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Analysis of the molecular basis for the non-amylolytic and non-proteolytic nature of Aspergillus vadensis CBS 113365.
Liu, Dujuan; Garrigues, Sandra; Culleton, Helena; McKie, Vincent A; de Vries, Ronald P.
Afiliación
  • Liu D; Fungal Physiology, Westerdijk Fungal Biodiversity Institute & Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands.
  • Garrigues S; Fungal Physiology, Westerdijk Fungal Biodiversity Institute & Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands; Departament of Food Biotechnology, Instituto de Agroquímica y Tecnología de Alimentos (IATA), Consejo Superior de Investigaciones Cientí
  • Culleton H; Fungal Physiology, Westerdijk Fungal Biodiversity Institute & Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands; Megazyme International Ireland, Bray, Co. Wicklow, Ireland.
  • McKie VA; Megazyme International Ireland, Bray, Co. Wicklow, Ireland.
  • de Vries RP; Fungal Physiology, Westerdijk Fungal Biodiversity Institute & Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands. Electronic address: r.devries@wi.knaw.nl.
N Biotechnol ; 82: 25-32, 2024 Sep 25.
Article en En | MEDLINE | ID: mdl-38697469
ABSTRACT
Aspergillus vadensis CBS 113365, a close relative of A. niger, has been suggested as a more favourable alternative for recombinant protein production as it does not acidify the culture medium and produces very low levels of extracellular proteases. The aim of this study was to investigate the underlying cause of the non-amylolytic and non-proteolytic phenotype of A. vadensis CBS 113365. Our results demonstrate that the non-functionality of the amylolytic transcription factor AmyR in A. vadensis CBS 113365 is primarily attributed to the lack of functionality of its gene's promoter sequence. In contrast, a different mechanism is likely causing the lack of PrtT activity, which is the main transcriptional regulator of protease production. The findings presented here not only expand our understanding of the genetic basis behind the distinct characteristics of A. vadensis CBS 113365, but also underscore its potential as a favourable alternative for recombinant protein production.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Aspergillus / Proteínas Fúngicas Idioma: En Revista: N Biotechnol Asunto de la revista: BIOLOGIA MOLECULAR / ENGENHARIA BIOMEDICA Año: 2024 Tipo del documento: Article País de afiliación: Países Bajos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Aspergillus / Proteínas Fúngicas Idioma: En Revista: N Biotechnol Asunto de la revista: BIOLOGIA MOLECULAR / ENGENHARIA BIOMEDICA Año: 2024 Tipo del documento: Article País de afiliación: Países Bajos
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