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2,4‐Dichlorophenol Degradation Using Streptomyces viridosporus T7A Lignin Peroxidase
Author(s) -
Yee Dennis C.,
Wood Thomas K.
Publication year - 1997
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/bp960091x
Subject(s) - phanerochaete , peroxidase , chemistry , lignin peroxidase , lignin , horseradish peroxidase , 2,4 dichlorophenol , chrysosporium , chromatography , degradation (telecommunications) , nuclear chemistry , biochemistry , enzyme , organic chemistry , bacteria , biology , telecommunications , computer science , genetics
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 H 2 O 2 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.