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

FEBS Letters

Field, Jim A.¹  de Bont, Jan A.M.¹  de Jong, Ed¹ 

[1] Division of Industrial Microbiology, Department of Food Science, Agricultural University Wageningen, PO Box 8129, 6700 EV Wageningen, The Netherlands

关键词: Ligninase;    Manganese peroxidase;    White-rot fungus;    Lignin degradation;    Manganese-inhibited peroxidase;    Bjerkandera;    DMP;    2;    6-dimethoxyphenol;    ABTS;    2;    2′-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt;    DTT;    dithiothreitol;    LiP;    ligninase (i.e. lignin peroxidase);    MnP;    manganese peroxidase;    HRP;    horseradish peroxidase;    MIP;    manganese-inhibited peroxidase;   

DOI  :  10.1016/0014-5793(92)80111-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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’.

【 授权许可】

Unknown