Do the extracellular enzymes cellobiose dehydrogenase and manganese peroxidase form a pathway in lignin biodegradation?
Identifieur interne : 000A88 ( Main/Corpus ); précédent : 000A87; suivant : 000A89Do the extracellular enzymes cellobiose dehydrogenase and manganese peroxidase form a pathway in lignin biodegradation?
Auteurs : L. Hildén ; G. Johansson ; G. Pettersson ; J. Li ; P. Ljungquist ; G. HenrikssonSource :
- FEBS letters [ 0014-5793 ] ; 2000.
English descriptors
- KwdEn :
- Anisoles (chemistry), Anisoles (metabolism), Benzyl Alcohols (chemistry), Benzyl Alcohols (metabolism), Biodegradation, Environmental (MeSH), Carbohydrate Dehydrogenases (metabolism), Chromatography, High Pressure Liquid (MeSH), Gas Chromatography-Mass Spectrometry (MeSH), Glycols (chemistry), Glycols (metabolism), Hydrogen Peroxide (metabolism), Hydroxyl Radical (metabolism), Hydroxylation (MeSH), Lignin (chemistry), Lignin (metabolism), Manganese Compounds (metabolism), Oxidants (metabolism), Oxidation-Reduction (MeSH), Peroxidases (metabolism), Phanerochaete (enzymology), Phenols (metabolism), Spectrophotometry, Ultraviolet (MeSH).
- MESH :
- chemical , chemistry : Anisoles, Benzyl Alcohols, Glycols, Lignin.
- chemical , metabolism : Anisoles, Benzyl Alcohols, Carbohydrate Dehydrogenases, Glycols, Hydrogen Peroxide, Hydroxyl Radical, Lignin, Manganese Compounds, Oxidants, Peroxidases, Phenols.
- enzymology : Phanerochaete.
- Biodegradation, Environmental, Chromatography, High Pressure Liquid, Gas Chromatography-Mass Spectrometry, Hydroxylation, Oxidation-Reduction, Spectrophotometry, Ultraviolet.
Abstract
The extracellular enzyme manganese peroxidase is believed to degrade lignin by a hydrogen peroxide-dependent oxidation of Mn(II) to the reactive species Mn(III) that attacks the lignin. However, Mn(III) is not able to directly oxidise the non-phenolic lignin structures that predominate in native lignin. We show here that pretreatment of a non-phenolic lignin model compound with another extracellular fungal enzyme, cellobiose dehydrogenase, allows the manganese peroxidase system to oxidise this molecule. The mechanism behind this effect is demethoxylation and/or hydroxylation, i.e. conversion of a non-phenolic structure to a phenolic one, mediated by hydroxyl radicals generated by cellobiose dehydrogenase. This suggests that cellobiose dehydrogenase and manganese peroxidase may act in an extracellular pathway in fungal lignin biodegradation. Analytical techniques used in this paper are reverse-phase high-pressure liquid chromatography, gas chromatography connected to mass spectroscopy and UV-visible spectroscopy.
DOI: 10.1016/s0014-5793(00)01757-9
PubMed: 10899314
Links to Exploration step
pubmed:10899314Le document en format XML
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<author><name sortKey="Hilden, L" sort="Hilden, L" uniqKey="Hilden L" first="L" last="Hildén">L. Hildén</name>
<affiliation><nlm:affiliation>Department of Pulp and Paper Chemistry and Technology, Royal Institute of Technology, Drottning Kristinas väg 53, SE-100 44 Stockholm, Sweden.</nlm:affiliation>
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<author><name sortKey="Johansson, G" sort="Johansson, G" uniqKey="Johansson G" first="G" last="Johansson">G. Johansson</name>
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<author><name sortKey="Pettersson, G" sort="Pettersson, G" uniqKey="Pettersson G" first="G" last="Pettersson">G. Pettersson</name>
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<author><name sortKey="Li, J" sort="Li, J" uniqKey="Li J" first="J" last="Li">J. Li</name>
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<author><name sortKey="Ljungquist, P" sort="Ljungquist, P" uniqKey="Ljungquist P" first="P" last="Ljungquist">P. Ljungquist</name>
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<author><name sortKey="Henriksson, G" sort="Henriksson, G" uniqKey="Henriksson G" first="G" last="Henriksson">G. Henriksson</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anisoles (chemistry)</term>
<term>Anisoles (metabolism)</term>
<term>Benzyl Alcohols (chemistry)</term>
<term>Benzyl Alcohols (metabolism)</term>
<term>Biodegradation, Environmental (MeSH)</term>
<term>Carbohydrate Dehydrogenases (metabolism)</term>
<term>Chromatography, High Pressure Liquid (MeSH)</term>
<term>Gas Chromatography-Mass Spectrometry (MeSH)</term>
<term>Glycols (chemistry)</term>
<term>Glycols (metabolism)</term>
<term>Hydrogen Peroxide (metabolism)</term>
<term>Hydroxyl Radical (metabolism)</term>
<term>Hydroxylation (MeSH)</term>
<term>Lignin (chemistry)</term>
<term>Lignin (metabolism)</term>
<term>Manganese Compounds (metabolism)</term>
<term>Oxidants (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peroxidases (metabolism)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phenols (metabolism)</term>
<term>Spectrophotometry, Ultraviolet (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Anisoles</term>
<term>Benzyl Alcohols</term>
<term>Glycols</term>
<term>Lignin</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Anisoles</term>
<term>Benzyl Alcohols</term>
<term>Carbohydrate Dehydrogenases</term>
<term>Glycols</term>
<term>Hydrogen Peroxide</term>
<term>Hydroxyl Radical</term>
<term>Lignin</term>
<term>Manganese Compounds</term>
<term>Oxidants</term>
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<keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term>
<term>Chromatography, High Pressure Liquid</term>
<term>Gas Chromatography-Mass Spectrometry</term>
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<front><div type="abstract" xml:lang="en">The extracellular enzyme manganese peroxidase is believed to degrade lignin by a hydrogen peroxide-dependent oxidation of Mn(II) to the reactive species Mn(III) that attacks the lignin. However, Mn(III) is not able to directly oxidise the non-phenolic lignin structures that predominate in native lignin. We show here that pretreatment of a non-phenolic lignin model compound with another extracellular fungal enzyme, cellobiose dehydrogenase, allows the manganese peroxidase system to oxidise this molecule. The mechanism behind this effect is demethoxylation and/or hydroxylation, i.e. conversion of a non-phenolic structure to a phenolic one, mediated by hydroxyl radicals generated by cellobiose dehydrogenase. This suggests that cellobiose dehydrogenase and manganese peroxidase may act in an extracellular pathway in fungal lignin biodegradation. Analytical techniques used in this paper are reverse-phase high-pressure liquid chromatography, gas chromatography connected to mass spectroscopy and UV-visible spectroscopy.</div>
</front>
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<Abstract><AbstractText>The extracellular enzyme manganese peroxidase is believed to degrade lignin by a hydrogen peroxide-dependent oxidation of Mn(II) to the reactive species Mn(III) that attacks the lignin. However, Mn(III) is not able to directly oxidise the non-phenolic lignin structures that predominate in native lignin. We show here that pretreatment of a non-phenolic lignin model compound with another extracellular fungal enzyme, cellobiose dehydrogenase, allows the manganese peroxidase system to oxidise this molecule. The mechanism behind this effect is demethoxylation and/or hydroxylation, i.e. conversion of a non-phenolic structure to a phenolic one, mediated by hydroxyl radicals generated by cellobiose dehydrogenase. This suggests that cellobiose dehydrogenase and manganese peroxidase may act in an extracellular pathway in fungal lignin biodegradation. Analytical techniques used in this paper are reverse-phase high-pressure liquid chromatography, gas chromatography connected to mass spectroscopy and UV-visible spectroscopy.</AbstractText>
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