Characterization of extracellular peroxidases produced by acetate-buffered cultures of the lignin-degrading basidiomycete Phanerochaete chrysosporium.
Identifieur interne : 000F68 ( Main/Exploration ); précédent : 000F67; suivant : 000F69Characterization of extracellular peroxidases produced by acetate-buffered cultures of the lignin-degrading basidiomycete Phanerochaete chrysosporium.
Auteurs : S B Dass [États-Unis] ; C A ReddySource :
- FEMS microbiology letters [ 0378-1097 ] ; 1990.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Basidiomycota.
- métabolisme : Lignine, Peroxidases.
- Acide acétique, Acétates, Chromatographie, Données de séquences moléculaires, Masse moléculaire, Substances tampon, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Lignin, Peroxidases.
- chemical : Acetates, Acetic Acid, Buffers.
- enzymology : Basidiomycota.
- Amino Acid Sequence, Chromatography, Molecular Sequence Data, Molecular Weight.
Abstract
Growth of Phanerochaete chrysosporium in a nitrogen-limited medium buffered with sodium acetate, instead of the commonly used 2,2-dimethylsuccinate (DMS), resulted in quantitative and qualitative differences in the production of various extracellular lignin peroxidases (LIPs) and manganese-dependent peroxidases (MNPs) involved in lignin degradation. The results indicate that production of LIPs and MNPs can be selectively enhanced by manipulation of culture conditions. Partial N-terminal analyses of the major LIPs and MNPs have made it possible to assign a specific protein to the specific genes and cDNAs that have been reported recently. The LIPs and MNPs differed widely in their ability to decolorize various dyes that are known to be degraded by the lignin degrading enzyme system of P. chrysosporium.
DOI: 10.1111/j.1574-6968.1990.tb04233.x
PubMed: 2210334
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<affiliation wicri:level="4"><nlm:affiliation>Department of Microbiology and Public Health, Michigan State University, East Lansing 48824-1101.</nlm:affiliation>
<orgName type="university">Université d'État du Michigan</orgName>
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<placeName><settlement type="city">East Lansing</settlement>
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<author><name sortKey="Reddy, C A" sort="Reddy, C A" uniqKey="Reddy C" first="C A" last="Reddy">C A Reddy</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetates (MeSH)</term>
<term>Acetic Acid (MeSH)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Basidiomycota (enzymology)</term>
<term>Buffers (MeSH)</term>
<term>Chromatography (MeSH)</term>
<term>Lignin (metabolism)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Molecular Weight (MeSH)</term>
<term>Peroxidases (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acide acétique (MeSH)</term>
<term>Acétates (MeSH)</term>
<term>Basidiomycota (enzymologie)</term>
<term>Chromatographie (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Lignine (métabolisme)</term>
<term>Masse moléculaire (MeSH)</term>
<term>Peroxidases (métabolisme)</term>
<term>Substances tampon (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term>
<term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Acetates</term>
<term>Acetic Acid</term>
<term>Buffers</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term>
<term>Peroxidases</term>
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<term>Molecular Sequence Data</term>
<term>Molecular Weight</term>
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<term>Acétates</term>
<term>Chromatographie</term>
<term>Données de séquences moléculaires</term>
<term>Masse moléculaire</term>
<term>Substances tampon</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Growth of Phanerochaete chrysosporium in a nitrogen-limited medium buffered with sodium acetate, instead of the commonly used 2,2-dimethylsuccinate (DMS), resulted in quantitative and qualitative differences in the production of various extracellular lignin peroxidases (LIPs) and manganese-dependent peroxidases (MNPs) involved in lignin degradation. The results indicate that production of LIPs and MNPs can be selectively enhanced by manipulation of culture conditions. Partial N-terminal analyses of the major LIPs and MNPs have made it possible to assign a specific protein to the specific genes and cDNAs that have been reported recently. The LIPs and MNPs differed widely in their ability to decolorize various dyes that are known to be degraded by the lignin degrading enzyme system of P. chrysosporium.</div>
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<DateRevised><Year>2019</Year>
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<Issue>3</Issue>
<PubDate><Year>1990</Year>
<Month>Jun</Month>
<Day>01</Day>
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<Title>FEMS microbiology letters</Title>
<ISOAbbreviation>FEMS Microbiol Lett</ISOAbbreviation>
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<ArticleTitle>Characterization of extracellular peroxidases produced by acetate-buffered cultures of the lignin-degrading basidiomycete Phanerochaete chrysosporium.</ArticleTitle>
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<Abstract><AbstractText>Growth of Phanerochaete chrysosporium in a nitrogen-limited medium buffered with sodium acetate, instead of the commonly used 2,2-dimethylsuccinate (DMS), resulted in quantitative and qualitative differences in the production of various extracellular lignin peroxidases (LIPs) and manganese-dependent peroxidases (MNPs) involved in lignin degradation. The results indicate that production of LIPs and MNPs can be selectively enhanced by manipulation of culture conditions. Partial N-terminal analyses of the major LIPs and MNPs have made it possible to assign a specific protein to the specific genes and cDNAs that have been reported recently. The LIPs and MNPs differed widely in their ability to decolorize various dyes that are known to be degraded by the lignin degrading enzyme system of P. chrysosporium.</AbstractText>
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