The existing method of determining the activity of manganese peroxidase (Mn
P), produced by Phanerochaete chrysosporium, was improved. 2,6-Dimethoxyphe
nol at 80 mM was used as a substrate and, after the decolorization of the r
eaction mixture, H2O2 was added and the initial reaction rate was used to d
etermine MnP activity.