[Peroxidase oxidation of phenols].
Partially purified preparations of horseradish peroxidase were able to catalyze the effective transformation of such phenol compounds as phenol, o-chlorophenol, 2,4,6-trichlorophenol, pentachlorophenol (giving rise to the formation of polymer products insoluble in water), resorcinol, and thymol (giving rise to the formation of low-molecular-weight products). The following conditions were found to be optimal for peroxidase oxidation and provide the maximum extent of elimination of phenol compounds: temperature, 15-25 and 25-30 degrees C for phenol and chlorophenol compounds, respectively; molar ratio H2O2/phenol, 1:1; and transformation time, 1-3 h. Although effective transformation was observed within a broad range of pH, the efficiency of the process slightly increased at a pH from 6.0 to 7.5. It was suggested to carry out multiple peroxidase oxidations of phenols using partially purified peroxidase enclosed in a dialysis membrane bag placed into a solution of a phenol compound containing hydrogen peroxide.
Davidenko
T I
TI
D002384:Catalysis; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000378:metabolism*; D010636:Phenols / Q000378:metabolism*
D010636:Phenols; D009195:Peroxidase