PhanerochaeteV1, Main, Exploration, bibRecord, 000201

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases.

Identifieur interne : 000201 ( Main/Exploration ); précédent : 000200; suivant : 000202

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases.

Auteurs : Camilla Lambertz [Allemagne] ; Selin Ece [Allemagne] ; Rainer Fischer [Allemagne] ; Ulrich Commandeur [Allemagne]

Source :

Bioengineered [ 2165-5987 ] ; 2016.

RBID : pubmed:27295524

Descripteurs français

KwdFr :
- Cinétique (MeSH), Clonage moléculaire (MeSH), Expression des gènes (MeSH), Génie métabolique (méthodes), Humains (MeSH), Hydrolyse (MeSH), Lignine (composition chimique), Lignine (métabolisme), Oxydoréduction (MeSH), Peroxidases (biosynthèse), Peroxidases (composition chimique), Peroxidases (génétique), Phanerochaete (enzymologie), Phanerochaete (génétique), Pichia (enzymologie), Pichia (génétique), Protéines recombinantes (biosynthèse), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique).
MESH :
- biosynthèse : Peroxidases, Protéines recombinantes.
- composition chimique : Lignine, Peroxidases, Protéines recombinantes.
- enzymologie : Phanerochaete, Pichia, Saccharomyces cerevisiae.
- génétique : Peroxidases, Phanerochaete, Pichia, Protéines recombinantes, Saccharomyces cerevisiae.
- métabolisme : Lignine.
- méthodes : Génie métabolique.
- Cinétique, Clonage moléculaire, Expression des gènes, Humains, Hydrolyse, Oxydoréduction.

English descriptors

KwdEn :
- Cloning, Molecular (MeSH), Gene Expression (MeSH), Humans (MeSH), Hydrolysis (MeSH), Kinetics (MeSH), Lignin (chemistry), Lignin (metabolism), Metabolic Engineering (methods), Oxidation-Reduction (MeSH), Peroxidases (biosynthesis), Peroxidases (chemistry), Peroxidases (genetics), Phanerochaete (enzymology), Phanerochaete (genetics), Pichia (enzymology), Pichia (genetics), Recombinant Proteins (biosynthesis), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics).
MESH :
- chemical , biosynthesis : Peroxidases, Recombinant Proteins.
- chemical , chemistry : Lignin, Peroxidases, Recombinant Proteins.
- chemical , genetics : Peroxidases, Recombinant Proteins.
- chemical , metabolism : Lignin.
- enzymology : Phanerochaete, Pichia, Saccharomyces cerevisiae.
- genetics : Phanerochaete, Pichia, Saccharomyces cerevisiae.
- methods : Metabolic Engineering.
- Cloning, Molecular, Gene Expression, Humans, Hydrolysis, Kinetics, Oxidation-Reduction.

Abstract

Lignin is 1 of the 3 major components of lignocellulose. Its polymeric structure includes aromatic subunits that can be converted into high-value-added products, but this potential cannot yet been fully exploited because lignin is highly recalcitrant to degradation. Different approaches for the depolymerization of lignin have been tested, including pyrolysis, chemical oxidation, and hydrolysis under supercritical conditions. An additional strategy is the use of lignin-degrading enzymes, which imitates the natural degradation process. A versatile set of enzymes for lignin degradation has been identified, and research has focused on the production of recombinant enzymes in sufficient amounts to characterize their structure and reaction mechanisms. Enzymes have been analyzed individually and in combinations using artificial substrates, lignin model compounds, lignin and lignocellulose. Here we consider progress in the production of recombinant lignin-degrading peroxidases, the advantages and disadvantages of different expression hosts, and obstacles that must be overcome before such enzymes can be characterized and used for the industrial processing of lignin.

DOI: 10.1080/21655979.2016.1191705
PubMed: 27295524
PubMed Central: PMC4927207

Affiliations:

Allemagne

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

to stream Main, to step Corpus: 000208
to stream Main, to step Curation: 000208

Le document en format XML

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<front><div type="abstract" xml:lang="en">Lignin is 1 of the 3 major components of lignocellulose. Its polymeric structure includes aromatic subunits that can be converted into high-value-added products, but this potential cannot yet been fully exploited because lignin is highly recalcitrant to degradation. Different approaches for the depolymerization of lignin have been tested, including pyrolysis, chemical oxidation, and hydrolysis under supercritical conditions. An additional strategy is the use of lignin-degrading enzymes, which imitates the natural degradation process. A versatile set of enzymes for lignin degradation has been identified, and research has focused on the production of recombinant enzymes in sufficient amounts to characterize their structure and reaction mechanisms. Enzymes have been analyzed individually and in combinations using artificial substrates, lignin model compounds, lignin and lignocellulose. Here we consider progress in the production of recombinant lignin-degrading peroxidases, the advantages and disadvantages of different expression hosts, and obstacles that must be overcome before such enzymes can be characterized and used for the industrial processing of lignin.</div>
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<Abstract><AbstractText>Lignin is 1 of the 3 major components of lignocellulose. Its polymeric structure includes aromatic subunits that can be converted into high-value-added products, but this potential cannot yet been fully exploited because lignin is highly recalcitrant to degradation. Different approaches for the depolymerization of lignin have been tested, including pyrolysis, chemical oxidation, and hydrolysis under supercritical conditions. An additional strategy is the use of lignin-degrading enzymes, which imitates the natural degradation process. A versatile set of enzymes for lignin degradation has been identified, and research has focused on the production of recombinant enzymes in sufficient amounts to characterize their structure and reaction mechanisms. Enzymes have been analyzed individually and in combinations using artificial substrates, lignin model compounds, lignin and lignocellulose. Here we consider progress in the production of recombinant lignin-degrading peroxidases, the advantages and disadvantages of different expression hosts, and obstacles that must be overcome before such enzymes can be characterized and used for the industrial processing of lignin.</AbstractText>
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Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases.

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases.

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