2,4-Dichlorophenol degradation using Streptomyces viridosporus T7A lignin peroxidase.
The Streptomyces viridosporus T7A bacterium produces the extracellular lignin peroxidase ALiP-P3. The ALiP-P3-catalyzed oxidation of 2,4-dichlorophenol (DCP) was examined to understand its kinetic behavior. Initial rate data of the oxidation of DCP were obtained by a spectrophotometric peroxidase assay, and the kinetics were best modeled with a random-binding bireactant system, which differs from the ping-pong bireactant system that is typically used for horseradish peroxidase and lignin peroxidase from the fungus Phanerochaete chrysosporium, and suggests that either DCP or H2O2 may bind first to ALiP-P3. Chloride ion measurements indicate that 16% of the reacted DCP was fully dechlorinated by ALiP-P3. Chemical ionization mass spectrometry was also utilized to identify the DCP degradation product as a hydrophobic chlorinated dimer of mass 322.
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Department of Chemical and Biochemical Engineering, University of California, Irvine 92697-2575, USA.
Wood
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D000838:Anions; D001673:Biodegradation, Environmental; D002384:Catalysis; D002712:Chlorides / Q000378:metabolism; D002733:Chlorophenols / Q000378:metabolism*; D002849:Chromatography, Gas; D007700:Kinetics; D013058:Mass Spectrometry; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology*
D000838:Anions; D002712:Chlorides; D002733:Chlorophenols; D010544:Peroxidases; C042858:lignin peroxidase; C004762:2,4-dichlorophenol