Serveur d'exploration sur le phanerochaete

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Enhanced Delignification of Lignocellulosic Biomass by Recombinant Fungus Phanerochaete chrysosporium Overexpressing Laccases and Peroxidases.

Identifieur interne : 000121 ( Main/Exploration ); précédent : 000120; suivant : 000122

Enhanced Delignification of Lignocellulosic Biomass by Recombinant Fungus Phanerochaete chrysosporium Overexpressing Laccases and Peroxidases.

Auteurs : Nancy Coconi Linares [Mexique] ; Francisco Fernández [Mexique] ; Achim M. Loske [Mexique] ; Miguel A. G Mez-Lim [Mexique]

Source :

RBID : pubmed:29486469

Descripteurs français

English descriptors

Abstract

Ligninolytic enzyme production and lignin degradation are typically the rate-limiting steps in the biofuel industry. To improve the efficiency of simultaneous bio-delignification and enzyme production, Phanerochaete chrysosporium was transformed by shock wave-induced acoustic cavitation to co-overexpress 3 peroxidases and 1 laccase and test it on the degradation of sugarcane bagasse and wheat bran. Lignin depolymerization was enhanced by up to 25% in the presence of recombinant fungi in comparison with the wild-type strain. Sugar release on lignocellulose was 2- to 6-fold higher by recombinant fungi as compared with the control. Wheat bran ostensibly stimulated the production of ligninolytic enzymes. The highest peroxidase activity from the recombinant strains was 2.6-fold higher, whereas the increase in laccase activity was 4-fold higher in comparison to the control. The improvement of lignin degradation was directly proportional to the highest peroxidase and laccase activity. Because various phenolic compounds released during lignocellulose degradation have proven to be toxic to cells and to inhibit enzyme activity, a significant reduction (over 40%) of the total phenolic content in the samples treated with recombinant strains was observed. To our knowledge, this is the first report that engineering P. chrysosporium enhances biodegradation of lignocellulosic biomass.

DOI: 10.1159/000485976
PubMed: 29486469


Affiliations:


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Le document en format XML

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<term>Biofuels (MeSH)</term>
<term>Biomass (MeSH)</term>
<term>Cellulose (metabolism)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Dietary Fiber (MeSH)</term>
<term>Ergosterol (MeSH)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Laccase (biosynthesis)</term>
<term>Laccase (genetics)</term>
<term>Lignin (metabolism)</term>
<term>Metabolic Engineering (MeSH)</term>
<term>Peroxidases (biosynthesis)</term>
<term>Peroxidases (genetics)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
<term>Phanerochaete (growth & development)</term>
<term>Phanerochaete (metabolism)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Saccharum (MeSH)</term>
<term>Transformation, Genetic (MeSH)</term>
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<term>Biocarburants (MeSH)</term>
<term>Biomasse (MeSH)</term>
<term>Cellulose (métabolisme)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Dépollution biologique de l'environnement (MeSH)</term>
<term>Ergostérol (MeSH)</term>
<term>Fibre alimentaire (MeSH)</term>
<term>Génie métabolique (MeSH)</term>
<term>Laccase (biosynthèse)</term>
<term>Laccase (génétique)</term>
<term>Lignine (métabolisme)</term>
<term>Peroxidases (biosynthèse)</term>
<term>Peroxidases (génétique)</term>
<term>Phanerochaete (croissance et développement)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Phanerochaete (génétique)</term>
<term>Phanerochaete (métabolisme)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Saccharum (MeSH)</term>
<term>Transformation génétique (MeSH)</term>
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<term>Laccase</term>
<term>Peroxidases</term>
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<term>Fungal Proteins</term>
<term>Laccase</term>
<term>Peroxidases</term>
<term>Recombinant Proteins</term>
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<term>Cellulose</term>
<term>Fungal Proteins</term>
<term>Lignin</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en">
<term>Biofuels</term>
<term>Dietary Fiber</term>
<term>Ergosterol</term>
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<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr">
<term>Laccase</term>
<term>Peroxidases</term>
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<keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr">
<term>Phanerochaete</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr">
<term>Phanerochaete</term>
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<term>Phanerochaete</term>
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<term>Phanerochaete</term>
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<term>Phanerochaete</term>
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<term>Laccase</term>
<term>Peroxidases</term>
<term>Phanerochaete</term>
<term>Protéines fongiques</term>
<term>Protéines recombinantes</term>
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<term>Phanerochaete</term>
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<term>Lignine</term>
<term>Phanerochaete</term>
<term>Protéines fongiques</term>
<term>Protéines recombinantes</term>
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<term>Cloning, Molecular</term>
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<term>Metabolic Engineering</term>
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<term>Transformation, Genetic</term>
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<term>Génie métabolique</term>
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<div type="abstract" xml:lang="en">Ligninolytic enzyme production and lignin degradation are typically the rate-limiting steps in the biofuel industry. To improve the efficiency of simultaneous bio-delignification and enzyme production, Phanerochaete chrysosporium was transformed by shock wave-induced acoustic cavitation to co-overexpress 3 peroxidases and 1 laccase and test it on the degradation of sugarcane bagasse and wheat bran. Lignin depolymerization was enhanced by up to 25% in the presence of recombinant fungi in comparison with the wild-type strain. Sugar release on lignocellulose was 2- to 6-fold higher by recombinant fungi as compared with the control. Wheat bran ostensibly stimulated the production of ligninolytic enzymes. The highest peroxidase activity from the recombinant strains was 2.6-fold higher, whereas the increase in laccase activity was 4-fold higher in comparison to the control. The improvement of lignin degradation was directly proportional to the highest peroxidase and laccase activity. Because various phenolic compounds released during lignocellulose degradation have proven to be toxic to cells and to inhibit enzyme activity, a significant reduction (over 40%) of the total phenolic content in the samples treated with recombinant strains was observed. To our knowledge, this is the first report that engineering P. chrysosporium enhances biodegradation of lignocellulosic biomass.</div>
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<AbstractText>Ligninolytic enzyme production and lignin degradation are typically the rate-limiting steps in the biofuel industry. To improve the efficiency of simultaneous bio-delignification and enzyme production, Phanerochaete chrysosporium was transformed by shock wave-induced acoustic cavitation to co-overexpress 3 peroxidases and 1 laccase and test it on the degradation of sugarcane bagasse and wheat bran. Lignin depolymerization was enhanced by up to 25% in the presence of recombinant fungi in comparison with the wild-type strain. Sugar release on lignocellulose was 2- to 6-fold higher by recombinant fungi as compared with the control. Wheat bran ostensibly stimulated the production of ligninolytic enzymes. The highest peroxidase activity from the recombinant strains was 2.6-fold higher, whereas the increase in laccase activity was 4-fold higher in comparison to the control. The improvement of lignin degradation was directly proportional to the highest peroxidase and laccase activity. Because various phenolic compounds released during lignocellulose degradation have proven to be toxic to cells and to inhibit enzyme activity, a significant reduction (over 40%) of the total phenolic content in the samples treated with recombinant strains was observed. To our knowledge, this is the first report that engineering P. chrysosporium enhances biodegradation of lignocellulosic biomass.</AbstractText>
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<Keyword MajorTopicYN="Y">Phanerochaete chrysosporium</Keyword>
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