PhanerochaeteV1, Main, Exploration, bibRecord, 000B92

2,4-Dichlorophenol degradation using Streptomyces viridosporus T7A lignin peroxidase.

Identifieur interne : 000B92 ( Main/Exploration ); précédent : 000B91; suivant : 000B93

2,4-Dichlorophenol degradation using Streptomyces viridosporus T7A lignin peroxidase.

Auteurs : D C Yee [États-Unis] ; T K Wood

Source :

Biotechnology progress [ 8756-7938 ]

RBID : pubmed:9041710

Descripteurs français

KwdFr :
- Anions (MeSH), Catalyse (MeSH), Chlorophénols (métabolisme), Chlorures (métabolisme), Chromatographie en phase gazeuse (MeSH), Cinétique (MeSH), Dépollution biologique de l'environnement (MeSH), Oxydoréduction (MeSH), Peroxidases (métabolisme), Spectrométrie de masse (MeSH), Streptomyces (enzymologie).
MESH :
- enzymologie : Streptomyces.
- métabolisme : Chlorophénols, Chlorures, Peroxidases.
- Anions, Catalyse, Chromatographie en phase gazeuse, Cinétique, Dépollution biologique de l'environnement, Oxydoréduction, Spectrométrie de masse.

English descriptors

KwdEn :
- Anions (MeSH), Biodegradation, Environmental (MeSH), Catalysis (MeSH), Chlorides (metabolism), Chlorophenols (metabolism), Chromatography, Gas (MeSH), Kinetics (MeSH), Mass Spectrometry (MeSH), Oxidation-Reduction (MeSH), Peroxidases (metabolism), Streptomyces (enzymology).
MESH :
- chemical , metabolism : Chlorides, Chlorophenols, Peroxidases.
- chemical : Anions.
- enzymology : Streptomyces.
- Biodegradation, Environmental, Catalysis, Chromatography, Gas, Kinetics, Mass Spectrometry, Oxidation-Reduction.

Abstract

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.

DOI: 10.1021/bp960091x
PubMed: 9041710

Affiliations:

États-Unis

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Le document en format XML

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<affiliation wicri:level="1"><nlm:affiliation>Department of Chemical and Biochemical Engineering, University of California, Irvine 92697-2575, USA.</nlm:affiliation>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anions (MeSH)</term>
<term>Biodegradation, Environmental (MeSH)</term>
<term>Catalysis (MeSH)</term>
<term>Chlorides (metabolism)</term>
<term>Chlorophenols (metabolism)</term>
<term>Chromatography, Gas (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Mass Spectrometry (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peroxidases (metabolism)</term>
<term>Streptomyces (enzymology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Anions (MeSH)</term>
<term>Catalyse (MeSH)</term>
<term>Chlorophénols (métabolisme)</term>
<term>Chlorures (métabolisme)</term>
<term>Chromatographie en phase gazeuse (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Dépollution biologique de l'environnement (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Peroxidases (métabolisme)</term>
<term>Spectrométrie de masse (MeSH)</term>
<term>Streptomyces (enzymologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Chlorides</term>
<term>Chlorophenols</term>
<term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Anions</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Streptomyces</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Streptomyces</term>
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<term>Chlorures</term>
<term>Peroxidases</term>
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<keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term>
<term>Catalysis</term>
<term>Chromatography, Gas</term>
<term>Kinetics</term>
<term>Mass Spectrometry</term>
<term>Oxidation-Reduction</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Anions</term>
<term>Catalyse</term>
<term>Chromatographie en phase gazeuse</term>
<term>Cinétique</term>
<term>Dépollution biologique de l'environnement</term>
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<front><div type="abstract" xml:lang="en">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.</div>
</front>
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<Month>03</Month>
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<DateRevised><Year>2012</Year>
<Month>11</Month>
<Day>15</Day>
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<Title>Biotechnology progress</Title>
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<Abstract><AbstractText>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.</AbstractText>
</Abstract>
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2,4-Dichlorophenol degradation using Streptomyces viridosporus T7A lignin peroxidase.

2,4-Dichlorophenol degradation using Streptomyces viridosporus T7A lignin peroxidase.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki