Cloning, expression and characterization of a halotolerant esterase from a marine bacterium Pelagibacterium halotolerans B2T

@article{Jiang2012CloningEA,
  title={Cloning, expression and characterization of a halotolerant esterase from a marine bacterium Pelagibacterium halotolerans B2T},
  author={Xiawei Jiang and Yingyi Huo and H. Cheng and Xinqi Zhang and Xufen Zhu and Min Wu},
  journal={Extremophiles},
  year={2012},
  volume={16},
  pages={427-435}
}
  • Xiawei Jiang, Yingyi Huo, +3 authors Min Wu
  • Published 2012
  • Biology, Medicine
  • Extremophiles
  • An esterase PE10 (279 aa) from Pelagibacterium halotolerans B2T was cloned and overexpressed in Escherichia coli Rosetta in a soluble form. The deduced protein was 29.91 kDa and the phylogenetic analysis of the deduced amino acids sequence showed it represented a new family of lipolytic enzymes. The recombinant protein was purified by Ni–NTA affinity chromatography column and the characterization showed its optimal temperature and pH were 45 °C and pH 7.5, respectively. Substrate specificity… CONTINUE READING
    36 Citations

    Figures, Tables, and Topics from this paper

    A Novel Halotolerant Thermoalkaliphilic Esterase from Marine Bacterium Erythrobacter seohaensis SW-135
    • 8
    • PDF
    Characterization of ML-005, a Novel Metaproteomics-Derived Esterase
    • 2
    • PDF

    References

    SHOWING 1-10 OF 49 REFERENCES
    Characterization of alcohol dehydrogenase from the haloalkaliphilic archaeon Natronomonas pharaonis
    • 25
    Extremely thermostable esterases from the thermoacidophilic euryarchaeon Picrophilus torridus
    • 57
    First evidence for the salt-dependent folding and activity of an esterase from the halophilic archaea Haloarcula marismortui.
    • 74
    • Highly Influential
    Functional expression and refolding of new alkaline esterase, EM2L8 from deep-sea sediment metagenome.
    • 90
    • Highly Influential
    Solution Behavior and Activity of a Halophilic Esterase under High Salt Concentration
    • 58
    • PDF