Oxidation of Chlorophenols Catalyzed by Coprinus cinereus Peroxidase with in Situ Production of Hydrogen Peroxide

Autor:	Fabio Pezzotti, Michel Therisod, Krzysztof Okrasa
Rok vydání:	2004
Předmět:	chemistry.chemical_classification biology Polyacrylamide Substrate (chemistry) Hydrogen Peroxide Enzymes Immobilized Catalysis Coprinus chemistry.chemical_compound Enzyme chemistry Reagent biology.protein Humans Organic chemistry Phenols Hydrogen peroxide Oxidation-Reduction Chlorophenols Peroxidase Biotechnology
Zdroj:	Biotechnology Progress. 20:1868-1871
ISSN:	8756-7938
DOI:	10.1021/bp049750t
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::161d1e91725f829a34412ceb6d78dac9 https://doi.org/10.1021/bp049750t Zobrazit plný text záznamu Plný text