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Characterization of a novel endo-β-1,4-glucanase from Armillaria gemina and its application in biomass hydrolysis.

Identifieur interne : 002337 ( Main/Exploration ); précédent : 002336; suivant : 002338

Characterization of a novel endo-β-1,4-glucanase from Armillaria gemina and its application in biomass hydrolysis.

Auteurs : Sujit Sadashiv Jagtap [Corée du Sud] ; Saurabh Sudha Dhiman ; Tae-Su Kim ; In-Won Kim ; Jung-Kul Lee

Source :

RBID : pubmed:23604561

Descripteurs français

English descriptors

Abstract

A novel endo-β-1,4-glucanase (EG)-producing strain was isolated and identified as Armillaria gemina KJS114 based on its morphology and internal transcribed spacer rDNA gene sequence. A. gemina EG (AgEG) was purified using a single-step purification by gel filtration. The relative molecular mass of AgEG by sodium dodecyl sulfate polyacrylamide gel electrophoresis was 65 kDa and by size exclusion chromatography was 66 kDa, indicating that the enzyme is a monomer in solution. The pH and temperature optima for hydrolysis were 5.0 and 60 °C, respectively. Purified AgEG had the highest catalytic efficiency with carboxymethylcellulose (k(cat)/K(m) = 3,590 mg mL⁻¹ s⁻¹) unlike that reported for any fungal EG, highlighting the significance of the current study. The amino acid sequence of AgEG showed homology with hydrolases from the glycoside hydrolase family 61. The addition of AgEG to a Populus nigra hydrolysate reaction containing a commercial cellulase mixture (Celluclast 1.5L and Novozyme 188) showed a stimulatory effect on reducing sugar production. AgEG is a good candidate for applications that convert lignocellulosic biomass to biofuels and chemicals.

DOI: 10.1007/s00253-013-4894-x
PubMed: 23604561


Affiliations:


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Le document en format XML

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<term>Armillaria (genetics)</term>
<term>Armillaria (isolation & purification)</term>
<term>Biomass (MeSH)</term>
<term>Carbohydrate Metabolism (MeSH)</term>
<term>Cellulase (chemistry)</term>
<term>Cellulase (isolation & purification)</term>
<term>Cellulase (metabolism)</term>
<term>Chromatography, Gel (MeSH)</term>
<term>DNA, Fungal (chemistry)</term>
<term>DNA, Fungal (genetics)</term>
<term>DNA, Ribosomal Spacer (chemistry)</term>
<term>DNA, Ribosomal Spacer (genetics)</term>
<term>Enzyme Stability (MeSH)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Hydrolysis (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Molecular Weight (MeSH)</term>
<term>Populus (metabolism)</term>
<term>Sequence Analysis, DNA (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Temperature (MeSH)</term>
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<term>ADN fongique (composition chimique)</term>
<term>ADN fongique (génétique)</term>
<term>Analyse de séquence d'ADN (MeSH)</term>
<term>Armillaria (classification)</term>
<term>Armillaria (enzymologie)</term>
<term>Armillaria (génétique)</term>
<term>Armillaria (isolement et purification)</term>
<term>Biomasse (MeSH)</term>
<term>Cellulase (composition chimique)</term>
<term>Cellulase (isolement et purification)</term>
<term>Cellulase (métabolisme)</term>
<term>Chromatographie sur gel (MeSH)</term>
<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Espaceur de l'ADN ribosomique (composition chimique)</term>
<term>Espaceur de l'ADN ribosomique (génétique)</term>
<term>Hydrolyse (MeSH)</term>
<term>Masse moléculaire (MeSH)</term>
<term>Métabolisme glucidique (MeSH)</term>
<term>Populus (métabolisme)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Stabilité enzymatique (MeSH)</term>
<term>Température (MeSH)</term>
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<term>Cellulase</term>
<term>DNA, Fungal</term>
<term>DNA, Ribosomal Spacer</term>
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<term>Armillaria</term>
<term>Cellulase</term>
<term>Espaceur de l'ADN ribosomique</term>
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<term>Armillaria</term>
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<term>Armillaria</term>
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<term>DNA, Fungal</term>
<term>DNA, Ribosomal Spacer</term>
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<term>Armillaria</term>
<term>Espaceur de l'ADN ribosomique</term>
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<term>Armillaria</term>
<term>Cellulase</term>
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<term>Cellulase</term>
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<term>Chromatography, Gel</term>
<term>Enzyme Stability</term>
<term>Hydrogen-Ion Concentration</term>
<term>Hydrolysis</term>
<term>Molecular Sequence Data</term>
<term>Molecular Weight</term>
<term>Sequence Analysis, DNA</term>
<term>Sequence Homology, Amino Acid</term>
<term>Temperature</term>
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<term>Chromatographie sur gel</term>
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<term>Masse moléculaire</term>
<term>Métabolisme glucidique</term>
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<front>
<div type="abstract" xml:lang="en">A novel endo-β-1,4-glucanase (EG)-producing strain was isolated and identified as Armillaria gemina KJS114 based on its morphology and internal transcribed spacer rDNA gene sequence. A. gemina EG (AgEG) was purified using a single-step purification by gel filtration. The relative molecular mass of AgEG by sodium dodecyl sulfate polyacrylamide gel electrophoresis was 65 kDa and by size exclusion chromatography was 66 kDa, indicating that the enzyme is a monomer in solution. The pH and temperature optima for hydrolysis were 5.0 and 60 °C, respectively. Purified AgEG had the highest catalytic efficiency with carboxymethylcellulose (k(cat)/K(m) = 3,590 mg mL⁻¹ s⁻¹) unlike that reported for any fungal EG, highlighting the significance of the current study. The amino acid sequence of AgEG showed homology with hydrolases from the glycoside hydrolase family 61. The addition of AgEG to a Populus nigra hydrolysate reaction containing a commercial cellulase mixture (Celluclast 1.5L and Novozyme 188) showed a stimulatory effect on reducing sugar production. AgEG is a good candidate for applications that convert lignocellulosic biomass to biofuels and chemicals.</div>
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