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 language | English (US) |
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Pages (from-to) | 107-110 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 299 |
Issue number | 1 |
DOIs | |
State | Published - 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