Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 97, Issue 13, Pages 5839-5849Publisher
SPRINGER
DOI: 10.1007/s00253-012-4521-2
Keywords
Dye-decolorizing peroxidase; Redox potential; Phenolic and nonphenolic aromatics; High-redox potential dyes
Categories
Funding
- European Union
- Deutsche Bundesstiftung Umwelt (DBU) [13211-032]
- DFG (Deutsche Forschungsgemeinschaft) [1374, HO 1961/4-1]
- Deutscher Akademischer Austauschdienst (DAAD) [PPP 50151083]
- Bundesministerium fur Bildung und Forschung (BMBF) [VNM 09/014]
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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 pH2.5, and the oxidation of nonphenolic aromatic substrates (lignin model compounds) was optimal below pH3. 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.
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