Serveur d'exploration sur le phanerochaete

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Characterization of extracellular peroxidases produced by acetate-buffered cultures of the lignin-degrading basidiomycete Phanerochaete chrysosporium.

Identifieur interne : 000F68 ( Main/Exploration ); précédent : 000F67; suivant : 000F69

Characterization of extracellular peroxidases produced by acetate-buffered cultures of the lignin-degrading basidiomycete Phanerochaete chrysosporium.

Auteurs : S B Dass [États-Unis] ; C A Reddy

Source :

RBID : pubmed:2210334

Descripteurs français

English descriptors

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


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Le document en format XML

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<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>
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<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>
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<term>Lignin</term>
<term>Peroxidases</term>
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<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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<term>Basidiomycota</term>
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<term>Lignine</term>
<term>Peroxidases</term>
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<term>Amino Acid Sequence</term>
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<term>Molecular Sequence Data</term>
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<term>Acide acétique</term>
<term>Acétates</term>
<term>Chromatographie</term>
<term>Données de séquences moléculaires</term>
<term>Masse moléculaire</term>
<term>Substances tampon</term>
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<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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<Title>FEMS microbiology letters</Title>
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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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<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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