PhanerochaeteV1, Main, Exploration, bibRecord, 000F22

Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay.

Identifieur interne : 000F22 ( Main/Exploration ); précédent : 000F21; suivant : 000F23

Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay.

Auteurs : A. Datta ; A. Bettermann ; T K Kirk

Source :

Applied and environmental microbiology [ 0099-2240 ] ; 1991.

RBID : pubmed:1854201

Descripteurs français

KwdFr :
- Alcohol oxidoreductases (isolement et purification), Alcohol oxidoreductases (ultrastructure), Basidiomycota (enzymologie), Basidiomycota (métabolisme), Bois (MeSH), Chromatographie d'échange d'ions (MeSH), Cinétique (MeSH), Données de séquences moléculaires (MeSH), Dépollution biologique de l'environnement (MeSH), Lignine (métabolisme), Peroxidases (isolement et purification), Peroxidases (métabolisme), Peroxidases (ultrastructure), Protéines fongiques (isolement et purification), Protéines fongiques (ultrastructure), Séquence d'acides aminés (MeSH), Technique de Western (MeSH).
MESH :
- enzymologie : Basidiomycota.
- isolement et purification : Alcohol oxidoreductases, Peroxidases, Protéines fongiques.
- métabolisme : Basidiomycota, Lignine, Peroxidases.
- ultrastructure : Alcohol oxidoreductases, Peroxidases, Protéines fongiques.
- Bois, Chromatographie d'échange d'ions, Cinétique, Données de séquences moléculaires, Dépollution biologique de l'environnement, Séquence d'acides aminés, Technique de Western.

English descriptors

KwdEn :
- Alcohol Oxidoreductases (isolation & purification), Alcohol Oxidoreductases (ultrastructure), Amino Acid Sequence (MeSH), Basidiomycota (enzymology), Basidiomycota (metabolism), Biodegradation, Environmental (MeSH), Blotting, Western (MeSH), Chromatography, Ion Exchange (MeSH), Fungal Proteins (isolation & purification), Fungal Proteins (ultrastructure), Kinetics (MeSH), Lignin (metabolism), Molecular Sequence Data (MeSH), Peroxidases (isolation & purification), Peroxidases (metabolism), Peroxidases (ultrastructure), Wood (MeSH).
MESH :
- chemical , isolation & purification : Alcohol Oxidoreductases, Fungal Proteins, Peroxidases.
- chemical , metabolism : Lignin, Peroxidases.
- chemical , ultrastructure : Alcohol Oxidoreductases, Fungal Proteins, Peroxidases.
- enzymology : Basidiomycota.
- metabolism : Basidiomycota.
- Amino Acid Sequence, Biodegradation, Environmental, Blotting, Western, Chromatography, Ion Exchange, Kinetics, Molecular Sequence Data, Wood.

Abstract

The specific enzymes associated with lignin degradation in solid lignocellulosic substrates have not been identified. Therefore, we examined extracts of cultures of Phanerochaete chrysosporium that were degrading a mechanical pulp of aspen wood. Western blot (immunoblot) analyses of the partially purified protein revealed lignin peroxidase, manganese-dependent peroxidase (MnP), and glyoxal oxidase. The dominant peroxidase, an isoenzyme of MnP (pI 4.9), was isolated, and its N-terminal amino acid sequence and amino acid composition were determined. The results reveal both similarities to and differences from the deduced amino acid sequences from cDNA clones of dominant MnP isoenzymes from liquid cultures. Our results suggest, therefore, that the ligninolytic-enzyme-encoding genes that are expressed during solid substrate degradation differ from those expressed in liquid culture or are allelic variants of their liquid culture counterparts. In addition to lignin peroxidase, MnP, and glyoxal oxidase, xylanase and protease activities were present in the extracts of the degrading pulp.

DOI: 10.1128/AEM.57.5.1453-1460.1991
PubMed: 1854201
PubMed Central: PMC182969

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (isolation & purification)</term>
<term>Alcohol Oxidoreductases (ultrastructure)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Basidiomycota (enzymology)</term>
<term>Basidiomycota (metabolism)</term>
<term>Biodegradation, Environmental (MeSH)</term>
<term>Blotting, Western (MeSH)</term>
<term>Chromatography, Ion Exchange (MeSH)</term>
<term>Fungal Proteins (isolation & purification)</term>
<term>Fungal Proteins (ultrastructure)</term>
<term>Kinetics (MeSH)</term>
<term>Lignin (metabolism)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Peroxidases (isolation & purification)</term>
<term>Peroxidases (metabolism)</term>
<term>Peroxidases (ultrastructure)</term>
<term>Wood (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Alcohol oxidoreductases (isolement et purification)</term>
<term>Alcohol oxidoreductases (ultrastructure)</term>
<term>Basidiomycota (enzymologie)</term>
<term>Basidiomycota (métabolisme)</term>
<term>Bois (MeSH)</term>
<term>Chromatographie d'échange d'ions (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Dépollution biologique de l'environnement (MeSH)</term>
<term>Lignine (métabolisme)</term>
<term>Peroxidases (isolement et purification)</term>
<term>Peroxidases (métabolisme)</term>
<term>Peroxidases (ultrastructure)</term>
<term>Protéines fongiques (isolement et purification)</term>
<term>Protéines fongiques (ultrastructure)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Technique de Western (MeSH)</term>
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<term>Fungal Proteins</term>
<term>Peroxidases</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term>
<term>Peroxidases</term>
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<keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Alcohol Oxidoreductases</term>
<term>Fungal Proteins</term>
<term>Peroxidases</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Basidiomycota</term>
<term>Lignine</term>
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<term>Blotting, Western</term>
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<term>Kinetics</term>
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<term>Cinétique</term>
<term>Données de séquences moléculaires</term>
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<front><div type="abstract" xml:lang="en">The specific enzymes associated with lignin degradation in solid lignocellulosic substrates have not been identified. Therefore, we examined extracts of cultures of Phanerochaete chrysosporium that were degrading a mechanical pulp of aspen wood. Western blot (immunoblot) analyses of the partially purified protein revealed lignin peroxidase, manganese-dependent peroxidase (MnP), and glyoxal oxidase. The dominant peroxidase, an isoenzyme of MnP (pI 4.9), was isolated, and its N-terminal amino acid sequence and amino acid composition were determined. The results reveal both similarities to and differences from the deduced amino acid sequences from cDNA clones of dominant MnP isoenzymes from liquid cultures. Our results suggest, therefore, that the ligninolytic-enzyme-encoding genes that are expressed during solid substrate degradation differ from those expressed in liquid culture or are allelic variants of their liquid culture counterparts. In addition to lignin peroxidase, MnP, and glyoxal oxidase, xylanase and protease activities were present in the extracts of the degrading pulp.</div>
</front>
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<Abstract><AbstractText>The specific enzymes associated with lignin degradation in solid lignocellulosic substrates have not been identified. Therefore, we examined extracts of cultures of Phanerochaete chrysosporium that were degrading a mechanical pulp of aspen wood. Western blot (immunoblot) analyses of the partially purified protein revealed lignin peroxidase, manganese-dependent peroxidase (MnP), and glyoxal oxidase. The dominant peroxidase, an isoenzyme of MnP (pI 4.9), was isolated, and its N-terminal amino acid sequence and amino acid composition were determined. The results reveal both similarities to and differences from the deduced amino acid sequences from cDNA clones of dominant MnP isoenzymes from liquid cultures. Our results suggest, therefore, that the ligninolytic-enzyme-encoding genes that are expressed during solid substrate degradation differ from those expressed in liquid culture or are allelic variants of their liquid culture counterparts. In addition to lignin peroxidase, MnP, and glyoxal oxidase, xylanase and protease activities were present in the extracts of the degrading pulp.</AbstractText>
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Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay.

Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay.

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