Fungal dye-decolorizing peroxidase diversity: roles in either intra- or extracellular processes

Publikation: Beitrag in FachzeitschriftForschungsartikelBeigetragenBegutachtung


  • Martino Adamo - , University of Turin, Universite Claude Bernard Lyon 1 (Autor:in)
  • Sophie Comtet-Marre - , Université Clermont Auvergne (Autor:in)
  • Enrico Büttner - , Professur für Umweltbiotechnologie (Autor:in)
  • Harald Kellner - , Professur für Umweltbiotechnologie (Autor:in)
  • Patricia Luis - , Universite Claude Bernard Lyon 1 (Autor:in)
  • Laurent Vallon - , Universite Claude Bernard Lyon 1 (Autor:in)
  • Rocio Prego - , Université Clermont Auvergne (Autor:in)
  • Martin Hofrichter - , Professur für Umweltbiotechnologie (Autor:in)
  • Mariangela Girlanda - , University of Turin (Autor:in)
  • Pierre Peyret - , Université Clermont Auvergne (Autor:in)
  • Roland Marmeisse - , University of Turin, Universite Claude Bernard Lyon 1, Sorbonne Université, National Research Council of Italy (CNR) (Autor:in)


Fungal dye-decolorizing peroxidases (DyPs) have found applications in the treatment of dye-contaminated industrial wastes or to improve biomass digestibility. Their roles in fungal biology are uncertain, although it has been repeatedly suggested that they could participate in lignin degradation and/or modification. Using a comprehensive set of 162 fully sequenced fungal species, we defined seven distinct fungal DyP clades on basis of a sequence similarity network. Sequences from one of these clades clearly diverged from all others, having on average the lower isoelectric points and hydropathy indices, the highest number of N-glycosylation sites, and N-terminal sequence peptides for secretion. Putative proteins from this clade are absent from brown-rot and ectomycorrhizal species that have lost the capability of degrading lignin enzymatically. They are almost exclusively present in white-rot and other saprotrophic Basidiomycota that digest lignin enzymatically, thus lending support for a specific role of DyPs from this clade in biochemical lignin modification. Additional nearly full-length fungal DyP genes were isolated from the environment by sequence capture by hybridization; they all belonged to the clade of the presumably secreted DyPs and to another related clade. We suggest focusing our attention on the presumably intracellular DyPs from the other clades, which have not been characterized thus far and could represent enzyme proteins with novel catalytic properties. KEY POINTS: • A fungal DyP phylogeny delineates seven main sequence clades. • Putative extracellular DyPs form a single clade of Basidiomycota sequences. • Extracellular DyPs are associated to white-rot fungi.


Seiten (von - bis)2993-3007
FachzeitschriftApplied Microbiology and Biotechnology
PublikationsstatusVeröffentlicht - 18 Apr. 2022

Externe IDs

PubMed 35435459
unpaywall 10.1007/s00253-022-11923-0
Mendeley 750cee96-6fbf-337c-a48d-64373df79b47


DFG-Fachsystematik nach Fachkollegium


  • DyP-type peroxidase, Fungi, Lignin degradation, Sequence capture, Lignin/metabolism, Peroxidases/genetics, Basidiomycota/metabolism, Coloring Agents/metabolism, Fungal Proteins/metabolism, Peroxidase/chemistry