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Evidence for a new extracellular peroxidase Manganese‐inhibited peroxidase from the white‐rot fungus Bjerkandera sp. BOS 55
Author(s) -
de Jong Ed,
Field Jim A.,
de Bont Jan A.M.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80111-s
Subject(s) - guaiacol , peroxidase , chemistry , manganese peroxidase , manganese , substrate (aquarium) , enzyme , abts , enzyme assay , phenol , extracellular , biochemistry , organic chemistry , biology , antioxidant , ecology , dpph
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 H 2 O 2 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 H 2 O 2 . With some substrates, a strong inhibition of the peroxidative activity by Mn 2+ 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 Mn 2+ , this substrate should not be used in assays to detect manganese peroxidase. The enzyme is tentatively named ‘Manganese‐Inhibited Peroxidase’.