Serveur d'exploration sur le phanerochaete

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In vitro degradation of natural insoluble lignin in aqueous media by the extracellular peroxidases of Phanerochaete chrysosporium.

Identifieur interne : 000B71 ( Main/Exploration ); précédent : 000B70; suivant : 000B72

In vitro degradation of natural insoluble lignin in aqueous media by the extracellular peroxidases of Phanerochaete chrysosporium.

Auteurs : D N Thompson [États-Unis] ; B R Hames ; C A Reddy ; H E Grethlein

Source :

RBID : pubmed:10099250

Descripteurs français

English descriptors

Abstract

The lignin peroxidases (LIP) and manganese peroxidases (MNP) of Phanerochaete chrysosporium catalyze a wide range of lignin depolymerization reactions with lignin models and synthetic lignins in solution. However, their ability to degrade insoluble natural lignin in aqueous media has not been demonstrated. Insoluble isolated poplar lignin similar to natural lignin was treated in vitro in aqueous media for 12 h with LIP, MNP, and both. Treatment with MNP alone slightly increased the solid mass and produced measurable amounts of lignin-derived 2,6-dimethoxyhydroquinone and 2-methoxyhydroquinone but did not appreciably decrease the total lignin content. Treatment with LIP alone did not decrease the mass but produced measurable amounts of lignin-derived p-hydroxybenzoic acid and slightly decreased the lignin content. Finally, treatment with LIP and MNP together decreased the solid mass by 11%, decreased the lignin content by 5%, and released low-concentration compounds with mass spectra containing the typical lignin-derived electron-impact fragments of mass 107, 137, 151, 167, and 181. These results suggest that MNP increases the effectiveness of LIP-mediated lignin degradation.

DOI: 10.1002/(sici)1097-0290(19980320)57:6<704::aid-bit8>3.0.co;2-p
PubMed: 10099250


Affiliations:


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Le document en format XML

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<nlm:affiliation>Department of Chemical Engineering, Michigan State University, East Lansing, Michigan 48824, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
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<term>Dialysis (methods)</term>
<term>Extracellular Matrix (enzymology)</term>
<term>Gas Chromatography-Mass Spectrometry (MeSH)</term>
<term>Image Processing, Computer-Assisted (MeSH)</term>
<term>Lignin (chemistry)</term>
<term>Lignin (metabolism)</term>
<term>Peroxidases (chemistry)</term>
<term>Peroxidases (metabolism)</term>
<term>Phanerochaete (enzymology)</term>
<term>Software (MeSH)</term>
<term>Solubility (MeSH)</term>
<term>Spectroscopy, Fourier Transform Infrared (methods)</term>
<term>Water (MeSH)</term>
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<term>Bioréacteurs (MeSH)</term>
<term>Chromatographie gazeuse-spectrométrie de masse (MeSH)</term>
<term>Dialyse (méthodes)</term>
<term>Dépollution biologique de l'environnement (MeSH)</term>
<term>Eau (MeSH)</term>
<term>Lignine (composition chimique)</term>
<term>Lignine (métabolisme)</term>
<term>Logiciel (MeSH)</term>
<term>Matrice extracellulaire (enzymologie)</term>
<term>Peroxidases (composition chimique)</term>
<term>Peroxidases (métabolisme)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Solubilité (MeSH)</term>
<term>Spectroscopie infrarouge à transformée de Fourier (méthodes)</term>
<term>Traitement d'image par ordinateur (MeSH)</term>
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<term>Peroxidases</term>
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<term>Peroxidases</term>
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<term>Peroxidases</term>
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<div type="abstract" xml:lang="en">The lignin peroxidases (LIP) and manganese peroxidases (MNP) of Phanerochaete chrysosporium catalyze a wide range of lignin depolymerization reactions with lignin models and synthetic lignins in solution. However, their ability to degrade insoluble natural lignin in aqueous media has not been demonstrated. Insoluble isolated poplar lignin similar to natural lignin was treated in vitro in aqueous media for 12 h with LIP, MNP, and both. Treatment with MNP alone slightly increased the solid mass and produced measurable amounts of lignin-derived 2,6-dimethoxyhydroquinone and 2-methoxyhydroquinone but did not appreciably decrease the total lignin content. Treatment with LIP alone did not decrease the mass but produced measurable amounts of lignin-derived p-hydroxybenzoic acid and slightly decreased the lignin content. Finally, treatment with LIP and MNP together decreased the solid mass by 11%, decreased the lignin content by 5%, and released low-concentration compounds with mass spectra containing the typical lignin-derived electron-impact fragments of mass 107, 137, 151, 167, and 181. These results suggest that MNP increases the effectiveness of LIP-mediated lignin degradation.</div>
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<AbstractText>The lignin peroxidases (LIP) and manganese peroxidases (MNP) of Phanerochaete chrysosporium catalyze a wide range of lignin depolymerization reactions with lignin models and synthetic lignins in solution. However, their ability to degrade insoluble natural lignin in aqueous media has not been demonstrated. Insoluble isolated poplar lignin similar to natural lignin was treated in vitro in aqueous media for 12 h with LIP, MNP, and both. Treatment with MNP alone slightly increased the solid mass and produced measurable amounts of lignin-derived 2,6-dimethoxyhydroquinone and 2-methoxyhydroquinone but did not appreciably decrease the total lignin content. Treatment with LIP alone did not decrease the mass but produced measurable amounts of lignin-derived p-hydroxybenzoic acid and slightly decreased the lignin content. Finally, treatment with LIP and MNP together decreased the solid mass by 11%, decreased the lignin content by 5%, and released low-concentration compounds with mass spectra containing the typical lignin-derived electron-impact fragments of mass 107, 137, 151, 167, and 181. These results suggest that MNP increases the effectiveness of LIP-mediated lignin degradation.</AbstractText>
<CopyrightInformation>Copyright 1998 John Wiley & Sons, Inc.</CopyrightInformation>
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