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During solid-state fermentation of wheat straw, a natural lignocellulosic substrate, the white rot fungus Pleurotus ostreatus produced an extracellular H2O2-requiring Remazol brilliant blue R (RBBR)-decolorizing enzymatic activity along with manganese peroxidase, manganese-independent peroxidase, and phenol oxidase activities. The presence of RBBR was not essential for the production of RBBR-decolorizing enzymatic activity by P. ostreatus, because this activity was also produced in the absence of RBBR. This RBBR-decolorizing enzymatic activity in crude enzyme preparations of 14- and 20-day-old cultures exhibited an apparent Km for RBBR of 31 and 52 microM, respectively. The RBBR-decolorizing enzyme activity was maximal in the pH range 3.5 to 4.0. This activity was independent of manganese, and veratryl alcohol had no influence on it. Manganese peroxidase of P. ostreatus did not decolorize RBBR. This H2O2-dependent RBBR-decolorizing enzymatic activity behaved like an oxygenase possessing a catalytic metal center, perhaps heme, because it was inhibited by Na2S2O5, NaCN, NaN3, and depletion of dissolved oxygen. Na2S2O5 brought an early end to the reaction without interfering with the initial reaction rate of RBBR oxygenase. The activity was also inhibited by cysteine. Concentrations of H2O2 higher than 154 microM were observed to be inhibitory as well. Decolorization of RBBR by P. ostreatus is an oxidative process.

applied and environmental microbiology

Involvement of an extracellular H2O2-dependent ligninolytic activity of the white rot fungus Pleurotus ostreatus in the decolorization of Remazol brilliant blue R