Literature DB >> 26861852

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

Wenjun Zhu1, Yan Li1, Honghua Jia2, Ping Wei1, Hua Zhou1, Min Jiang1.   

Abstract

OBJECTIVE: A potential thermotolerant L-leucine dehydrogenase from Laceyella sacchari (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.

Entities:  

Keywords:  Halophilic thermophile; Laceyella sacchari; Leucine dehydrogenase; Thermostable dehydrogenase

Mesh:

Substances:

Year:  2016        PMID: 26861852     DOI: 10.1007/s10529-016-2053-z

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN: 0141-5492            Impact factor:   2.461


  3 in total

1.  Enhanced catalytic efficiency and coenzyme affinity of leucine dehydrogenase by comprehensive screening strategy for L-tert-leucine synthesis.

Authors:  Feng Zhou; Xiaoqing Mu; Yao Nie; Yan Xu
Journal:  Appl Microbiol Biotechnol       Date:  2021-04-30       Impact factor: 4.813

2.  A Novel Cold-Adapted Leucine Dehydrogenase from Antarctic Sea-Ice Bacterium Pseudoalteromonas sp. ANT178.

Authors:  Yatong Wang; Yanhua Hou; Yifan Wang; Lu Zheng; Xianlei Xu; Kang Pan; Rongqi Li; Quanfu Wang
Journal:  Mar Drugs       Date:  2018-10-01       Impact factor: 5.118

3.  Cloning and Expression of a Novel Leucine Dehydrogenase: Characterization and L-tert-Leucine Production.

Authors:  Wei Luo; Jing Zhu; Yuzheng Zhao; Huili Zhang; Xue Yang; Yuantao Liu; Zhiming Rao; Xiaobin Yu
Journal:  Front Bioeng Biotechnol       Date:  2020-03-31
  3 in total

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