White-rot basidiomycetes Junghuhnia nitida and Steccherinum bourdotii: Oxidative potential and laccase properties in comparison with Trametes hirsuta and Coriolopsis caperata

PLoS One. 2018 Jun 1;13(6):e0197667. doi: 10.1371/journal.pone.0197667. eCollection 2018.

Abstract

White-rot basidiomycetes from the poorly studied residual polyporoid clade of Polyporales order Junghuhnia nitida (Pers.) Ryvarden and Steccherinum bourdotii Saliba & A. David grow as secondary xylotrohps on well decomposed woody materials. The main objective of the current study was to compare oxidative potential, growth, production of oxidative enzymes and laccase properties of J. nitida and S. bourdotii with that of typical primary xylotrohps Trametes hirsuta (Wulfen) Lloyd and Coriolopsis caperata (Berk.) Murrill, belonging to the core polyporoid clade. For the first time we report species J. nitida and S. bourdotii as active laccase producers. New laccases from J. nitida and S. bourdotii were purified and characterized. They had an identical molecular weight of 63 kDa and isoelectric points of 3.4 and 3.1, respectively. However, the redox potential of the T1 copper site for both J. nitida (610 mV) and S. bourdotii (640 mV) laccases was lower than those for T. hirsuta and C. caperata laccases. The new laccases showed higher temperature optima and better thermal stability than T. hirsuta and C. caperata laccases. Their half-lives were more than 40 min at 70 °C. The laccases from J. nitida and S. bourdotii showed higher affinity to syringyl-type phenolic compounds than T. hirsuta and C. caperata laccases. The oxidative potential of studied fungi as well as the properties of their laccases are discussed in terms of the fungal life-style.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Basidiomycota / enzymology*
  • Coriolaceae / enzymology
  • Enzyme Stability
  • Laccase / chemistry*
  • Laccase / genetics
  • Laccase / metabolism
  • Oxidation-Reduction
  • Oxidative Stress / genetics*
  • Polyporales / enzymology
  • Temperature
  • Trametes / enzymology

Substances

  • Laccase

Grants and funding

This work was supported by the Russian Foundation for Basic Research (http://www.rfbr.ru/rffi/ru/), grant no 16-04-01184 to TVF. The funder had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.