Applied Microbiology and Biotechnology

, Volume 85, Issue 6, pp 1869–1879 | Cite as

DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes

  • Christiane Liers
  • Caroline Bobeth
  • Marek Pecyna
  • René Ullrich
  • Martin Hofrichter
Biotechnologically Relevant Enzymes and Proteins

Abstract

The jelly fungus Auricularia auricula-judae produced an enzyme with manganese-independent peroxidase activity during growth on beech wood (∼300 U l−1). The same enzymatic activity was detected and produced at larger scale in agitated cultures comprising of liquid, plant-based media (e.g. tomato juice suspensions) at levels up to 8,000 U l−1. Two pure peroxidase forms (A. auricula-judae peroxidase (AjP I and AjP II) could be obtained from respective culture liquids by three chromatographic steps. Spectroscopic and electrophoretic analyses of the purified proteins revealed their heme and peroxidase nature. The N-terminal amino acid sequence of AjP matched well with sequences of fungal enzymes known as “dye-decolorizing peroxidases”. Homology was found to the N-termini of peroxidases from Marasmius scorodonius (up to 86%), Thanatephorus cucumeris (60%), and Termitomyces albuminosus (60%). Both enzyme forms catalyzed not only the conversion of typical peroxidase substrates such as 2,6-dimethoxyphenol and 2,2′-azino-bis(3-ethylthiazoline-6-sulfonate) but also the decolorization of the high-redox potential dyes Reactive Blue 5 and Reactive Black 5, whereas manganese(II) ions (Mn2+) were not oxidized. Most remarkable, however, is the finding that both AjPs oxidized nonphenolic lignin model compounds (veratryl alcohol; adlerol, a nonphenolic β-O-4 lignin model dimer) at low pH (maximum activity at pH 1.4), which indicates a certain ligninolytic activity of dye-decolorizing peroxidases.

Keywords

Dye-decolorizing peroxidases Jelly fungi White rot Nonphenolic β-O-4 lignin model compound Azo and anthraquinone dyes 

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Copyright information

© Springer-Verlag 2009

Authors and Affiliations

  • Christiane Liers
    • 1
  • Caroline Bobeth
    • 1
  • Marek Pecyna
    • 1
  • René Ullrich
    • 1
  • Martin Hofrichter
    • 1
  1. 1.Unit of Environmental BiotechnologyInternational Graduate School of ZittauZittauGermany

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