Comparative Analysis of Enzyme Production Patterns of Lignocellulose Degradation of Two White Rot Fungi: Obba rivulosa and Gelatoporia subvermispora

Biomolecules. 2022 Jul 22;12(8):1017. doi: 10.3390/biom12081017.

Abstract

The unique ability of basidiomycete white rot fungi to degrade all components of plant cell walls makes them indispensable organisms in the global carbon cycle. In this study, we analyzed the proteomes of two closely related white rot fungi, Obba rivulosa and Gelatoporia subvermispora, during eight-week cultivation on solid spruce wood. Plant cell wall degrading carbohydrate-active enzymes (CAZymes) represented approximately 5% of the total proteins in both species. A core set of orthologous plant cell wall degrading CAZymes was shared between these species on spruce suggesting a conserved plant biomass degradation approach in this clade of basidiomycete fungi. However, differences in time-dependent production of plant cell wall degrading enzymes may be due to differences among initial growth rates of these species on solid spruce wood. The obtained results provide insight into specific enzymes and enzyme sets that are produced during the degradation of solid spruce wood in these fungi. These findings expand the knowledge on enzyme production in nature-mimicking conditions and may contribute to the exploitation of white rot fungi and their enzymes for biotechnological applications.

Keywords: CAZymes; Gelatoporia subvermispora; LC-MS/MS; Obba rivulosa; lignin biodegradation; proteome; white rot fungi.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Basidiomycota*
  • Fungi / metabolism
  • Lignin* / metabolism
  • Polyporales

Substances

  • lignocellulose
  • Lignin

Supplementary concepts

  • Gelatoporia subvermispora
  • Obba rivulosa

Grants and funding

M.M. was supported by the European Commission, Marie Curie ITN network SuBiCat FP7 Grant agreement no: 607044 and the Academy of Finland research grant no: 297847. The Academy of Finland grant no: 308284 to MRM is acknowledged. M.V.A.P. was supported by a grant of the Dutch Technology Foundation STW, Applied Science division of NWO; and the Technology Program of the Dutch Ministry of Economic Affairs 016.130.609 to RPdV. Mass spectrometry analysis was performed at the Centre for Biological Applications of Mass Spectrometry (CBAMS) at Concordia University, Montreal, Canada.