Oxidative polymerization and partial dechlorination of 2,4,6-trichlorophenol by a mixture of peroxidase isozymes from Vaccinium myrtillus

Plant peroxidases (EC 1.11.1.7) catalyze the oxidation of phenolic pollutan ts in the presence of hydrogen peroxide. In the present study, extracellula r peroxidases from Vaccinium myrtillus cell suspension cultures (VMP) were evaluated for their ability to polymerize 2,4,6-trichlorophenol (TCP), a ub iquitous environmental contaminant. The effect of pH, temperature, reaction time, enzyme amount and initial pollutant concentration on the treatment e fficiency was investigated in order to optimize the reaction conditions for TCP removal. An appreciable removal efficiency and a partial dehalogenatio n 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 u seful for potential decontamination applications. The use of polyethylene g lycol in the reaction mixture allowed a reduction of the catalyst requireme nts needed to obtain well defined extents of TCP removal. (C) 2001 Society of Chemical Industry.