Oxidation of chlorophenols catalyzed by Coprinus cinereus peroxidase with in situ production of hydrogen peroxide.
Degradation of 2,6-dichlorophenol (2,6-DCP) was accomplished by oxidation catalyzed by Coprinus cinereus peroxidase. Immobilization of the enzyme in a polyacrylamide matrix enhanced DCP oxidation. Hydrogen peroxide, peroxidase's natural substrate, was produced enzymatically in situ to avoid peroxidase inactivation by its too high concentration. In the case of larger scale utilization, the method would also avoid direct handling of this hazardous reagent.
Pezzotti
Fabio
F
LCBB, ICMMO, Université Paris-Sud, bat. 420, 91405 Orsay, France.
Okrasa
Krzysztof
K
Therisod
Michel
M
D002384:Catalysis; D002733:Chlorophenols / Q000737:chemistry*; D003302:Coprinus / Q000201:enzymology*; D004800:Enzymes, Immobilized / Q000737:chemistry; D006801:Humans; D006861:Hydrogen Peroxide / Q000138:chemical synthesis*; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000737:chemistry*
D002733:Chlorophenols; D004800:Enzymes, Immobilized; D006861:Hydrogen Peroxide; D009195:Peroxidase; C032729:2,6-dichlorophenol