Chloroperoxidase mediated oxidation of chlorinated phenols using electrogenerated hydrogen peroxide

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) du...

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Auteurs principaux:	La Rotta,Camilo E, D'Elia,Eliane, Bon,Elba P.S
Langue:	English
Publié:	Pontificia Universidad Católica de Valparaíso 2007
Sujets:	biodegradation bioelectrochemistry Caldariomyces fumago chlorinated phenols chloroperoxidase hydrogen peroxide electrogeneration
Accès en ligne:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582007000100003
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spelling	oai:scielo:S0717-345820070001000032007-08-14Chloroperoxidase mediated oxidation of chlorinated phenols using electrogenerated hydrogen peroxideLa Rotta,Camilo ED'Elia,ElianeBon,Elba P.S biodegradation bioelectrochemistry Caldariomyces fumago chlorinated phenols chloroperoxidase hydrogen peroxide electrogeneration 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 mV SCE, 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%, 93% and 88% 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 DAinfo:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.10 n.1 20072007-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582007000100003en10.4067/S0717-34582007000100003
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	biodegradation bioelectrochemistry Caldariomyces fumago chlorinated phenols chloroperoxidase hydrogen peroxide electrogeneration
spellingShingle	biodegradation bioelectrochemistry Caldariomyces fumago chlorinated phenols chloroperoxidase hydrogen peroxide electrogeneration La Rotta,Camilo E D'Elia,Eliane Bon,Elba P.S Chloroperoxidase mediated oxidation of chlorinated phenols using electrogenerated hydrogen peroxide
description	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 mV SCE, 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%, 93% and 88% 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
author	La Rotta,Camilo E D'Elia,Eliane Bon,Elba P.S
author_facet	La Rotta,Camilo E D'Elia,Eliane Bon,Elba P.S
author_sort	La Rotta,Camilo E
title	Chloroperoxidase mediated oxidation of chlorinated phenols using electrogenerated hydrogen peroxide
title_short	Chloroperoxidase mediated oxidation of chlorinated phenols using electrogenerated hydrogen peroxide
title_full	Chloroperoxidase mediated oxidation of chlorinated phenols using electrogenerated hydrogen peroxide
title_fullStr	Chloroperoxidase mediated oxidation of chlorinated phenols using electrogenerated hydrogen peroxide
title_full_unstemmed	Chloroperoxidase mediated oxidation of chlorinated phenols using electrogenerated hydrogen peroxide
title_sort	chloroperoxidase mediated oxidation of chlorinated phenols using electrogenerated hydrogen peroxide
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2007
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582007000100003
work_keys_str_mv	AT larottacamiloe chloroperoxidasemediatedoxidationofchlorinatedphenolsusingelectrogeneratedhydrogenperoxide AT deliaeliane chloroperoxidasemediatedoxidationofchlorinatedphenolsusingelectrogeneratedhydrogenperoxide AT bonelbaps chloroperoxidasemediatedoxidationofchlorinatedphenolsusingelectrogeneratedhydrogenperoxide
_version_	1718441761201717248

Chloroperoxidase mediated oxidation of chlorinated phenols using electrogenerated hydrogen peroxide

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