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Oxidation of Chlorophenols Catalyzed by Coprinus cinereus Peroxidase with in Situ Production of Hydrogen Peroxide
Author(s) -
Pezzotti Fabio,
Okrasa Krzysztof,
Therisod Michel
Publication year - 2004
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp049750t
Subject(s) - hydrogen peroxide , peroxidase , chemistry , catalysis , substrate (aquarium) , reagent , peroxide , horseradish peroxidase , degradation (telecommunications) , enzyme , in situ , biochemistry , organic chemistry , biology , ecology , telecommunications , computer science
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, peroxidaseapos;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.