Heterologous expression of Phanerochaete chrysosporium cellobiose dehydrogenase in Trichoderma reesei.

Catalytic constants Cellobiose dehydrogenase Cofactor occupancy Glycosylation Lignocellulose depolymerization Phanerochaete chrysosporium Redox potential Trichoderma reesei

Journal

Microbial cell factories
ISSN: 1475-2859
Titre abrégé: Microb Cell Fact
Pays: England
ID NLM: 101139812

Informations de publication

Date de publication:
06 Jan 2021
Historique:
received: 22 09 2020
accepted: 03 12 2020
entrez: 7 1 2021
pubmed: 8 1 2021
medline: 7 9 2021
Statut: epublish

Résumé

Cellobiose dehydrogenase from Phanerochaete chrysosporium (PcCDH) is a key enzyme in lignocellulose depolymerization, biosensors and biofuel cells. For these applications, it should retain important molecular and catalytic properties when recombinantly expressed. While homologous expression is time-consuming and the prokaryote Escherichia coli is not suitable for expression of the two-domain flavocytochrome, the yeast Pichia pastoris is hyperglycosylating the enzyme. Fungal expression hosts like Aspergillus niger and Trichoderma reesei were successfully used to express CDH from the ascomycete Corynascus thermophilus. This study describes the expression of basidiomycetes PcCDH in T. reesei (PcCDH PcCDH Heterologous production of PcCDH

Sections du résumé

BACKGROUND BACKGROUND
Cellobiose dehydrogenase from Phanerochaete chrysosporium (PcCDH) is a key enzyme in lignocellulose depolymerization, biosensors and biofuel cells. For these applications, it should retain important molecular and catalytic properties when recombinantly expressed. While homologous expression is time-consuming and the prokaryote Escherichia coli is not suitable for expression of the two-domain flavocytochrome, the yeast Pichia pastoris is hyperglycosylating the enzyme. Fungal expression hosts like Aspergillus niger and Trichoderma reesei were successfully used to express CDH from the ascomycete Corynascus thermophilus. This study describes the expression of basidiomycetes PcCDH in T. reesei (PcCDH
RESULTS RESULTS
PcCDH
CONCLUSIONS CONCLUSIONS
Heterologous production of PcCDH

Identifiants

pubmed: 33407462
doi: 10.1186/s12934-020-01492-0
pii: 10.1186/s12934-020-01492-0
pmc: PMC7789494
doi:

Substances chimiques

Recombinant Proteins 0
Cellobiose 16462-44-5
Carbohydrate Dehydrogenases EC 1.1.-
cellobiose-quinone oxidoreductase EC 1.1.99.18

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

2

Subventions

Organisme : European Research Council
ID : 726396
Pays : International

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Auteurs

Lena Wohlschlager (L)

Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria.

Florian Csarman (F)

Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria.

Hucheng Chang (H)

Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria.

Elisabeth Fitz (E)

Research Division Biochemical Technology, Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, 1060, Vienna, Austria.

Bernhard Seiboth (B)

Research Division Biochemical Technology, Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, 1060, Vienna, Austria.

Roland Ludwig (R)

Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria. roland.ludwig@boku.ac.at.

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Classifications MeSH