.0 and 30°C. Interestingly, Algb possessed broader substrate specificity. It showed activities toward both polyM (poly β-d-mannuronate) and polyG (poly α-l-guluronate). Furthermore, Km values of Algb toward alginate (0.67mg/ml) and polyMG (0.50mg/ml) are lower than those toward polyG (1.04mg/ml) and polyM (6.90mg/ml). The TLC and ESI-MS analysis suggested that Algb mainly released oligosaccharides with DP of 2-5 from the four kinds of substrates in an endolytic manner. Therefore, it may be a potent tool to produce alginate oligosaccharides with low DP.",

keywords = "Alginate lyase, Polysaccharide lyase family 7, Vibrio sp",

author = "Benwei Zhu and Haidong Tan and Yuqi Qin and Qingsong Xu and Yuguang Du and Heng Yin",

note = "Publisher Copyright: {\textcopyright} 2015 Elsevier B.V.",

year = "2015",

month = apr,

day = "1",

doi = "10.1016/j.ijbiomac.2015.01.053",

language = "英语",

volume = "75",

pages = "330--337",

journal = "International Journal of Biological Macromolecules",

issn = "0141-8130",

publisher = "Elsevier B.V.",

}

TY - JOUR

T1 - Characterization of a new endo-type alginate lyase from Vibrio sp. W13

AU - Zhu, Benwei

AU - Tan, Haidong

AU - Qin, Yuqi

AU - Xu, Qingsong

AU - Du, Yuguang

AU - Yin, Heng

PY - 2015/4/1

Y1 - 2015/4/1

N2 - A gene, encoding a new alginate lyase Algb, was identified and cloned from marine bacterium Vibrio sp. W13. The recombinant alginate lyase was characterized followed by being purified on Ni-NTA Sepharose. It exhibited the highest activity (457U/mg) at pH 8.0 and 30°C. Interestingly, Algb possessed broader substrate specificity. It showed activities toward both polyM (poly β-d-mannuronate) and polyG (poly α-l-guluronate). Furthermore, Km values of Algb toward alginate (0.67mg/ml) and polyMG (0.50mg/ml) are lower than those toward polyG (1.04mg/ml) and polyM (6.90mg/ml). The TLC and ESI-MS analysis suggested that Algb mainly released oligosaccharides with DP of 2-5 from the four kinds of substrates in an endolytic manner. Therefore, it may be a potent tool to produce alginate oligosaccharides with low DP.

AB - A gene, encoding a new alginate lyase Algb, was identified and cloned from marine bacterium Vibrio sp. W13. The recombinant alginate lyase was characterized followed by being purified on Ni-NTA Sepharose. It exhibited the highest activity (457U/mg) at pH 8.0 and 30°C. Interestingly, Algb possessed broader substrate specificity. It showed activities toward both polyM (poly β-d-mannuronate) and polyG (poly α-l-guluronate). Furthermore, Km values of Algb toward alginate (0.67mg/ml) and polyMG (0.50mg/ml) are lower than those toward polyG (1.04mg/ml) and polyM (6.90mg/ml). The TLC and ESI-MS analysis suggested that Algb mainly released oligosaccharides with DP of 2-5 from the four kinds of substrates in an endolytic manner. Therefore, it may be a potent tool to produce alginate oligosaccharides with low DP.

KW - Alginate lyase

KW - Polysaccharide lyase family 7

KW - Vibrio sp

UR - http://www.scopus.com/inward/record.url?scp=84923016603&partnerID=8YFLogxK

U2 - 10.1016/j.ijbiomac.2015.01.053

DO - 10.1016/j.ijbiomac.2015.01.053

M3 - 文章

C2 - 25661880

AN - SCOPUS:84923016603

SN - 0141-8130

VL - 75

SP - 330

EP - 337

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

ER -

Characterization of a new endo-type alginate lyase from Vibrio sp. W13

Abstract

Keywords

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this