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Accelerated degradation of lignin by lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium with engineered 4-O-methyltransferase from Clarkia breweri.

Identifieur interne : 000296 ( Main/Corpus ); précédent : 000295; suivant : 000297

Accelerated degradation of lignin by lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium with engineered 4-O-methyltransferase from Clarkia breweri.

Auteurs : Le Thanh Mai Pham ; Yong Hwan Kim

Source :

RBID : pubmed:25248703

English descriptors

Abstract

Free-hydroxyl phenolic units can decrease or even abort the catalytic activity of lignin peroxidase H8 during oxidation of veratryl alcohol and model lignin dimers, resulting in slow and inefficient lignin degradation. In this study we applied engineered 4-O-methyltransferase from Clarkia breweri to detoxify the inhibiting free-hydroxyl phenolic groups by converting them to methylated phenolic groups. The multistep, enzyme-catalyzed process that combines 4-O-methyltransferase and lignin peroxidase H8 suggested in this work can increase the efficiency of lignin-degradation. This study also suggests approaching the field of multi-enzyme in vitro systems to improve the understanding and development of plant biomass in biorefinery operations.

DOI: 10.1016/j.enzmictec.2014.08.011
PubMed: 25248703

Links to Exploration step

pubmed:25248703

Le document en format XML

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<name sortKey="Pham, Le Thanh Mai" sort="Pham, Le Thanh Mai" uniqKey="Pham L" first="Le Thanh Mai" last="Pham">Le Thanh Mai Pham</name>
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<nlm:affiliation>Department of Chemical Engineering, Kwangwoon University, 447-1, Wolgye-Dong, Nowon-Gu, Seoul 139-701, Republic of Korea.</nlm:affiliation>
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<name sortKey="Kim, Yong Hwan" sort="Kim, Yong Hwan" uniqKey="Kim Y" first="Yong Hwan" last="Kim">Yong Hwan Kim</name>
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<name sortKey="Pham, Le Thanh Mai" sort="Pham, Le Thanh Mai" uniqKey="Pham L" first="Le Thanh Mai" last="Pham">Le Thanh Mai Pham</name>
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<term>Benzyl Alcohols (metabolism)</term>
<term>Biodegradation, Environmental (MeSH)</term>
<term>Biomass (MeSH)</term>
<term>Clarkia (enzymology)</term>
<term>Clarkia (genetics)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Isoenzymes (genetics)</term>
<term>Isoenzymes (metabolism)</term>
<term>Lignin (metabolism)</term>
<term>Methyltransferases (genetics)</term>
<term>Methyltransferases (metabolism)</term>
<term>Peroxidases (genetics)</term>
<term>Peroxidases (metabolism)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Protein Engineering (MeSH)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
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<term>Benzyl Alcohols</term>
<term>Fungal Proteins</term>
<term>Isoenzymes</term>
<term>Lignin</term>
<term>Methyltransferases</term>
<term>Peroxidases</term>
<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en">
<term>Clarkia</term>
<term>Phanerochaete</term>
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<term>Clarkia</term>
<term>Phanerochaete</term>
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<div type="abstract" xml:lang="en">Free-hydroxyl phenolic units can decrease or even abort the catalytic activity of lignin peroxidase H8 during oxidation of veratryl alcohol and model lignin dimers, resulting in slow and inefficient lignin degradation. In this study we applied engineered 4-O-methyltransferase from Clarkia breweri to detoxify the inhibiting free-hydroxyl phenolic groups by converting them to methylated phenolic groups. The multistep, enzyme-catalyzed process that combines 4-O-methyltransferase and lignin peroxidase H8 suggested in this work can increase the efficiency of lignin-degradation. This study also suggests approaching the field of multi-enzyme in vitro systems to improve the understanding and development of plant biomass in biorefinery operations. </div>
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<AbstractText>Free-hydroxyl phenolic units can decrease or even abort the catalytic activity of lignin peroxidase H8 during oxidation of veratryl alcohol and model lignin dimers, resulting in slow and inefficient lignin degradation. In this study we applied engineered 4-O-methyltransferase from Clarkia breweri to detoxify the inhibiting free-hydroxyl phenolic groups by converting them to methylated phenolic groups. The multistep, enzyme-catalyzed process that combines 4-O-methyltransferase and lignin peroxidase H8 suggested in this work can increase the efficiency of lignin-degradation. This study also suggests approaching the field of multi-enzyme in vitro systems to improve the understanding and development of plant biomass in biorefinery operations. </AbstractText>
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