PoplarV1, Main, Exploration, bibRecord, 001F18

A highly efficient recombinant laccase from the yeast Yarrowia lipolytica and its application in the hydrolysis of biomass.

Identifieur interne : 001F18 ( Main/Exploration ); précédent : 001F17; suivant : 001F19

A highly efficient recombinant laccase from the yeast Yarrowia lipolytica and its application in the hydrolysis of biomass.

Auteurs : Dayanand Kalyani [Corée du Sud] ; Manish Kumar Tiwari [Corée du Sud] ; Jinglin Li [Corée du Sud] ; Sun Chang Kim [Corée du Sud] ; Vipin C. Kalia [Inde] ; Yun Chan Kang [Corée du Sud] ; Jung-Kul Lee [Corée du Sud]

Source :

PloS one [ 1932-6203 ] ; 2015.

RBID : pubmed:25781945

Descripteurs français

KwdFr :
- Biomasse (MeSH), Bois (composition chimique), Hydrolyse (MeSH), Laccase (composition chimique), Laccase (génétique), Pichia (génétique), Pichia (métabolisme), Populus (composition chimique), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Yarrowia (enzymologie), Yarrowia (génétique).
MESH :
- composition chimique : Bois, Laccase, Populus, Protéines fongiques, Protéines recombinantes.
- enzymologie : Yarrowia.
- génétique : Laccase, Pichia, Protéines fongiques, Protéines recombinantes, Yarrowia.
- métabolisme : Pichia.
- Biomasse, Hydrolyse.

English descriptors

KwdEn :
- Biomass (MeSH), Fungal Proteins (chemistry), Fungal Proteins (genetics), Hydrolysis (MeSH), Laccase (chemistry), Laccase (genetics), Pichia (genetics), Pichia (metabolism), Populus (chemistry), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Wood (chemistry), Yarrowia (enzymology), Yarrowia (genetics).
MESH :
- chemical , chemistry : Fungal Proteins, Laccase, Recombinant Proteins.
- chemical , genetics : Fungal Proteins, Laccase, Recombinant Proteins.
- chemistry : Populus, Wood.
- enzymology : Yarrowia.
- genetics : Pichia, Yarrowia.
- metabolism : Pichia.
- Biomass, Hydrolysis.

Abstract

A modified thermal asymmetric interlaced polymerase chain reaction was performed to obtain the first yeast laccase gene (YlLac) from the isolated yeast Yarrowia lipolytica. The 1557-bp full-length cDNA of YlLac encoded a mature laccase protein containing 519 amino acids preceded by a signal peptide of 19 amino acids, and the YlLac gene was expressed in the yeast Pichia pastoris. YlLac is a monomeric glycoprotein with a molecular mass of ~55 kDa as determined by polyacrylamide-gel electrophoresis. It showed a higher catalytic efficiency towards 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (kcat/Km = 17.5 s(-1) μM(-1)) and 2,6-dimethoxyphenol (kcat/Km = 16.1 s(-1) μM(-1)) than other reported laccases. The standard redox potential of the T1 site of the enzyme was found to be 772 mV. The highest catalytic efficiency of the yeast recombinant laccase, YlLac, makes it a good candidate for industrial applications: it removes phenolic compounds in acid-pretreated woody biomass (Populus balsamifera) and enhanced saccharification.

DOI: 10.1371/journal.pone.0120156
PubMed: 25781945
PubMed Central: PMC4363317

Affiliations:

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

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Le document en format XML

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<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (genetics)</term>
<term>Hydrolysis (MeSH)</term>
<term>Laccase (chemistry)</term>
<term>Laccase (genetics)</term>
<term>Pichia (genetics)</term>
<term>Pichia (metabolism)</term>
<term>Populus (chemistry)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Wood (chemistry)</term>
<term>Yarrowia (enzymology)</term>
<term>Yarrowia (genetics)</term>
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<term>Bois (composition chimique)</term>
<term>Hydrolyse (MeSH)</term>
<term>Laccase (composition chimique)</term>
<term>Laccase (génétique)</term>
<term>Pichia (génétique)</term>
<term>Pichia (métabolisme)</term>
<term>Populus (composition chimique)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (génétique)</term>
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<term>Protéines recombinantes (génétique)</term>
<term>Yarrowia (enzymologie)</term>
<term>Yarrowia (génétique)</term>
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<term>Laccase</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term>
<term>Laccase</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Populus</term>
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<term>Laccase</term>
<term>Populus</term>
<term>Protéines fongiques</term>
<term>Protéines recombinantes</term>
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<front><div type="abstract" xml:lang="en">A modified thermal asymmetric interlaced polymerase chain reaction was performed to obtain the first yeast laccase gene (YlLac) from the isolated yeast Yarrowia lipolytica. The 1557-bp full-length cDNA of YlLac encoded a mature laccase protein containing 519 amino acids preceded by a signal peptide of 19 amino acids, and the YlLac gene was expressed in the yeast Pichia pastoris. YlLac is a monomeric glycoprotein with a molecular mass of ~55 kDa as determined by polyacrylamide-gel electrophoresis. It showed a higher catalytic efficiency towards 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (kcat/Km = 17.5 s(-1) μM(-1)) and 2,6-dimethoxyphenol (kcat/Km = 16.1 s(-1) μM(-1)) than other reported laccases. The standard redox potential of the T1 site of the enzyme was found to be 772 mV. The highest catalytic efficiency of the yeast recombinant laccase, YlLac, makes it a good candidate for industrial applications: it removes phenolic compounds in acid-pretreated woody biomass (Populus balsamifera) and enhanced saccharification.</div>
</front>
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<Abstract><AbstractText>A modified thermal asymmetric interlaced polymerase chain reaction was performed to obtain the first yeast laccase gene (YlLac) from the isolated yeast Yarrowia lipolytica. The 1557-bp full-length cDNA of YlLac encoded a mature laccase protein containing 519 amino acids preceded by a signal peptide of 19 amino acids, and the YlLac gene was expressed in the yeast Pichia pastoris. YlLac is a monomeric glycoprotein with a molecular mass of ~55 kDa as determined by polyacrylamide-gel electrophoresis. It showed a higher catalytic efficiency towards 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (kcat/Km = 17.5 s(-1) μM(-1)) and 2,6-dimethoxyphenol (kcat/Km = 16.1 s(-1) μM(-1)) than other reported laccases. The standard redox potential of the T1 site of the enzyme was found to be 772 mV. The highest catalytic efficiency of the yeast recombinant laccase, YlLac, makes it a good candidate for industrial applications: it removes phenolic compounds in acid-pretreated woody biomass (Populus balsamifera) and enhanced saccharification.</AbstractText>
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A highly efficient recombinant laccase from the yeast Yarrowia lipolytica and its application in the hydrolysis of biomass.

A highly efficient recombinant laccase from the yeast Yarrowia lipolytica and its application in the hydrolysis of biomass.

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