Abstract

Fungal secretory peroxidases mediate fundamental ecological functions in the conversion and degradation of plant biomass. Many of these enzymes have strong oxidizing activities towards aromatic compounds and are involved in the degradation of plant cell wall (lignin) and humus. They comprise three major groups: class II peroxidases (including lignin peroxidase, manganese peroxidase, versatile peroxidase and generic peroxidase), dye-decolorizing peroxidases, and heme-thiolate peroxidases (e.g. unspecific/aromatic peroxygenase, chloroperoxidase). Here, we have repeatedly observed a widespread expression of all major peroxidase groups in leaf and needle litter across a range of forest ecosystems (e.g. Fagus, Picea, Acer, Quercus, and Populus spp.), which are widespread in Europe and North America. Manganese peroxidases and unspecific peroxygenases were found expressed in all nine investigated forest sites, and dye-decolorizing peroxidases were observed in five of the nine sites, thereby indicating biological significance of these enzymes for fungal physiology and ecosystem processes. Transcripts of selected secretory peroxidase genes were also analyzed in pure cultures of several litter-decomposing species and other fungi. Using this information, we were able to match, in environmental litter samples, two manganese peroxidase sequences to Mycena galopus and Mycena epipterygia and one unspecific peroxygenase transcript to Mycena galopus, suggesting an important role of this litter- and coarse woody debris-dwelling genus in the disintegration and transformation of litter aromatics and organic matter formation.

Highlights

  • Wood and plant litter are the ubiquitous results of terrestrial plant life

  • Lignocellulosic biomass is dominant in forest ecosystems and is composed of polysaccharides as well as of the aromatic heteropolymer lignin derived from woody plants [1]

  • Fungal secretory peroxidases are known to be of significance during litter decay, inasmuch as they initiate the decomposition of lignin and transformation of resulting aromatics, which, in turn, foster humus formation (Fig. 1; [3], [4], [8], [30])

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Summary

Introduction

Wood and plant litter are the ubiquitous results of terrestrial plant life. Lignocellulosic biomass is dominant in forest ecosystems and is composed of polysaccharides (cellulose and hemicelluloses) as well as of the aromatic heteropolymer lignin derived from woody plants [1]. In particular saprotrophic members of the phylum Basidiomycota, have evolved extracellular oxidative enzymes to oxidize lignin and convert its aromatic constituents [3]. The hemecontaining peroxidases of the class II peroxidase group are considered truly lignin-modifying enzymes, which are able to oxidize high-redox potential aromatic substrates [4]. Members of this family of fungal secretory peroxidases, namely lignin peroxidase (LiP, EC 1.11.1.14), manganese peroxidase (MnP, EC 1.11.1.13) and versatile peroxidase (VP, EC 1.11.1.16), are the primary agents of enzymatic lignin decomposition [3,4,5,6]. The aforementioned enzymes have been identified and characterized, we do not understand the extent to which they are deployed by saprotrophic fungi residing in forest soils, or their explicit biological function in the detritus decay process

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