Oxidative degradation of high molecular weight chlorolignin by manganese peroxidase of Phanerochaete chrysosporium.
Identifieur interne : 000F07 ( Main/Corpus ); précédent : 000F06; suivant : 000F08Oxidative degradation of high molecular weight chlorolignin by manganese peroxidase of Phanerochaete chrysosporium.
Auteurs : R. Lackner ; E. Srebotnik ; K. MessnerSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1991.
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
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pubmed:1872832Le document en format XML
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<author><name sortKey="Lackner, R" sort="Lackner, R" uniqKey="Lackner R" first="R" last="Lackner">R. Lackner</name>
<affiliation><nlm:affiliation>Abteilung Mykologie, Technische Universität Wien, Austria.</nlm:affiliation>
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<author><name sortKey="Srebotnik, E" sort="Srebotnik, E" uniqKey="Srebotnik E" first="E" last="Srebotnik">E. Srebotnik</name>
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<author><name sortKey="Messner, K" sort="Messner, K" uniqKey="Messner K" first="K" last="Messner">K. Messner</name>
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<author><name sortKey="Lackner, R" sort="Lackner, R" uniqKey="Lackner R" first="R" last="Lackner">R. Lackner</name>
<affiliation><nlm:affiliation>Abteilung Mykologie, Technische Universität Wien, Austria.</nlm:affiliation>
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<author><name sortKey="Srebotnik, E" sort="Srebotnik, E" uniqKey="Srebotnik E" first="E" last="Srebotnik">E. Srebotnik</name>
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<author><name sortKey="Messner, K" sort="Messner, K" uniqKey="Messner K" first="K" last="Messner">K. Messner</name>
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<series><title level="j">Biochemical and biophysical research communications</title>
<idno type="ISSN">0006-291X</idno>
<imprint><date when="1991" type="published">1991</date>
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<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="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term>
<term>Manganese</term>
<term>Peroxidases</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Agaricales</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Manganese</term>
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<keywords scheme="MESH" xml:lang="en"><term>Chromatography, Gel</term>
<term>Kinetics</term>
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<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>
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<Issue>3</Issue>
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<Month>Aug</Month>
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<Title>Biochemical and biophysical research communications</Title>
<ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation>
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<ArticleTitle>Oxidative degradation of high molecular weight chlorolignin by manganese peroxidase of Phanerochaete chrysosporium.</ArticleTitle>
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<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>
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