Enzymatic oxidation of aqueous pentachlorophenol.
The influence of the nonionic surfactant Tween 80 on pentachlorophenol (PCP) oxidation catalyzed by horseradish peroxidase was studied. The surfactant was tested at concentrations below and above its critical micelle concentration (CMC). Enhancement of PCP removal was observed at sub-CMCs. The presence of Tween 80 in the reaction mixture reduced enzyme inactivation which occurred through a combination of free radical attack and sorption by precipitated products. A simple first-order model was able to simulate time profiles for enzyme inactivation in the presence or absence of Tween 80. At supra-CMCs, the surfactant caused noticeable reductions in PCP removal, presumably through micelle partitioning of PCP which precluded the hydrophobic PCP molecule from interacting with the enzyme.
Kim
E Y
EY
Department of Chemical Engineering, The University of Seoul, Seoul 130-743, Korea. eykim@uos.ac.kr
Chae
H J
HJ
Chu
K H
KH
D006735:Horseradish Peroxidase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D010416:Pentachlorophenol / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature; D014874:Water Pollutants, Chemical / Q000378:metabolism*
D014874:Water Pollutants, Chemical; D010416:Pentachlorophenol; D006735:Horseradish Peroxidase