PhanerochaeteV1, Main, Exploration, bibRecord, 000288

Assembly of evolved ligninolytic genes in Saccharomyces cerevisiae.

Identifieur interne : 000288 ( Main/Exploration ); précédent : 000287; suivant : 000289

Assembly of evolved ligninolytic genes in Saccharomyces cerevisiae.

Auteurs : David Gonzalez-Perez [Espagne] ; Miguel Alcalde [Espagne]

Source :

Bioengineered [ 2165-5987 ]

RBID : pubmed:24830983

Descripteurs français

KwdFr :
- Clonage moléculaire (MeSH), Conformation des protéines (MeSH), Fermentation (MeSH), Ingénierie des protéines (MeSH), Laccase (génétique), Laccase (métabolisme), Lignine (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Pleurotus (enzymologie), Pleurotus (génétique), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Régions promotrices (génétique) (MeSH), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Vecteurs génétiques (génétique).
MESH :
- composition chimique : Lignine, Protéines recombinantes.
- enzymologie : Phanerochaete, Pleurotus, Saccharomyces cerevisiae.
- génétique : Laccase, Peroxidases, Phanerochaete, Pleurotus, Protéines recombinantes, Saccharomyces cerevisiae, Vecteurs génétiques.
- métabolisme : Laccase, Peroxidases.
- Clonage moléculaire, Conformation des protéines, Fermentation, Ingénierie des protéines, Régions promotrices (génétique).

English descriptors

KwdEn :
- Cloning, Molecular (MeSH), Fermentation (MeSH), Genetic Vectors (genetics), Laccase (genetics), Laccase (metabolism), Lignin (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Pleurotus (enzymology), Pleurotus (genetics), Promoter Regions, Genetic (MeSH), Protein Conformation (MeSH), Protein Engineering (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics).
MESH :
- chemical , chemistry : Lignin, Recombinant Proteins.
- chemical , genetics : Laccase, Peroxidases, Recombinant Proteins.
- enzymology : Phanerochaete, Pleurotus, Saccharomyces cerevisiae.
- genetics : Genetic Vectors, Phanerochaete, Pleurotus, Saccharomyces cerevisiae.
- chemical , metabolism : Laccase, Peroxidases.
- Cloning, Molecular, Fermentation, Promoter Regions, Genetic, Protein Conformation, Protein Engineering.

Abstract

The ligninolytic enzymatic consortium produced by white-rot fungi is one of the most efficient oxidative systems found in nature, with many potential applications that range from the production of 2nd generation biofuels to chemicals synthesis. In the current study, two high redox potential oxidoreductase fusion genes (laccase -Lac- and versatile peroxidase -Vp-) that had been evolved in the laboratory were re-assembled in Saccharomyces cerevisiae. First, cell viability and secretion were assessed after co-transforming the Lac and Vp genes into yeast. Several expression cassettes were inserted in vivo into episomal bi-directional vectors in order to evaluate inducible promoter and/or terminator pairs of different strengths in an individual and combined manner. The synthetic white-rot yeast model harboring Vp(GAL1/CYC1)-Lac(GAL10/ADH1) displayed up to 1000 and 100 Units per L of peroxidase and laccase activity, respectively, representing a suitable point of departure for future synthetic biology studies.

DOI: 10.4161/bioe.29167
PubMed: 24830983
PubMed Central: PMC4143396

Affiliations:

Espagne

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000320
to stream Main, to step Curation: 000320

Le document en format XML

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<term>Laccase (genetics)</term>
<term>Laccase (metabolism)</term>
<term>Lignin (chemistry)</term>
<term>Peroxidases (genetics)</term>
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<term>Phanerochaete (genetics)</term>
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<term>Saccharomyces cerevisiae (genetics)</term>
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<term>Conformation des protéines (MeSH)</term>
<term>Fermentation (MeSH)</term>
<term>Ingénierie des protéines (MeSH)</term>
<term>Laccase (génétique)</term>
<term>Laccase (métabolisme)</term>
<term>Lignine (composition chimique)</term>
<term>Peroxidases (génétique)</term>
<term>Peroxidases (métabolisme)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Phanerochaete (génétique)</term>
<term>Pleurotus (enzymologie)</term>
<term>Pleurotus (génétique)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Régions promotrices (génétique) (MeSH)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Vecteurs génétiques (génétique)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lignin</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Lignine</term>
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<term>Pleurotus</term>
<term>Saccharomyces cerevisiae</term>
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<term>Phanerochaete</term>
<term>Pleurotus</term>
<term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Laccase</term>
<term>Peroxidases</term>
<term>Phanerochaete</term>
<term>Pleurotus</term>
<term>Protéines recombinantes</term>
<term>Saccharomyces cerevisiae</term>
<term>Vecteurs génétiques</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Laccase</term>
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<front><div type="abstract" xml:lang="en">The ligninolytic enzymatic consortium produced by white-rot fungi is one of the most efficient oxidative systems found in nature, with many potential applications that range from the production of 2nd generation biofuels to chemicals synthesis. In the current study, two high redox potential oxidoreductase fusion genes (laccase -Lac- and versatile peroxidase -Vp-) that had been evolved in the laboratory were re-assembled in Saccharomyces cerevisiae. First, cell viability and secretion were assessed after co-transforming the Lac and Vp genes into yeast. Several expression cassettes were inserted in vivo into episomal bi-directional vectors in order to evaluate inducible promoter and/or terminator pairs of different strengths in an individual and combined manner. The synthetic white-rot yeast model harboring Vp(GAL1/CYC1)-Lac(GAL10/ADH1) displayed up to 1000 and 100 Units per L of peroxidase and laccase activity, respectively, representing a suitable point of departure for future synthetic biology studies. </div>
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<Abstract><AbstractText>The ligninolytic enzymatic consortium produced by white-rot fungi is one of the most efficient oxidative systems found in nature, with many potential applications that range from the production of 2nd generation biofuels to chemicals synthesis. In the current study, two high redox potential oxidoreductase fusion genes (laccase -Lac- and versatile peroxidase -Vp-) that had been evolved in the laboratory were re-assembled in Saccharomyces cerevisiae. First, cell viability and secretion were assessed after co-transforming the Lac and Vp genes into yeast. Several expression cassettes were inserted in vivo into episomal bi-directional vectors in order to evaluate inducible promoter and/or terminator pairs of different strengths in an individual and combined manner. The synthetic white-rot yeast model harboring Vp(GAL1/CYC1)-Lac(GAL10/ADH1) displayed up to 1000 and 100 Units per L of peroxidase and laccase activity, respectively, representing a suitable point of departure for future synthetic biology studies. </AbstractText>
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   |texte=   Assembly of evolved ligninolytic genes in Saccharomyces cerevisiae.
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Assembly of evolved ligninolytic genes in Saccharomyces cerevisiae.

Assembly of evolved ligninolytic genes in Saccharomyces cerevisiae.

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