In vitro degradation of a polymeric dye (Poly R-478) by manganese peroxidase.
Identifieur interne : 000A31 ( Main/Curation ); précédent : 000A30; suivant : 000A32In vitro degradation of a polymeric dye (Poly R-478) by manganese peroxidase.
Auteurs : M T Moreira [Espagne] ; C. Palma ; I. Mielgo ; G. Feijoo ; J M LemaSource :
- Biotechnology and bioengineering [ 0006-3592 ] ; 2001.
Descripteurs français
- KwdFr :
- Agents colorants (composition chimique), Agents colorants (métabolisme), Anthraquinones (composition chimique), Anthraquinones (métabolisme), Chromatographie sur gel (MeSH), Couleur (MeSH), Hydrolyse (MeSH), Manganèse (métabolisme), Masse moléculaire (MeSH), Peroxidases (isolement et purification), Peroxidases (métabolisme), Peroxyde d'hydrogène (métabolisme), Phanerochaete (enzymologie), Phanerochaete (métabolisme), Polymères (composition chimique), Polymères (métabolisme).
- MESH :
- composition chimique : Agents colorants, Anthraquinones, Polymères.
- enzymologie : Phanerochaete.
- isolement et purification : Peroxidases.
- métabolisme : Agents colorants, Anthraquinones, Manganèse, Peroxidases, Peroxyde d'hydrogène, Phanerochaete, Polymères.
- Chromatographie sur gel, Couleur, Hydrolyse, Masse moléculaire.
English descriptors
- KwdEn :
- Anthraquinones (chemistry), Anthraquinones (metabolism), Chromatography, Gel (MeSH), Color (MeSH), Coloring Agents (chemistry), Coloring Agents (metabolism), Hydrogen Peroxide (metabolism), Hydrolysis (MeSH), Manganese (metabolism), Molecular Weight (MeSH), Peroxidases (isolation & purification), Peroxidases (metabolism), Phanerochaete (enzymology), Phanerochaete (metabolism), Polymers (chemistry), Polymers (metabolism).
- MESH :
- chemical , chemistry : Anthraquinones, Coloring Agents, Polymers.
- chemical , isolation & purification : Peroxidases.
- chemical , metabolism : Anthraquinones, Coloring Agents, Hydrogen Peroxide, Manganese, Peroxidases, Polymers.
- enzymology : Phanerochaete.
- metabolism : Phanerochaete.
- Chromatography, Gel, Color, Hydrolysis, Molecular Weight.
Abstract
The aim of this study is the evaluation of the enzymatic action of the ligninolytic enzyme manganese peroxidase (MnP), through a suitable addition of H(2)O(2), as a feasible system for the in vitro degradation of complex structures. For this purpose, a highly recalcitrant polymeric dye (Poly R-478) was selected as a model compound. An amperometric technique was used to determine the H(2)O(2) requirement in the decolorization by nonpurified MnP. Two H(2)O(2) supply strategies-fed-batch (every hour) or semicontinuous (every 5 min)-were applied. The addition of H(2)O(2) in pulses led to a limited decolorization after the pulses and the instantaneous consumption or decomposition of H(2)O(2). Therefore, this way of addition may limit the actual H(2)O(2) concentration in the reaction mixture. In contrast, the semicontinuous strategy maintained lower and prolonged concentrations of H(2)O(2), which allowed a clearly greater decolorization (48% after 2 h). In addition, the effect of Mn(+2) concentration on the decolorization efficiency was investigated to establish the optimal application of the MnP-oxidative system. The enzymatic treatment provoked not only the destruction of the chromophoric groups but also a noticeable breakdown of the chemical structure of the dye. In experiments with pure enzyme, MnP proved to be the main factor responsible for the dye decolorization.
DOI: 10.1002/bit.10052
PubMed: 11590609
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Mielgo</name></author><author><name sortKey="Feijoo, G" sort="Feijoo, G" uniqKey="Feijoo G" first="G" last="Feijoo">G. 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For this purpose, a highly recalcitrant polymeric dye (Poly R-478) was selected as a model compound. An amperometric technique was used to determine the H(2)O(2) requirement in the decolorization by nonpurified MnP. Two H(2)O(2) supply strategies-fed-batch (every hour) or semicontinuous (every 5 min)-were applied. The addition of H(2)O(2) in pulses led to a limited decolorization after the pulses and the instantaneous consumption or decomposition of H(2)O(2). Therefore, this way of addition may limit the actual H(2)O(2) concentration in the reaction mixture. In contrast, the semicontinuous strategy maintained lower and prolonged concentrations of H(2)O(2), which allowed a clearly greater decolorization (48% after 2 h). In addition, the effect of Mn(+2) concentration on the decolorization efficiency was investigated to establish the optimal application of the MnP-oxidative system. The enzymatic treatment provoked not only the destruction of the chromophoric groups but also a noticeable breakdown of the chemical structure of the dye. In experiments with pure enzyme, MnP proved to be the main factor responsible for the dye decolorization.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11590609</PMID><DateCompleted><Year>2002</Year><Month>02</Month><Day>21</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3592</ISSN><JournalIssue CitedMedium="Print"><Volume>75</Volume><Issue>3</Issue><PubDate><Year>2001</Year><Month>Nov</Month><Day>05</Day></PubDate></JournalIssue><Title>Biotechnology and bioengineering</Title><ISOAbbreviation>Biotechnol Bioeng</ISOAbbreviation></Journal><ArticleTitle>In vitro degradation of a polymeric dye (Poly R-478) by manganese peroxidase.</ArticleTitle><Pagination><MedlinePgn>362-8</MedlinePgn></Pagination><Abstract><AbstractText>The aim of this study is the evaluation of the enzymatic action of the ligninolytic enzyme manganese peroxidase (MnP), through a suitable addition of H(2)O(2), as a feasible system for the in vitro degradation of complex structures. For this purpose, a highly recalcitrant polymeric dye (Poly R-478) was selected as a model compound. An amperometric technique was used to determine the H(2)O(2) requirement in the decolorization by nonpurified MnP. Two H(2)O(2) supply strategies-fed-batch (every hour) or semicontinuous (every 5 min)-were applied. The addition of H(2)O(2) in pulses led to a limited decolorization after the pulses and the instantaneous consumption or decomposition of H(2)O(2). Therefore, this way of addition may limit the actual H(2)O(2) concentration in the reaction mixture. In contrast, the semicontinuous strategy maintained lower and prolonged concentrations of H(2)O(2), which allowed a clearly greater decolorization (48% after 2 h). In addition, the effect of Mn(+2) concentration on the decolorization efficiency was investigated to establish the optimal application of the MnP-oxidative system. The enzymatic treatment provoked not only the destruction of the chromophoric groups but also a noticeable breakdown of the chemical structure of the dye. In experiments with pure enzyme, MnP proved to be the main factor responsible for the dye decolorization.</AbstractText><CopyrightInformation>Copyright 2001 John Wiley & Sons, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Moreira</LastName><ForeName>M T</ForeName><Initials>MT</Initials><AffiliationInfo><Affiliation>Department of Chemical Engineering, Institute of Technology, University of Santiago de Compostela, E-15706 Santiago de Compostela, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Palma</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Mielgo</LastName><ForeName>I</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Feijoo</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Lema</LastName><ForeName>J M</ForeName><Initials>JM</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biotechnol Bioeng</MedlineTA><NlmUniqueID>7502021</NlmUniqueID><ISSNLinking>0006-3592</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000880">Anthraquinones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004396">Coloring Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011108">Polymers</NameOfSubstance></Chemical><Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber><NameOfSubstance UI="D008345">Manganese</NameOfSubstance></Chemical><Chemical><RegistryNumber>68816-54-6</RegistryNumber><NameOfSubstance UI="C017971">poly R-478</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000880" MajorTopicYN="N">Anthraquinones</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003116" MajorTopicYN="N">Color</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004396" MajorTopicYN="N">Coloring Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008345" MajorTopicYN="N">Manganese</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011108" MajorTopicYN="N">Polymers</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>10</Month><Day>9</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>2</Month><Day>22</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>10</Month><Day>9</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11590609</ArticleId><ArticleId IdType="pii">10.1002/bit.10052</ArticleId><ArticleId IdType="doi">10.1002/bit.10052</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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