Chloroperoxidase mediated oxidation of chlorinated phenols using electrogenerated hydrogen peroxide
Electron. j. biotechnol
;
10(1): 24-36, Jan. 2007. ilus, tab, graf
Article
in English
| LILACS
| ID: lil-460040
ABSTRACT
Chloroperoxidase (CPO) from Caldariomyces fumago catalyses the oxidation of several chlorinated phenols (CP) commonly found in industrial waste waters in the presence of hydrogen peroxide. This study compares the direct addition of hydrogen peroxide (DA) with its continuous electrogeneration (EG) during the enzymatic oxidation of CP. Reaction mixtures were studied containing chemically modified CPO, hydrogen peroxide and the phenolic substrates: phenol (P), 4-chlorophenol (4-CP), 2,4-dichlorophenol (2,4-DCP), 2,4,6-trichlorophenol (2,4,6-TCP) and pentachlorophenol (PCP), in 100 mM sodium-potassium phosphate buffer pH 6.0, at 25ºC. Results were compared in terms of residual phenol concentration (oxidation efficiency), precipitate formation (removal) and residual enzyme activity (stability). With the electrochemical system evaluated at -620 mVSCE, and continuous aeration the maximum H2O2 concentration of 1.2 mM was obtained. Under this conditions and after 4 hrs using EG, no phenol or 4-CP were detected, and 97 percent, 93 percent and 88 percent of 2,4-DCP, 2,4,6-TCP and PCP were degraded, respectively. The use of EG improves enzyme half-life time in comparison to the results obtained by DA.
Full text:
Available
Index:
LILACS (Americas)
Language:
English
Journal:
Electron. j. biotechnol
Journal subject:
Biotechnology
Year:
2007
Type:
Article
Affiliation country:
Brazil
Institution/Affiliation country:
Federal University of Rio de Janeiro/BR
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