Oxidative degradation of high molecular weight chlorolignin by manganese peroxidase of Phanerochaete chrysosporium.
Identifieur interne : 000F04 ( Main/Exploration ); précédent : 000F03; suivant : 000F05Oxidative degradation of high molecular weight chlorolignin by manganese peroxidase of Phanerochaete chrysosporium.
Auteurs : R. Lackner [Autriche] ; E. Srebotnik ; K. MessnerSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1991.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Agaricales.
- métabolisme : Lignine, Manganèse, Peroxidases.
- pharmacologie : Manganèse.
- Chromatographie sur gel, Cinétique.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Lignin, Manganese, Peroxidases.
- enzymology : Agaricales.
- chemical , pharmacology : Manganese.
- Chromatography, Gel, Kinetics.
Abstract
Phanerochaete chrysosporium was able to degrade high molecular weight chlorolignins (Mr greater than 30,000) from bleach plant effluents, although a direct contact between ligninolytic enzymes and chlorolignin was prevented by a dialysis tubing. In the absence of the enzymes, Mn3+ depolymerized chlorolignin when complexed with lactate causing the color, chemical oxygen demand (COD) and dry weight to decrease by 80%, 60% and 40%, respectively. Manganese peroxidase effectively catalyzed the depolymerization of chlorolignin in the presence of Mn2+ and H2O2. It can be concluded from these results that manganese peroxidase plays the major role in the initial breakdown and decolorization of high molecular weight chlorolignin in bleach plant effluents by P. chrysosporium in vivo.
DOI: 10.1016/0006-291x(91)91004-v
PubMed: 1872832
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Messner</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991</date><idno type="RBID">pubmed:1872832</idno><idno type="pmid">1872832</idno><idno type="doi">10.1016/0006-291x(91)91004-v</idno><idno type="wicri:Area/Main/Corpus">000F07</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000F07</idno><idno type="wicri:Area/Main/Curation">000F07</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000F07</idno><idno type="wicri:Area/Main/Exploration">000F07</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Oxidative degradation of high molecular weight chlorolignin by manganese peroxidase of Phanerochaete chrysosporium.</title><author><name sortKey="Lackner, R" sort="Lackner, R" uniqKey="Lackner R" first="R" last="Lackner">R. Lackner</name><affiliation wicri:level="1"><nlm:affiliation>Abteilung Mykologie, Technische Universität Wien, Austria.</nlm:affiliation><country xml:lang="fr">Autriche</country><wicri:regionArea>Abteilung Mykologie, Technische Universität Wien</wicri:regionArea><wicri:noRegion>Technische Universität Wien</wicri:noRegion></affiliation></author><author><name sortKey="Srebotnik, E" sort="Srebotnik, E" uniqKey="Srebotnik E" first="E" last="Srebotnik">E. Srebotnik</name></author><author><name sortKey="Messner, K" sort="Messner, K" uniqKey="Messner K" first="K" last="Messner">K. Messner</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Agaricales (enzymology)</term><term>Chromatography, Gel (MeSH)</term><term>Kinetics (MeSH)</term><term>Lignin (metabolism)</term><term>Manganese (metabolism)</term><term>Manganese (pharmacology)</term><term>Peroxidases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agaricales (enzymologie)</term><term>Chromatographie sur gel (MeSH)</term><term>Cinétique (MeSH)</term><term>Lignine (métabolisme)</term><term>Manganèse (métabolisme)</term><term>Manganèse (pharmacologie)</term><term>Peroxidases (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term><term>Manganese</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term><term>Manganèse</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Manganèse</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Manganese</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Gel</term><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie sur gel</term><term>Cinétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Phanerochaete chrysosporium was able to degrade high molecular weight chlorolignins (Mr greater than 30,000) from bleach plant effluents, although a direct contact between ligninolytic enzymes and chlorolignin was prevented by a dialysis tubing. In the absence of the enzymes, Mn3+ depolymerized chlorolignin when complexed with lactate causing the color, chemical oxygen demand (COD) and dry weight to decrease by 80%, 60% and 40%, respectively. Manganese peroxidase effectively catalyzed the depolymerization of chlorolignin in the presence of Mn2+ and H2O2. It can be concluded from these results that manganese peroxidase plays the major role in the initial breakdown and decolorization of high molecular weight chlorolignin in bleach plant effluents by P. chrysosporium in vivo.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1872832</PMID><DateCompleted><Year>1991</Year><Month>09</Month><Day>18</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>178</Volume><Issue>3</Issue><PubDate><Year>1991</Year><Month>Aug</Month><Day>15</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Oxidative degradation of high molecular weight chlorolignin by manganese peroxidase of Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>1092-8</MedlinePgn></Pagination><Abstract><AbstractText>Phanerochaete chrysosporium was able to degrade high molecular weight chlorolignins (Mr greater than 30,000) from bleach plant effluents, although a direct contact between ligninolytic enzymes and chlorolignin was prevented by a dialysis tubing. In the absence of the enzymes, Mn3+ depolymerized chlorolignin when complexed with lactate causing the color, chemical oxygen demand (COD) and dry weight to decrease by 80%, 60% and 40%, respectively. Manganese peroxidase effectively catalyzed the depolymerization of chlorolignin in the presence of Mn2+ and H2O2. It can be concluded from these results that manganese peroxidase plays the major role in the initial breakdown and decolorization of high molecular weight chlorolignin in bleach plant effluents by P. chrysosporium in vivo.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lackner</LastName><ForeName>R</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Abteilung Mykologie, Technische Universität Wien, Austria.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Srebotnik</LastName><ForeName>E</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Messner</LastName><ForeName>K</ForeName><Initials>K</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber><NameOfSubstance UI="D008345">Manganese</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</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="D000363" MajorTopicYN="N">Agaricales</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008345" MajorTopicYN="N">Manganese</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>8</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>8</Month><Day>15</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>8</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1872832</ArticleId><ArticleId IdType="pii">0006-291X(91)91004-V</ArticleId><ArticleId IdType="doi">10.1016/0006-291x(91)91004-v</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Autriche</li></country></list><tree><noCountry><name sortKey="Messner, K" sort="Messner, K" uniqKey="Messner K" first="K" last="Messner">K. Messner</name><name sortKey="Srebotnik, E" sort="Srebotnik, E" uniqKey="Srebotnik E" first="E" last="Srebotnik">E. Srebotnik</name></noCountry><country name="Autriche"><noRegion><name sortKey="Lackner, R" sort="Lackner, R" uniqKey="Lackner R" first="R" last="Lackner">R. Lackner</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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