Journal Article

Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases

Pecyna, Marek J., Worrich, Anja, Zorn, Holger, Hofrichter, Martin, Liers, Christiane, Kellner, Harald, Steffen, Kari T., Ullrich, René

2013

Overview

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 (r Msc DyP; LDF), the wild-type Auricularia auricula-judae DyP ( Aau DyP; WRF), and two new DyPs secreted by the jelly fungi Exidia glandulosa ( Egl DyP; WRF) and Mycena epipterygia ( Mep DyP; 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 Aau DyP, Mep DyP, and Egl DyP 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 ( Pch LiP; WRF), versatile peroxidase of Bjerkandera adusta ( Bad VP; 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.

• Publisher: Springer-Verlag,Springer,Springer Nature B.V
• Subject: Analysis / Aromatic compounds / Auricularia / Basidiomycota / Basidiomycota - enzymology / Biomedical and Life Sciences / Biosynthesis / Biotechnologically Relevant Enzymes and Proteins / Biotechnology / Bjerkandera adusta / Catalysis / chemistry / Chromatography / Chromatography, Liquid / Coloring Agents / Coloring Agents - metabolism / Coprinopsis / Decoloring / Dyes / Environmental science / Enzymatic activity / enzyme activity / Enzyme Stability / Enzymes / enzymology / Exidia / Fungi / Genetic recombination / Glycine max / Heme / Homology / Hydrogen-Ion Concentration / isolation & purification / Life Sciences / Lignin / Lignin peroxidase / Liquid chromatography / Litter / metabolism / Microbial Genetics and Genomics / Microbiology / Models, Molecular / Molecular Weight / Mycena / Oxidation / Oxidation-Reduction / Peptides / Peroxidase / Peroxidases / Peroxidases - chemistry / Peroxidases - isolation & purification / Peroxidases - metabolism / pH effects / Phanerochaete chrysosporium / Phenolic compounds / Phenols / Physicochemical properties / Protein Conformation / Proteins / Sequence Homology, Amino Acid / Sequences / Soybeans / Studies / White rot / White rot fungi / Wood