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A novel bifunctional aldehyde/alcohol dehydrogenase catalyzing reduction of acetyl-CoA to ethanol at temperatures up to 95 °C.
Wang, Qiang; Sha, Chong; Wang, Hongcheng; Ma, Kesen; Wiegle, Juergen; Abomohra, Abd El-Fatah; Shao, Weilan.
Afiliación
  • Wang Q; School of the Environment and Safety Engineering, Biofuels Institute, Jiangsu University, Zhenjiang, 212013, Jiangsu, China.
  • Sha C; School of the Environment and Safety Engineering, Biofuels Institute, Jiangsu University, Zhenjiang, 212013, Jiangsu, China.
  • Wang H; School of the Environment and Safety Engineering, Biofuels Institute, Jiangsu University, Zhenjiang, 212013, Jiangsu, China.
  • Ma K; Department of Biology, University of Waterloo, Waterloo, ON, N2L 3G1, Canada.
  • Wiegle J; Department of Microbiology, University of Georgia, Athens, GA, 30602, USA.
  • Abomohra AE; Department of Environmental Engineering, School of Architecture and Civil Engineering, Chengdu University, Chengdu, 610106, China. abomohra@yahoo.com.
  • Shao W; Botany Department, Faculty of Science, Tanta University, Tanta, 31527, Egypt. abomohra@yahoo.com.
Sci Rep ; 11(1): 1050, 2021 01 13.
Article en En | MEDLINE | ID: mdl-33441766
Hyperthermophilic Thermotoga spp. are excellent candidates for the biosynthesis of cellulosic ethanol producing strains because they can grow optimally at 80 °C with ability to degrade and utilize cellulosic biomass. In T. neapolitana (Tne), a putative iron-containing alcohol dehydrogenase was, for the first time, revealed to be a bifunctional aldehyde/alcohol dehydrogenase (Fe-AAdh) that catalyzed both reactions from acetyl-coenzyme A (ac-CoA) to acetaldehyde (ac-ald), and from ac-ald to ethanol, while the putative aldehyde dehydrogenase (Aldh) exhibited only CoA-independent activity that oxidizes ac-ald to acetic acid. The biochemical properties of Fe-AAdh were characterized, and bioinformatics were analyzed. Fe-AAdh exhibited the highest activities for the reductions of ac-CoA and acetaldehyde at 80-85 °C, pH 7.54, and had a 1-h half-life at about 92 °C. The Fe-AAdh gene is highly conserved in Thermotoga spp., Pyrococcus furiosus and Thermococcus kodakarensis, indicating the existence of a fermentation pathway from ac-CoA to ethanol via acetaldehyde as the intermediate in hyperthermophiles.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Acetilcoenzima A / Aldehído Deshidrogenasa / Thermotoga Idioma: En Revista: Sci Rep Año: 2021 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Acetilcoenzima A / Aldehído Deshidrogenasa / Thermotoga Idioma: En Revista: Sci Rep Año: 2021 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido