High-level heterologous expression of active Chaetomium thermophilum FDH in Pichia pastoris.


Journal

Enzyme and microbial technology
ISSN: 1879-0909
Titre abrégé: Enzyme Microb Technol
Pays: United States
ID NLM: 8003761

Informations de publication

Date de publication:
Jun 2020
Historique:
received: 19 12 2019
revised: 14 02 2020
accepted: 09 03 2020
entrez: 20 5 2020
pubmed: 20 5 2020
medline: 1 12 2020
Statut: ppublish

Résumé

Nowadays, the use of formate dehydrogenase (FDH, EC 1.17.1.9) is well established as a means of NADH regeneration from NAD

Identifiants

pubmed: 32423672
pii: S0141-0229(20)30045-4
doi: 10.1016/j.enzmictec.2020.109552
pii:
doi:

Substances chimiques

Amino Acids 0
Culture Media 0
casamino acids 0
Formate Dehydrogenases EC 1.17.1.9

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

109552

Informations de copyright

Copyright © 2020 Elsevier Inc. All rights reserved.

Auteurs

Zeynep Efsun Duman (ZE)

Department of Bioengineering, Gebze Technical University, 41400, Gebze, Kocaeli, Turkey; Enzyme Consultancy and Identification Center (ETDAM), Gebze Technical University, 41400, Gebze, Kocaeli, Turkey.

Bedri Burak Duraksoy (BB)

Department of Chemistry, Gebze Technical University, 41400, Gebze, Kocaeli, Turkey; Enzyme Consultancy and Identification Center (ETDAM), Gebze Technical University, 41400, Gebze, Kocaeli, Turkey.

Fatih Aktaş (F)

Department of Environmental Engineering, Düzce University, 81620, Düzce, Turkey.

John M Woodley (JM)

Department of Chemical and Biochemical Engineering, Technical University of Denmark, DK-2800 Kgs, Lyngby, Denmark. Electronic address: jw@kt.dtu.dk.

Barış Binay (B)

Department of Bioengineering, Gebze Technical University, 41400, Gebze, Kocaeli, Turkey; Enzyme Consultancy and Identification Center (ETDAM), Gebze Technical University, 41400, Gebze, Kocaeli, Turkey. Electronic address: binay@gtu.edu.tr.

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Classifications MeSH