Expression, purification and characterization of a thermostable leucine dehydrogenase from the halophilic thermophile Laceyella sacchari

Wenjun Zhu; Yan Li; Honghua Jia; Ping Wei; Hua Zhou; Min Jiang

doi:10.1007/s10529-016-2053-z

Expression, purification and characterization of a thermostable leucine dehydrogenase from the halophilic thermophile Laceyella sacchari

Wenjun Zhu, Yan Li, Honghua Jia, Ping Wei, Hua Zhou, Min Jiang

COLLEGE OF BIOTECHNOLOGY AND PHARMACEUTICAL ENGINEERING

Nanjing Tech University

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

18 Scopus citations

Abstract

Objective: A potential thermotolerant l-leucine dehydrogenase from Laceyellasacchari (Ls-LeuDH) was over-expressed in E. coli, purified and characterized. Results: Ls-LeuDH had excellent thermostability with a specific activity of 183 U/mg at pH 10.5 and 25 °C. It retained a high activity in 200 mM carbonate buffer from pH 9.5 to 11. The optimal temperature for Ls-LeuDH was 60 °C. Conclusion: It is the first time that a thermostable and highly active LeuDH originating from L. sacchari has been characterized. It may be useful for medical and pharmaceutical applications.

Original language	English
Pages (from-to)	855-861
Number of pages	7
Journal	Biotechnology Letters
Volume	38
Issue number	5
DOIs	https://doi.org/10.1007/s10529-016-2053-z
State	Published - 1 May 2016

Keywords

Halophilic thermophile
Laceyellasacchari
Leucine dehydrogenase
Thermostable dehydrogenase

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title = "Expression, purification and characterization of a thermostable leucine dehydrogenase from the halophilic thermophile Laceyella sacchari",

abstract = "Objective: A potential thermotolerant l-leucine dehydrogenase from Laceyellasacchari (Ls-LeuDH) was over-expressed in E. coli, purified and characterized. Results: Ls-LeuDH had excellent thermostability with a specific activity of 183 U/mg at pH 10.5 and 25 °C. It retained a high activity in 200 mM carbonate buffer from pH 9.5 to 11. The optimal temperature for Ls-LeuDH was 60 °C. Conclusion: It is the first time that a thermostable and highly active LeuDH originating from L. sacchari has been characterized. It may be useful for medical and pharmaceutical applications.",

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T1 - Expression, purification and characterization of a thermostable leucine dehydrogenase from the halophilic thermophile Laceyella sacchari

AU - Zhu, Wenjun

AU - Li, Yan

AU - Jia, Honghua

AU - Wei, Ping

AU - Zhou, Hua

AU - Jiang, Min

PY - 2016/5/1

Y1 - 2016/5/1

N2 - Objective: A potential thermotolerant l-leucine dehydrogenase from Laceyellasacchari (Ls-LeuDH) was over-expressed in E. coli, purified and characterized. Results: Ls-LeuDH had excellent thermostability with a specific activity of 183 U/mg at pH 10.5 and 25 °C. It retained a high activity in 200 mM carbonate buffer from pH 9.5 to 11. The optimal temperature for Ls-LeuDH was 60 °C. Conclusion: It is the first time that a thermostable and highly active LeuDH originating from L. sacchari has been characterized. It may be useful for medical and pharmaceutical applications.

AB - Objective: A potential thermotolerant l-leucine dehydrogenase from Laceyellasacchari (Ls-LeuDH) was over-expressed in E. coli, purified and characterized. Results: Ls-LeuDH had excellent thermostability with a specific activity of 183 U/mg at pH 10.5 and 25 °C. It retained a high activity in 200 mM carbonate buffer from pH 9.5 to 11. The optimal temperature for Ls-LeuDH was 60 °C. Conclusion: It is the first time that a thermostable and highly active LeuDH originating from L. sacchari has been characterized. It may be useful for medical and pharmaceutical applications.

KW - Halophilic thermophile

KW - Laceyellasacchari

KW - Leucine dehydrogenase

KW - Thermostable dehydrogenase

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DO - 10.1007/s10529-016-2053-z

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SN - 0141-5492

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JO - Biotechnology Letters

JF - Biotechnology Letters

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Expression, purification and characterization of a thermostable leucine dehydrogenase from the halophilic thermophile Laceyella sacchari

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