PhanerochaeteV1, Main, Exploration, bibRecord, 000A67

Studies on the production of fungal peroxidases in Aspergillus niger.

Identifieur interne : 000A67 ( Main/Exploration ); précédent : 000A66; suivant : 000A68

Studies on the production of fungal peroxidases in Aspergillus niger.

Auteurs : A. Conesa [Pays-Bas] ; C A Van Den Hondel ; P J Punt

Source :

Applied and environmental microbiology [ 0099-2240 ] ; 2000.

RBID : pubmed:10877800

Descripteurs français

KwdFr :
- Aspergillus niger (croissance et développement), Aspergillus niger (enzymologie), Aspergillus niger (génétique), Composés du fer II (métabolisme), Hème (métabolisme), Peroxidases (génétique), Peroxidases (isolement et purification), Peroxidases (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Protéines recombinantes (métabolisme), Technique de Northern (MeSH), Technique de Western (MeSH), Transformation génétique (MeSH).
MESH :
- croissance et développement : Aspergillus niger.
- enzymologie : Aspergillus niger, Phanerochaete.
- génétique : Aspergillus niger, Peroxidases, Phanerochaete.
- isolement et purification : Peroxidases.
- métabolisme : Composés du fer II, Hème, Peroxidases, Protéines recombinantes.
- Technique de Northern, Technique de Western, Transformation génétique.

English descriptors

KwdEn :
- Aspergillus niger (enzymology), Aspergillus niger (genetics), Aspergillus niger (growth & development), Blotting, Northern (MeSH), Blotting, Western (MeSH), Ferrous Compounds (metabolism), Heme (metabolism), Peroxidases (genetics), Peroxidases (isolation & purification), Peroxidases (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Recombinant Proteins (metabolism), Transformation, Genetic (MeSH).
MESH :
- chemical , genetics : Peroxidases.
- chemical , isolation & purification : Peroxidases.
- chemical , metabolism : Ferrous Compounds, Heme, Peroxidases, Recombinant Proteins.
- enzymology : Aspergillus niger, Phanerochaete.
- genetics : Aspergillus niger, Phanerochaete.
- growth & development : Aspergillus niger.
- Blotting, Northern, Blotting, Western, Transformation, Genetic.

Abstract

To get insight into the limiting factors existing for the efficient production of fungal peroxidase in filamentous fungi, the expression of the Phanerochaete chrysosporium lignin peroxidase H8 (lipA) and manganese peroxidase (MnP) H4 (mnp1) genes in Aspergillus niger has been studied. For this purpose, a protease-deficient A. niger strain and different expression cassettes have been used. Northern blotting experiments indicated high steady-state mRNA levels for the recombinant genes. Manganese peroxidase was secreted into the culture medium as an active protein. The recombinant protein showed specific activity and a spectrum profile similar to those of the native enzyme, was correctly processed at its N terminus, and had a slightly lower mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Recombinant MnP production could be increased up to 100 mg/liter upon hemoglobin supplementation of the culture medium. Lignin peroxidase was also secreted into the extracellular medium, although the protein was not active, presumably due to incorrect processing of the secreted enzyme. Expression of the lipA and mnp1 genes fused to the A. niger glucoamylase gene did not result in improved production yields.

DOI: 10.1128/aem.66.7.3016-3023.2000
PubMed: 10877800
PubMed Central: PMC92105

Affiliations:

Pays-Bas

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

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Le document en format XML

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<front><div type="abstract" xml:lang="en">To get insight into the limiting factors existing for the efficient production of fungal peroxidase in filamentous fungi, the expression of the Phanerochaete chrysosporium lignin peroxidase H8 (lipA) and manganese peroxidase (MnP) H4 (mnp1) genes in Aspergillus niger has been studied. For this purpose, a protease-deficient A. niger strain and different expression cassettes have been used. Northern blotting experiments indicated high steady-state mRNA levels for the recombinant genes. Manganese peroxidase was secreted into the culture medium as an active protein. The recombinant protein showed specific activity and a spectrum profile similar to those of the native enzyme, was correctly processed at its N terminus, and had a slightly lower mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Recombinant MnP production could be increased up to 100 mg/liter upon hemoglobin supplementation of the culture medium. Lignin peroxidase was also secreted into the extracellular medium, although the protein was not active, presumably due to incorrect processing of the secreted enzyme. Expression of the lipA and mnp1 genes fused to the A. niger glucoamylase gene did not result in improved production yields.</div>
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<Abstract><AbstractText>To get insight into the limiting factors existing for the efficient production of fungal peroxidase in filamentous fungi, the expression of the Phanerochaete chrysosporium lignin peroxidase H8 (lipA) and manganese peroxidase (MnP) H4 (mnp1) genes in Aspergillus niger has been studied. For this purpose, a protease-deficient A. niger strain and different expression cassettes have been used. Northern blotting experiments indicated high steady-state mRNA levels for the recombinant genes. Manganese peroxidase was secreted into the culture medium as an active protein. The recombinant protein showed specific activity and a spectrum profile similar to those of the native enzyme, was correctly processed at its N terminus, and had a slightly lower mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Recombinant MnP production could be increased up to 100 mg/liter upon hemoglobin supplementation of the culture medium. Lignin peroxidase was also secreted into the extracellular medium, although the protein was not active, presumably due to incorrect processing of the secreted enzyme. Expression of the lipA and mnp1 genes fused to the A. niger glucoamylase gene did not result in improved production yields.</AbstractText>
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<tree><noCountry><name sortKey="Punt, P J" sort="Punt, P J" uniqKey="Punt P" first="P J" last="Punt">P J Punt</name>
<name sortKey="Van Den Hondel, C A" sort="Van Den Hondel, C A" uniqKey="Van Den Hondel C" first="C A" last="Van Den Hondel">C A Van Den Hondel</name>
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<country name="Pays-Bas"><noRegion><name sortKey="Conesa, A" sort="Conesa, A" uniqKey="Conesa A" first="A" last="Conesa">A. Conesa</name>
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EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000A67 | SxmlIndent | more

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Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    PhanerochaeteV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:10877800
   |texte=   Studies on the production of fungal peroxidases in Aspergillus niger.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:10877800" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a PhanerochaeteV1

This area was generated with Dilib version V0.6.37.
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	Serveur d'exploration sur le phanerochaete
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Serveur d'exploration sur le phanerochaete

Studies on the production of fungal peroxidases in Aspergillus niger.

Studies on the production of fungal peroxidases in Aspergillus niger.

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Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki