Evidence for a new extracellular peroxidase Manganese-inhibited peroxidase from the white-rot fungus Bjerkandera sp. BOS 55

Ed de Jong, Jim A. Field, Jan A.M. de Bont

Research output: Contribution to journalArticle

57 Scopus citations

Abstract

A novel enzyme activity was detected in the extracellular fluid of Bjerkandera sp, BOS 55. The purified enzyme could oxidize several compounds, such as Phenol red, 2,6-dimethoxyphenol (DMP), Poly R-478, ABTS and guaiacol, with H2O2 as an electron acceptor. In contrast, veratryl alcohol was not a substrate. This enzyme also had the capacity to oxidize DMP in the absence of H2O2. With some substrates, a strong inhibition of the peroxidative activity by Mn2+ was observed. Phenol red oxidation was inhibited by 84% with only 1 mM of this metal ion. Because DMP oxidation by this enzyme is only slightly inhibited by Mn2+, this substrate should not be used in assays to detect manganese peroxidase. The enzyme is tentatively named 'Manganese-Inhibited Peroxidase'.

Original languageEnglish (US)
Pages (from-to)107-110
Number of pages4
JournalFEBS Letters
Volume299
Issue number1
DOIs
StatePublished - Mar 2 1992

Keywords

  • Bjerkandera
  • Lignin degradation
  • Ligninase
  • Manganese peroxidase
  • Manganese-inhibited peroxidase
  • White-rot fungus

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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