PhanerochaeteV1, Main, Exploration, bibRecord, 000183

Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds.

Identifieur interne : 000183 ( Main/Exploration ); précédent : 000182; suivant : 000184

Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds.

Auteurs : Silvia Hüttner [Suède] ; Sylvia Klaubauf [Suède] ; Ronald P. De Vries [Pays-Bas] ; Lisbeth Olsson [Suède]

Source :

Applied microbiology and biotechnology [ 1432-0614 ] ; 2017.

RBID : pubmed:28429057

Descripteurs français

KwdFr :
- Acide glucuronique (composition chimique), Acide glucuronique (métabolisme), Acide glucuronique (pharmacologie), Acremonium (effets des médicaments et des substances chimiques), Acremonium (enzymologie), Acremonium (génétique), Biomasse (MeSH), Champignons (effets des médicaments et des substances chimiques), Champignons (enzymologie), Champignons (génétique), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Esterases (composition chimique), Esterases (génétique), Esterases (métabolisme), Esters (composition chimique), Esters (métabolisme), Glucides (composition chimique), Métabolisme glucidique (MeSH), Phanerochaete (effets des médicaments et des substances chimiques), Phanerochaete (enzymologie), Phanerochaete (génétique), Spécificité du substrat (MeSH), Wolfiporia (effets des médicaments et des substances chimiques), Wolfiporia (enzymologie), Wolfiporia (génétique).
MESH :
- composition chimique : Acide glucuronique, Esterases, Esters, Glucides.
- effets des médicaments et des substances chimiques : Acremonium, Champignons, Phanerochaete, Wolfiporia.
- enzymologie : Acremonium, Champignons, Phanerochaete, Wolfiporia.
- génétique : Acremonium, Champignons, Esterases, Phanerochaete, Wolfiporia.
- métabolisme : Acide glucuronique, Esterases, Esters.
- pharmacologie : Acide glucuronique.
- Biomasse, Cinétique, Concentration en ions d'hydrogène, Métabolisme glucidique, Spécificité du substrat.

English descriptors

KwdEn :
- Acremonium (drug effects), Acremonium (enzymology), Acremonium (genetics), Biomass (MeSH), Carbohydrate Metabolism (MeSH), Carbohydrates (chemistry), Esterases (chemistry), Esterases (genetics), Esterases (metabolism), Esters (chemistry), Esters (metabolism), Fungi (drug effects), Fungi (enzymology), Fungi (genetics), Glucuronic Acid (chemistry), Glucuronic Acid (metabolism), Glucuronic Acid (pharmacology), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), Phanerochaete (drug effects), Phanerochaete (enzymology), Phanerochaete (genetics), Substrate Specificity (MeSH), Wolfiporia (drug effects), Wolfiporia (enzymology), Wolfiporia (genetics).
MESH :
- chemical , chemistry : Carbohydrates, Esterases, Esters, Glucuronic Acid.
- drug effects : Acremonium, Fungi, Phanerochaete, Wolfiporia.
- enzymology : Acremonium, Fungi, Phanerochaete, Wolfiporia.
- genetics : Acremonium, Esterases, Fungi, Phanerochaete, Wolfiporia.
- chemical , metabolism : Esterases, Esters, Glucuronic Acid.
- chemical , pharmacology : Glucuronic Acid.
- Biomass, Carbohydrate Metabolism, Hydrogen-Ion Concentration, Kinetics, Substrate Specificity.

Abstract

The glucuronoyl esterases (GEs) that have been identified so far belong to family 15 of the carbohydrate esterases in the CAZy classification system and are presumed to target ester bonds between lignin alcohols and (4-O-methyl-)D-glucuronic acid residues of xylan. Few GEs have been cloned, expressed and characterised to date. Characterisation has been done on a variety of synthetic substrates; however, the number of commercially available substrates is very limited. We identified novel putative GEs from a wide taxonomic range of fungi and expressed the enzymes originating from Acremonium alcalophilum and Wolfiporia cocos as well as the previously described PcGE1 from Phanerochaete chrysosporium. All three fungal GEs were active on the commercially available compounds benzyl glucuronic acid (BnGlcA), allyl glucuronic acid (allylGlcA) and to a lower degree on methyl glucuronic acid (MeGlcA). The enzymes showed pH stability over a wide pH range and tolerated 6-h incubations of up to 50 °C. Kinetic parameters were determined for BnGlcA. This study shows the suitability of the commercially available model compounds BnGlcA, MeGlcA and allylGlcA in GE activity screening and characterisation experiments. We enriched the spectrum of characterised GEs with two new members of a relatively young enzyme family. Due to its biotechnological significance, this family deserves to be more extensively studied. The presented enzymes are promising candidates as auxiliary enzymes to improve saccharification of plant biomass.

DOI: 10.1007/s00253-017-8266-9
PubMed: 28429057
PubMed Central: PMC5486812

Affiliations:

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

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Le document en format XML

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<term>Biomass (MeSH)</term>
<term>Carbohydrate Metabolism (MeSH)</term>
<term>Carbohydrates (chemistry)</term>
<term>Esterases (chemistry)</term>
<term>Esterases (genetics)</term>
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<term>Glucuronic Acid (pharmacology)</term>
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<term>Kinetics (MeSH)</term>
<term>Phanerochaete (drug effects)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
<term>Substrate Specificity (MeSH)</term>
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<term>Esterases (génétique)</term>
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<term>Esters (métabolisme)</term>
<term>Glucides (composition chimique)</term>
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<term>Phanerochaete (enzymologie)</term>
<term>Phanerochaete (génétique)</term>
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<term>Wolfiporia (effets des médicaments et des substances chimiques)</term>
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<term>Wolfiporia (génétique)</term>
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<term>Esterases</term>
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<term>Wolfiporia</term>
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<term>Champignons</term>
<term>Esterases</term>
<term>Phanerochaete</term>
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<front><div type="abstract" xml:lang="en">The glucuronoyl esterases (GEs) that have been identified so far belong to family 15 of the carbohydrate esterases in the CAZy classification system and are presumed to target ester bonds between lignin alcohols and (4-O-methyl-)D-glucuronic acid residues of xylan. Few GEs have been cloned, expressed and characterised to date. Characterisation has been done on a variety of synthetic substrates; however, the number of commercially available substrates is very limited. We identified novel putative GEs from a wide taxonomic range of fungi and expressed the enzymes originating from Acremonium alcalophilum and Wolfiporia cocos as well as the previously described PcGE1 from Phanerochaete chrysosporium. All three fungal GEs were active on the commercially available compounds benzyl glucuronic acid (BnGlcA), allyl glucuronic acid (allylGlcA) and to a lower degree on methyl glucuronic acid (MeGlcA). The enzymes showed pH stability over a wide pH range and tolerated 6-h incubations of up to 50 °C. Kinetic parameters were determined for BnGlcA. This study shows the suitability of the commercially available model compounds BnGlcA, MeGlcA and allylGlcA in GE activity screening and characterisation experiments. We enriched the spectrum of characterised GEs with two new members of a relatively young enzyme family. Due to its biotechnological significance, this family deserves to be more extensively studied. The presented enzymes are promising candidates as auxiliary enzymes to improve saccharification of plant biomass.</div>
</front>
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<Abstract><AbstractText>The glucuronoyl esterases (GEs) that have been identified so far belong to family 15 of the carbohydrate esterases in the CAZy classification system and are presumed to target ester bonds between lignin alcohols and (4-O-methyl-)D-glucuronic acid residues of xylan. Few GEs have been cloned, expressed and characterised to date. Characterisation has been done on a variety of synthetic substrates; however, the number of commercially available substrates is very limited. We identified novel putative GEs from a wide taxonomic range of fungi and expressed the enzymes originating from Acremonium alcalophilum and Wolfiporia cocos as well as the previously described PcGE1 from Phanerochaete chrysosporium. All three fungal GEs were active on the commercially available compounds benzyl glucuronic acid (BnGlcA), allyl glucuronic acid (allylGlcA) and to a lower degree on methyl glucuronic acid (MeGlcA). The enzymes showed pH stability over a wide pH range and tolerated 6-h incubations of up to 50 °C. Kinetic parameters were determined for BnGlcA. This study shows the suitability of the commercially available model compounds BnGlcA, MeGlcA and allylGlcA in GE activity screening and characterisation experiments. We enriched the spectrum of characterised GEs with two new members of a relatively young enzyme family. Due to its biotechnological significance, this family deserves to be more extensively studied. The presented enzymes are promising candidates as auxiliary enzymes to improve saccharification of plant biomass.</AbstractText>
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<AffiliationInfo><Affiliation>Wallenberg Wood Science Center, Chalmers University of Technology, SE-412 96, Gothenburg, Sweden.</Affiliation>
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<AffiliationInfo><Affiliation>Division of Industrial Biotechnology, Department of Biology and Biological Engineering, Chalmers University of Technology, SE-412 96, Gothenburg, Sweden.</Affiliation>
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<AffiliationInfo><Affiliation>Wallenberg Wood Science Center, Chalmers University of Technology, SE-412 96, Gothenburg, Sweden.</Affiliation>
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<Author ValidYN="Y"><LastName>de Vries</LastName>
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<AffiliationInfo><Affiliation>Wallenberg Wood Science Center, Chalmers University of Technology, SE-412 96, Gothenburg, Sweden. lisbeth.olsson@chalmers.se.</Affiliation>
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Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds.

Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds.

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