Characterization of a new oligoalginate lyase from marine bacterium Vibrio sp.

Zuochen Yu; Benwei Zhu; Wenxia Wang; Haidong Tan; Heng Yin

doi:10.1016/j.ijbiomac.2018.02.046

Characterization of a new oligoalginate lyase from marine bacterium Vibrio sp.

Zuochen Yu, Benwei Zhu, Wenxia Wang, Haidong Tan, Heng Yin

COLLEGE OF FOOD SCIENCE AND LIGHT INDUSTRY

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

20 Scopus citations

Abstract

A new oligoalginate lyase encoding gene, designed oal17A, was cloned from marine bacterium Vibrio sp. W13, and then expressed in Escherichia coli. The recombinant Oal17A was purified by NTA-Ni resin with maximal activity at 30 °C and pH 7.0. Oal17A exhibited broad substrate specificity, and preferred to degrade alginate than polyM or polyG into monosaccharide acid. The specific activity of Oal17A toward alginate, polyM and polyG was 21.14 U/mg, 12.31 U/mg and 7.43 U/mg, respectively. With features of high-level expression and broad substrate specificity, Oal17A would be a potential tool for alginate monomer production process of alginate utilizing for biofuels and bioethanol production.

Original language	English
Pages (from-to)	937-942
Number of pages	6
Journal	International Journal of Biological Macromolecules
Volume	112
DOIs	https://doi.org/10.1016/j.ijbiomac.2018.02.046
State	Published - Jun 2018

Keywords

Alginate
Monosaccharide
Oligoalginate lyase

UN SDGs

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

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10.1016/j.ijbiomac.2018.02.046

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title = "Characterization of a new oligoalginate lyase from marine bacterium Vibrio sp.",

abstract = "A new oligoalginate lyase encoding gene, designed oal17A, was cloned from marine bacterium Vibrio sp. W13, and then expressed in Escherichia coli. The recombinant Oal17A was purified by NTA-Ni resin with maximal activity at 30 °C and pH 7.0. Oal17A exhibited broad substrate specificity, and preferred to degrade alginate than polyM or polyG into monosaccharide acid. The specific activity of Oal17A toward alginate, polyM and polyG was 21.14 U/mg, 12.31 U/mg and 7.43 U/mg, respectively. With features of high-level expression and broad substrate specificity, Oal17A would be a potential tool for alginate monomer production process of alginate utilizing for biofuels and bioethanol production.",

keywords = "Alginate, Monosaccharide, Oligoalginate lyase",

author = "Zuochen Yu and Benwei Zhu and Wenxia Wang and Haidong Tan and Heng Yin",

note = "Publisher Copyright: {\textcopyright} 2018 Elsevier B.V.",

year = "2018",

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doi = "10.1016/j.ijbiomac.2018.02.046",

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volume = "112",

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TY - JOUR

T1 - Characterization of a new oligoalginate lyase from marine bacterium Vibrio sp.

AU - Yu, Zuochen

AU - Zhu, Benwei

AU - Wang, Wenxia

AU - Tan, Haidong

AU - Yin, Heng

PY - 2018/6

Y1 - 2018/6

N2 - A new oligoalginate lyase encoding gene, designed oal17A, was cloned from marine bacterium Vibrio sp. W13, and then expressed in Escherichia coli. The recombinant Oal17A was purified by NTA-Ni resin with maximal activity at 30 °C and pH 7.0. Oal17A exhibited broad substrate specificity, and preferred to degrade alginate than polyM or polyG into monosaccharide acid. The specific activity of Oal17A toward alginate, polyM and polyG was 21.14 U/mg, 12.31 U/mg and 7.43 U/mg, respectively. With features of high-level expression and broad substrate specificity, Oal17A would be a potential tool for alginate monomer production process of alginate utilizing for biofuels and bioethanol production.

AB - A new oligoalginate lyase encoding gene, designed oal17A, was cloned from marine bacterium Vibrio sp. W13, and then expressed in Escherichia coli. The recombinant Oal17A was purified by NTA-Ni resin with maximal activity at 30 °C and pH 7.0. Oal17A exhibited broad substrate specificity, and preferred to degrade alginate than polyM or polyG into monosaccharide acid. The specific activity of Oal17A toward alginate, polyM and polyG was 21.14 U/mg, 12.31 U/mg and 7.43 U/mg, respectively. With features of high-level expression and broad substrate specificity, Oal17A would be a potential tool for alginate monomer production process of alginate utilizing for biofuels and bioethanol production.

KW - Alginate

KW - Monosaccharide

KW - Oligoalginate lyase

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U2 - 10.1016/j.ijbiomac.2018.02.046

DO - 10.1016/j.ijbiomac.2018.02.046

M3 - 文章

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AN - SCOPUS:85042227157

SN - 0141-8130

VL - 112

SP - 937

EP - 942

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

ER -

Characterization of a new oligoalginate lyase from marine bacterium Vibrio sp.

Abstract

Keywords

UN SDGs

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