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  • Engineering Towards Catalytic Use of Fungal Class-II Peroxidases for Dye-Decolorizing and Conversion of Lignin Model Compounds

    Author(s)
    Lundell, Taina
    Bentley, Elodie
    Hilden, Kristiina
    Rytioja, Johanna
    Kuuskeri, Jaana
    Ufot, Usenobong F.
    Nousiainen, Paula
    Hofrichter, Martin
    Wahlsten, Matti
    Doyle, Wendy
    Smith, Andrew T.
    Griffith University Author(s)
    Smith, Andrew T.
    Year published
    2017
    Metadata
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    Abstract
    Background: Manganese peroxidases (MnP) and lignin peroxidases (LiP) are haem-including fungal secreted class-II peroxidases, which are interesting oxidoreductases in protein engineering aimed at designing of biocatalysts for lignin and lignocellulose conversion, dye compound degradation, activation of aromatic compounds, and biofuel production. Objective. Recombinant short-type MnP (Pr-MnP3) of the white rot fungus Phlebia radiata, and its manganese- binding site (E40, E44, D186) directed variants were produced and characterized. To allow catalytic applications, enzymatic bleaching of Reactive Blue 5 and conversion of ...
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    Background: Manganese peroxidases (MnP) and lignin peroxidases (LiP) are haem-including fungal secreted class-II peroxidases, which are interesting oxidoreductases in protein engineering aimed at designing of biocatalysts for lignin and lignocellulose conversion, dye compound degradation, activation of aromatic compounds, and biofuel production. Objective. Recombinant short-type MnP (Pr-MnP3) of the white rot fungus Phlebia radiata, and its manganese- binding site (E40, E44, D186) directed variants were produced and characterized. To allow catalytic applications, enzymatic bleaching of Reactive Blue 5 and conversion of lignin-like compounds by engineered class- II peroxidases were explored. Method: Pr-MnP3 and its variants were expressed in Escherichia coli. The resultant body proteins were lysed, purified and refolded into haem-including enzymes in 6-7% protein recovery, and examined spectroscopically and kinetically. Results: Successful production of active enzymes was attained, with spectral characteristics of high-spin class-II peroxidases. Recombinant Pr-MnP3 demonstrated high affinity to Mn2+, which was noticeably affected by single (D186H/N) and double (E40H+E44H) mutations. Without addition of Mn2+, Pr- MnP3 was able to oxidize ABTS and decolorize Reactive Blue 5. Pc-LiPH8, its Trp-radical site variants, and engineered CiP-LiP demonstrated conversion of veratryl alcohol and dimeric non-phenolic lignin-model compounds (arylglycerol-β-aryl ethers) with production of veratraldehyde, which is evidence for cation radical formation with subsequent Cα-Cβ cleavage. Pc-LiPH8 and CiP variants were able to effectively oxidize and convert the phenolic dimer (guaiacylglycerol-β-guaiacyl ether). Conclusion: Our results demonstrate suitability of engineered MnP and LiP peroxidases for dyedecolorizing, and efficiency of LiP and its variants for activation and degradation of phenolic and nonphenolic lignin-like aryl ether-linked compounds.
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    Journal Title
    Current Biotechnology
    Volume
    6
    Issue
    2
    DOI
    https://doi.org/10.2174/2211550105666160520120101
    Subject
    Medicinal and Biomolecular Chemistry not elsewhere classified
    Biological Sciences
    Technology
    Publication URI
    http://hdl.handle.net/10072/337474
    Collection
    • Journal articles

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