Heterologous expression of lignin peroxidase of Phanerochaete chrysosporium in Pichia methanolica.
Identifieur interne : 000876 ( Main/Exploration ); précédent : 000875; suivant : 000877Heterologous expression of lignin peroxidase of Phanerochaete chrysosporium in Pichia methanolica.
Auteurs : Haikuan Wang [République populaire de Chine] ; Fuping Lu ; Yafan Sun ; Lianxiang DuSource :
- Biotechnology letters [ 0141-5492 ] ; 2004.
Descripteurs français
- KwdFr :
- Activation enzymatique (MeSH), Clonage moléculaire (méthodes), Masse moléculaire (MeSH), Peroxidases (biosynthèse), Peroxidases (composition chimique), Peroxidases (génétique), Phanerochaete (enzymologie), Phanerochaete (génétique), Pichia (enzymologie), Pichia (génétique), Protéines recombinantes (biosynthèse), Protéines recombinantes (composition chimique).
- MESH :
- biosynthèse : Peroxidases, Protéines recombinantes.
- composition chimique : Peroxidases, Protéines recombinantes.
- enzymologie : Phanerochaete, Pichia.
- génétique : Peroxidases, Phanerochaete, Pichia.
- méthodes : Clonage moléculaire.
- Activation enzymatique, Masse moléculaire.
English descriptors
- KwdEn :
- Cloning, Molecular (methods), Enzyme Activation (MeSH), Molecular Weight (MeSH), Peroxidases (biosynthesis), Peroxidases (chemistry), Peroxidases (genetics), Phanerochaete (enzymology), Phanerochaete (genetics), Pichia (enzymology), Pichia (genetics), Recombinant Proteins (biosynthesis), Recombinant Proteins (chemistry).
- MESH :
- chemical , biosynthesis : Peroxidases, Recombinant Proteins.
- chemical , chemistry : Peroxidases, Recombinant Proteins.
- chemical , genetics : Peroxidases.
- enzymology : Phanerochaete, Pichia.
- genetics : Phanerochaete, Pichia.
- methods : Cloning, Molecular.
- Enzyme Activation, Molecular Weight.
Abstract
The cDNA encoding for lignin peroxidase of Phanerochaete chrysosporium was expressed in the Pichia methanolica under the control of the alcohol oxidase (AUG1) promoter which was followed by either the lignin peroxidase leader peptide of Phanerochaete chrysosporium or the Saccharomyces cerevisiae alpha-factor signal peptide. Both peptides efficiently directed the secretion of lignin peroxidase from the recombinant yeast cell. The extracellular lignin peroxidase activity in two recombinants was 932 U l(-1) and 1933 U l(-1). The purity of the recombinant product was confirmed by SDS-PAGE.
DOI: 10.1023/B:BILE.0000045654.66689.b4
PubMed: 15604798
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<author><name sortKey="Wang, Haikuan" sort="Wang, Haikuan" uniqKey="Wang H" first="Haikuan" last="Wang">Haikuan Wang</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Food Science and Biology Engineering, Tianjin Science and Technology University, P.R. China.</nlm:affiliation>
<country xml:lang="fr" wicri:curation="lc">République populaire de Chine</country>
<wicri:regionArea>Department of Food Science and Biology Engineering, Tianjin Science and Technology University</wicri:regionArea>
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<author><name sortKey="Lu, Fuping" sort="Lu, Fuping" uniqKey="Lu F" first="Fuping" last="Lu">Fuping Lu</name>
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<author><name sortKey="Sun, Yafan" sort="Sun, Yafan" uniqKey="Sun Y" first="Yafan" last="Sun">Yafan Sun</name>
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<author><name sortKey="Du, Lianxiang" sort="Du, Lianxiang" uniqKey="Du L" first="Lianxiang" last="Du">Lianxiang Du</name>
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<term>Enzyme Activation (MeSH)</term>
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<term>Peroxidases (biosynthesis)</term>
<term>Peroxidases (chemistry)</term>
<term>Peroxidases (genetics)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
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<term>Pichia (genetics)</term>
<term>Recombinant Proteins (biosynthesis)</term>
<term>Recombinant Proteins (chemistry)</term>
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<term>Clonage moléculaire (méthodes)</term>
<term>Masse moléculaire (MeSH)</term>
<term>Peroxidases (biosynthèse)</term>
<term>Peroxidases (composition chimique)</term>
<term>Peroxidases (génétique)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Phanerochaete (génétique)</term>
<term>Pichia (enzymologie)</term>
<term>Pichia (génétique)</term>
<term>Protéines recombinantes (biosynthèse)</term>
<term>Protéines recombinantes (composition chimique)</term>
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<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Peroxidases</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peroxidases</term>
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<front><div type="abstract" xml:lang="en">The cDNA encoding for lignin peroxidase of Phanerochaete chrysosporium was expressed in the Pichia methanolica under the control of the alcohol oxidase (AUG1) promoter which was followed by either the lignin peroxidase leader peptide of Phanerochaete chrysosporium or the Saccharomyces cerevisiae alpha-factor signal peptide. Both peptides efficiently directed the secretion of lignin peroxidase from the recombinant yeast cell. The extracellular lignin peroxidase activity in two recombinants was 932 U l(-1) and 1933 U l(-1). The purity of the recombinant product was confirmed by SDS-PAGE.</div>
</front>
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<Title>Biotechnology letters</Title>
<ISOAbbreviation>Biotechnol Lett</ISOAbbreviation>
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<Abstract><AbstractText>The cDNA encoding for lignin peroxidase of Phanerochaete chrysosporium was expressed in the Pichia methanolica under the control of the alcohol oxidase (AUG1) promoter which was followed by either the lignin peroxidase leader peptide of Phanerochaete chrysosporium or the Saccharomyces cerevisiae alpha-factor signal peptide. Both peptides efficiently directed the secretion of lignin peroxidase from the recombinant yeast cell. The extracellular lignin peroxidase activity in two recombinants was 932 U l(-1) and 1933 U l(-1). The purity of the recombinant product was confirmed by SDS-PAGE.</AbstractText>
</Abstract>
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