Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases
Autor: | Holger Zorn, Martin Hofrichter, Christiane Liers, Anja Worrich, Kari Steffen, René Ullrich, Harald Kellner, Marek J. Pecyna |
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Jazyk: | angličtina |
Rok vydání: | 2012 |
Předmět: |
Models
Molecular Protein Conformation Applied Microbiology and Biotechnology 03 medical and health sciences chemistry.chemical_compound Bjerkandera adusta Enzyme Stability Lignin Organic chemistry Versatile peroxidase Coloring Agents 030304 developmental biology Dye decolorizing peroxidase 0303 health sciences biology Sequence Homology Amino Acid 030306 microbiology Chemistry Basidiomycota General Medicine Lignin peroxidase Hydrogen-Ion Concentration biology.organism_classification Molecular Weight Coprinopsis cinerea Biochemistry Peroxidases biology.protein Phanerochaete Oxidation-Reduction Biotechnology Peroxidase Chromatography Liquid |
Zdroj: | Applied Microbiology and Biotechnology |
ISSN: | 1432-0614 0175-7598 |
DOI: | 10.1007/s00253-012-4521-2 |
Popis: | Catalytic and physicochemical properties of representative fungal dye-decolorizing peroxidases (DyPs) of wood- (WRF) and litter-decomposing white-rot fungi (LDF) are summarized and compared, including one recombinant Mycetinis scorodonius DyP (rMscDyP; LDF), the wild-type Auricularia auricula-judae DyP (AauDyP; WRF), and two new DyPs secreted by the jelly fungi Exidia glandulosa (EglDyP; WRF) and Mycena epipterygia (MepDyP; LDF). Homogeneous preparations of these DyPs were obtained after different steps of fast protein liquid chromatography, and they increase the total number of characterized fungal DyP proteins to eight. The peptide sequences of AauDyP, MepDyP, and EglDyP showed highest homologies (52–56 %) to the DyPs of M. scorodonius. Five out of the eight characterized fungal DyPs were used to evaluate their catalytic properties compared to classic fungal and plant heme peroxidases, namely lignin peroxidase of Phanerochaete chrysosporium (PchLiP; WRF), versatile peroxidase of Bjerkandera adusta (BadVP; WRF), and generic peroxidases of Coprinopsis cinerea (CiP) and Glycine max (soybean peroxidase = SBP). All DyPs tested possess unique properties regarding the stability at low pH values: 50–90 % enzymatic activity remained after 4-h exposition at pH 2.5, and the oxidation of nonphenolic aromatic substrates (lignin model compounds) was optimal below pH 3. Furthermore, all DyPs efficiently oxidized recalcitrant dyes (e.g., Azure B) as well as the phenolic substrate 2,6-dimethoxyphenol. Thus, DyPs combine features of different peroxidases on the functional level and may be part of the biocatalytic system secreted by fungi for the oxidation of lignin and/or toxic aromatic compounds. |
Databáze: | OpenAIRE |
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