title: Oxidation of chlorophenols catalyzed by Coprinus cinereus peroxidase with in situ production of hydrogen peroxide.
abstract: 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.
authors.affiliation: LCBB, ICMMO, Université Paris-Sud, bat. 420, 91405 Orsay, France.
authors.forename: Fabio
authors.initials: F
authors.lastname: Pezzotti
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Okrasa
authors.forename: Michel
authors.initials: M
authors.lastname: Therisod
mesh_terms: 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*
chemical_list: D002733:Chlorophenols; D004800:Enzymes, Immobilized; D006861:Hydrogen Peroxide; D009195:Peroxidase; C032729:2,6-dichlorophenol