Reevaluation of the manganese requirement for the biobleaching of kraft pulp by white rot fungi

M. T. Moreira, G. Feijoo, R. Sierra-Alvarez, J. A. Field

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


Manganese dependent peroxidase (MnP) is the main enzyme implicated in the biobleaching of kraft pulps by white rot fungi. The goal of this study was to evaluate the Mn requirement for biobleaching of eucalyptus oxygen delignified kraft pulp (OKP) by various white rot fungi: Trametes versicolor, Phanerochaete sordida, Phlebia radiata, Stereum hirsutum and Bjerkandera sp. strain BOS55. All of the strains tested produced MnP and provided extensive bleaching of OKP when 33 μM Mn was included in the medium. Bjerkandera sp. strain BOS55 was the only strain that also displayed MnP production and biobleaching activity of EDTA-extracted OKP in the complete absence of Mn. However, MnP and biobleaching activity in the absence of Mn was dependent on the presence of organic acids in the medium. The fact the biobleaching was correlated to MnP activity irrespective of whether Mn was present or absent suggests that there may be roles for MnP in Bjerkandera under Mn-deficient conditions. Although manganese-independent peroxidase (MIP) and lignin peroxidase (LiP) were also detected, the titres were much smaller in comparison with those of MnP, so their relative role in biobleaching can be predicted to have a minor importance in comparison with MnP. Only in the case of Bjerkandera, was the expression of LiP stimulated in the presence of oxalate but final brightness was not substantially affected.

Original languageEnglish (US)
Pages (from-to)255-260
Number of pages6
JournalBioresource Technology
Issue number3
StatePublished - Dec 1999


  • Biobleaching
  • Delignification
  • Mn-deficient conditions
  • Organic acids
  • White rot fungi

ASJC Scopus subject areas

  • Bioengineering
  • Environmental Engineering
  • Renewable Energy, Sustainability and the Environment
  • Waste Management and Disposal


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