Plant peroxidases (EC 1.11.1.7) catalyze the oxidation of phenolic pollutants in the presence of hydrogen peroxide. In the present study, extracellular peroxidases from Vaccinium myrtillus cell suspension cultures (VMP) were evaluated for their ability to polymerize 2,4,6-trichlorophenol (TCP), a ubiquitous environmental contaminant. The effect of pH, temperature, reaction time, enzyme amount and initial pollutant concentration on the treatment efficiency was investigated in order to optimize the reaction conditions for TCP removal. An appreciable removal efficiency and a partial dehalogenation of TCP was observed over a wide range of initial pollutant concentrations (0.1-20mmol dm(-3)) and reaction conditions suggesting that VMP could be useful for potential decontamination applications. The use of polyethylene glycol in the reaction mixture allowed a reduction of the catalyst requirements needed to obtain well defined extents of TCP removal.