Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju.
Identifieur interne : 001005 ( Main/Curation ); précédent : 001004; suivant : 001006Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju.
Auteurs : R. Bourbonnais ; M G PaiceSource :
- The Biochemical journal [ 0264-6021 ] ; 1988.
Descripteurs français
- KwdFr :
- Acides aminés (analyse), Alcohol oxidoreductases (isolement et purification), Alcohol oxidoreductases (métabolisme), Basidiomycota (enzymologie), Chromatographie d'échange d'ions (MeSH), Cinétique (MeSH), Laccase (MeSH), Lignine (métabolisme), Oxidoreductases (métabolisme), Polyporaceae (enzymologie), Spectrophotométrie UV (MeSH), Spécificité du substrat (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- analyse : Acides aminés.
- enzymologie : Basidiomycota, Polyporaceae.
- isolement et purification : Alcohol oxidoreductases.
- métabolisme : Alcohol oxidoreductases, Lignine, Oxidoreductases.
- Chromatographie d'échange d'ions, Cinétique, Laccase, Spectrophotométrie UV, Spécificité du substrat, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (isolation & purification), Alcohol Oxidoreductases (metabolism), Amino Acids (analysis), Basidiomycota (enzymology), Chromatography, Ion Exchange (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Kinetics (MeSH), Laccase (MeSH), Lignin (metabolism), Oxidoreductases (metabolism), Polyporaceae (enzymology), Spectrophotometry, Ultraviolet (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , analysis : Amino Acids.
- chemical , isolation & purification : Alcohol Oxidoreductases.
- chemical , metabolism : Alcohol Oxidoreductases, Lignin, Oxidoreductases.
- enzymology : Basidiomycota, Polyporaceae.
- Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Kinetics, Laccase, Spectrophotometry, Ultraviolet, Substrate Specificity.
Abstract
The basidiomycete Pleurotus sajor-caju mineralizes ring-14C-labelled lignin (dehydrogenative polymer) when grown in mycological broth. Under these conditions, two veratryl alcohol oxidase (VAO) enzymes were found in the culture medium. They oxidized a number of aromatic alcohols to aldehydes and reduced O2 to H2O2. The enzymes were purified by ion-exchange and gel-permeation chromatography. The final step of purification on Mono Q resolved the activity into two peaks (VAO I and VAO II). Both enzymes had the same Mr, approx. 71,000, but their isoelectric points differed slightly, 3.8 for VAO I and 4.0 for VAO II. Their amino acid compositions were similar except for aspartic acid/asparagine and glycine. Both enzymes are glycoproteins and contain flavin prosthetic groups. Their pH optima were around 5, and kinetic constants and specificities were similar. 4-Methoxybenzyl alcohol was oxidized the most rapidly, followed by veratryl alcohol. Not all aromatic alcohols were oxidized, neither were non-aromatic alcohols. Cinnamyl alcohol was oxidized at the gamma position. The VAO enzymes thus represent a significantly different route for veratryl alcohol oxidation from that catalysed by the previously found lignin peroxidases from Phanerochaete chrysosporium. The role of the oxidases in biodegradation might be to produce H2O2 during oxidation of lignin fragments.
DOI: 10.1042/bj2550445
PubMed: 3060110
PubMed Central: PMC1135248
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R. Bourbonnais<affiliation><nlm:affiliation>Pulp and Paper Research Institute of Canada, Pointe Claire, Quebec.</nlm:affiliation>
<wicri:noCountry code="subField">Quebec</wicri:noCountry>
</affiliation>
Le document en format XML
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<series><title level="j">The Biochemical journal</title>
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<imprint><date when="1988" type="published">1988</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (isolation & purification)</term>
<term>Alcohol Oxidoreductases (metabolism)</term>
<term>Amino Acids (analysis)</term>
<term>Basidiomycota (enzymology)</term>
<term>Chromatography, Ion Exchange (MeSH)</term>
<term>Electrophoresis, Polyacrylamide Gel (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Laccase (MeSH)</term>
<term>Lignin (metabolism)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Polyporaceae (enzymology)</term>
<term>Spectrophotometry, Ultraviolet (MeSH)</term>
<term>Substrate Specificity (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (analyse)</term>
<term>Alcohol oxidoreductases (isolement et purification)</term>
<term>Alcohol oxidoreductases (métabolisme)</term>
<term>Basidiomycota (enzymologie)</term>
<term>Chromatographie d'échange d'ions (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Laccase (MeSH)</term>
<term>Lignine (métabolisme)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Polyporaceae (enzymologie)</term>
<term>Spectrophotométrie UV (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Électrophorèse sur gel de polyacrylamide (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Amino Acids</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Alcohol Oxidoreductases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term>
<term>Lignin</term>
<term>Oxidoreductases</term>
</keywords>
<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Acides aminés</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term>
<term>Polyporaceae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term>
<term>Polyporaceae</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Alcohol oxidoreductases</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcohol oxidoreductases</term>
<term>Lignine</term>
<term>Oxidoreductases</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Chromatography, Ion Exchange</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Kinetics</term>
<term>Laccase</term>
<term>Spectrophotometry, Ultraviolet</term>
<term>Substrate Specificity</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Chromatographie d'échange d'ions</term>
<term>Cinétique</term>
<term>Laccase</term>
<term>Spectrophotométrie UV</term>
<term>Spécificité du substrat</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
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<front><div type="abstract" xml:lang="en">The basidiomycete Pleurotus sajor-caju mineralizes ring-14C-labelled lignin (dehydrogenative polymer) when grown in mycological broth. Under these conditions, two veratryl alcohol oxidase (VAO) enzymes were found in the culture medium. They oxidized a number of aromatic alcohols to aldehydes and reduced O2 to H2O2. The enzymes were purified by ion-exchange and gel-permeation chromatography. The final step of purification on Mono Q resolved the activity into two peaks (VAO I and VAO II). Both enzymes had the same Mr, approx. 71,000, but their isoelectric points differed slightly, 3.8 for VAO I and 4.0 for VAO II. Their amino acid compositions were similar except for aspartic acid/asparagine and glycine. Both enzymes are glycoproteins and contain flavin prosthetic groups. Their pH optima were around 5, and kinetic constants and specificities were similar. 4-Methoxybenzyl alcohol was oxidized the most rapidly, followed by veratryl alcohol. Not all aromatic alcohols were oxidized, neither were non-aromatic alcohols. Cinnamyl alcohol was oxidized at the gamma position. The VAO enzymes thus represent a significantly different route for veratryl alcohol oxidation from that catalysed by the previously found lignin peroxidases from Phanerochaete chrysosporium. The role of the oxidases in biodegradation might be to produce H2O2 during oxidation of lignin fragments.</div>
</front>
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<DateCompleted><Year>1989</Year>
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<DateRevised><Year>2019</Year>
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<PubDate><Year>1988</Year>
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<Title>The Biochemical journal</Title>
<ISOAbbreviation>Biochem J</ISOAbbreviation>
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<ArticleTitle>Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju.</ArticleTitle>
<Pagination><MedlinePgn>445-50</MedlinePgn>
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<Abstract><AbstractText>The basidiomycete Pleurotus sajor-caju mineralizes ring-14C-labelled lignin (dehydrogenative polymer) when grown in mycological broth. Under these conditions, two veratryl alcohol oxidase (VAO) enzymes were found in the culture medium. They oxidized a number of aromatic alcohols to aldehydes and reduced O2 to H2O2. The enzymes were purified by ion-exchange and gel-permeation chromatography. The final step of purification on Mono Q resolved the activity into two peaks (VAO I and VAO II). Both enzymes had the same Mr, approx. 71,000, but their isoelectric points differed slightly, 3.8 for VAO I and 4.0 for VAO II. Their amino acid compositions were similar except for aspartic acid/asparagine and glycine. Both enzymes are glycoproteins and contain flavin prosthetic groups. Their pH optima were around 5, and kinetic constants and specificities were similar. 4-Methoxybenzyl alcohol was oxidized the most rapidly, followed by veratryl alcohol. Not all aromatic alcohols were oxidized, neither were non-aromatic alcohols. Cinnamyl alcohol was oxidized at the gamma position. The VAO enzymes thus represent a significantly different route for veratryl alcohol oxidation from that catalysed by the previously found lignin peroxidases from Phanerochaete chrysosporium. The role of the oxidases in biodegradation might be to produce H2O2 during oxidation of lignin fragments.</AbstractText>
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