Number of the records: 1  

Galactose Oxidase from Fusarium oxysporum - Expression in E. coli and P. pastoris and Biochemical Characterization

  1. 1.
    SYSNO ASEP0440666
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleGalactose Oxidase from Fusarium oxysporum - Expression in E. coli and P. pastoris and Biochemical Characterization
    Author(s) Paukner, R. (AT)
    Staudigl, P. (AT)
    Choosri, W. (TH)
    Sygmund, Ch. (AT)
    Halada, Petr (MBU-M) RID, ORCID
    Haltrich, D. (AT)
    Leitner, CH. (AT)
    Number of authors7
    Source TitlePLoS ONE. - : Public Library of Science - ISSN 1932-6203
    Roč. 9, č. 6 (2014)
    Number of pages8 s.
    Languageeng - English
    CountryUS - United States
    Keywordsgalactose oxidase ; gene ; Fusarium ; gene expression
    Subject RIVCE - Biochemistry
    Institutional supportMBU-M - RVO:61388971
    UT WOS000338280800025
    AnnotationA gene coding for galactose 6-oxidase from Fusarium oxysporum G12 was cloned together with its native preprosequence and a C-terminal His-tag, and successfully expressed both in Escherichia coli and Pichia pastoris. The enzyme was subsequently purified and characterized. Among all tested substrates, the highest catalytic efficiency (k(cat)/K-m) was found with 1-methyl-beta-D-galactopyranoside (2.2 mM(-1) s(-1)). The Michaelis constant (K-m) for D-galactose was determined to be 47 mM. Optimal pH and temperature for the enzyme activity were 7.0 and 40 degrees C, respectively, and the enzyme was thermoinactivated at temperatures above 50 degrees C. GalOx contains a unique metalloradical complex consisting of a copper atom and a tyrosine residue covalently attached to the sulphur of a cysteine. The correct formation of this thioether bond during the heterologous expression in E. coli and P. pastoris could be unequivocally confirmed by MALDI mass spectrometry, which offers a convenient alternative to prove this Tyr-Cys crosslink, which is essential for the catalytic activity of GalOx.
    WorkplaceInstitute of Microbiology
    ContactEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Year of Publishing2015
Number of the records: 1  

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