Stimulation of Wood Degradation by Daedaleopsis confragosa and D. tricolor


Biological pretreatment of the lignocellulosic residues, in which white-rot fungi have a crucial role, has many advantages compared to the chemical, physical, and physico-chemical methods of delignification and therefore attracts increasing scientific attention. Regarding the fact that properties and capacities of the ligninolytic enzymes of Daedaleopsis spp. are still unknown, the aim of this study was to research how nitrogen sources and inducers affect the potential of Daedaleopsis confragosa and Daedaleopsis tricolor to degrade cherry sawdust. NH4NO3, (NH4)2SO4, and peptone were tested as nitrogen sources, while veratryl alcohol, p-anisidine, vanillic acid, and phenylmethylsulfonyl fluoride were the studied inducers. As Mn-dependent peroxidase and laccase were the leader enzymes and cherry sawdust/peptone medium the best stimulator of their activities, the effect of inducers on delignification potential of these species was studied during fermentation of that substrate. Veratryl alcohol was the best stimulator of laccase and phenylmethylsulfonyl fluoride of Mn-dependent peroxidase activity (27,610.0 and 1338.4 U/L, respectively). These inducers also increased cherry sawdust delignification selectivity, particularly in D. tricolor in the presence of phenylmethylsulfonyl fluoride (lignin:hemicellulose:cellulose = 32.1%:0.9%:11.7%). Owing to the presented results, studied species could have an important role in the phase of lignocellulose pretreatment in various biotechnological processes.

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This study was carried out under Project No. 173032, which is financially supported by the Ministry of Education, Science and Technological Development of Republic of Serbia.

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Correspondence to Jasmina Ćilerdžić.

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Ćilerdžić, J., Galić, M., Ivanović, Ž. et al. Stimulation of Wood Degradation by Daedaleopsis confragosa and D. tricolor. Appl Biochem Biotechnol 187, 1371–1383 (2019).

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  • Cherry sawdust
  • Daedaleopsis spp.
  • Delignification
  • Laccases
  • Mn-oxidizing peroxidases