Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/190009
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Alcohol dehydrogenase AdhA plays a role in ethanol tolerance in model cyanobacterium Synechocystis sp. PCC 6803 |
Autor: | Vidal, Rebeca CSIC ORCID | Palabras clave: | Stress Redox homeostasis Cyanobacteria Biofuel |
Fecha de publicación: | abr-2017 | Editor: | Springer Nature | Citación: | Applied Microbiology and Biotechnology 101(8): 3473-3482 (2017) | Resumen: | The protein AdhA from the cyanobacterium Synechocystis sp. PCC 6803 (hereafter Synechocystis) has been previously reported to show alcohol dehydrogenase activity towards ethanol and both NAD and NADP. This protein is currently being used in genetically modified strains of Synechocystis capable of synthesizing ethanol showing the highest ethanol productivities. In the present work, mutant strains of Synechocystis lacking AdhA have been constructed and tested for tolerance to ethanol. The lack of AdhA in the wild-type strain reduces survival to externally added ethanol at lethal concentration of 4% (v/v). On the other hand, the lack of AdhA in an ethanologenic strain diminishes tolerance of cells to internally produced ethanol. It is also shown that light-activated heterotrophic growth (LAHG) of the wild-type strain is impaired in the mutant strain lacking AdhA (∆adhA strain). Photoautotrophic, mixotrophic, and photoheterotrophic growth are not affected in the mutant strain. Based on phenotypic characterization of ∆adhA mutants, the possible physiological function of AdhA in Synechocystis is discussed. | Versión del editor: | https://doi.org/10.1007/s00253-017-8138-3 | URI: | http://hdl.handle.net/10261/190009 | DOI: | 10.1007/s00253-017-8138-3 | ISSN: | 0175-7598 | E-ISSN: | 1432-0614 |
Aparece en las colecciones: | (IBVF) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
13
checked on 08-abr-2024
WEB OF SCIENCETM
Citations
10
checked on 29-feb-2024
Page view(s)
187
checked on 22-abr-2024
Download(s)
18
checked on 22-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.