Degradation of Diuron byPhanerochaete chrysosporium: Role of Ligninolytic Enzymes and Cytochrome P450

Abstract

The white-rot fungusPhanerochaete chrysosporiumwas investigated for its capacity to degrade the herbicide diuron in liquid stationary cultures. The presence of diuron increased the production of lignin peroxidase in relation to control cultures but only barely affected the production of manganese peroxidase. The herbicide at the concentration of 7 μg/mL did not cause any reduction in the biomass production and it was almost completely removed after 10 days. Concomitantly with the removal of diuron, two metabolites, DCPMU [1-(3,4-dichlorophenyl)-3-methylurea] and DCPU [(3,4-dichlorophenyl)urea], were detected in the culture medium at the concentrations of 0.74 μg/mL and 0.06 μg/mL, respectively. Crude extracellular ligninolytic enzymes were not efficient in thein vitrodegradation of diuron. In addition, 1-aminobenzotriazole (ABT), a cytochrome P450 inhibitor, significantly inhibited both diuron degradation and metabolites production. Significant reduction in the toxicity evaluated by theLactuca sativaL. bioassay was observed in the cultures after 10 days of cultivation. In conclusion,P. chrysosporiumcan efficiently metabolize diuron without the accumulation of toxic products.