Influencia de la fuente de carbono sobre la expresión de proteínas AOX1-reguladas en Pichia pastoris

• Poutou Piñales BQ MSC, Raúl Alberto ^[2] ; Quevedo MSC, Balkys E. ; Córdoba MSC, Henrry A. ^[1] ; Sáenz MSC, Homero ; Barrera BQ PhD, Luis A. ^[2]
  1. [1] Pontífica Universidad Javeriana

     Pontífica Universidad Javeriana

     Colombia

     
  2. [2] Instituto de Errores Innatos del Metabolismo
• Localización: NOVA, ISSN-e 2462-9448, ISSN 1794-2470, Vol. 3, Nº. 3, 2005, págs. 75-87
• Idioma: español
• DOI: 10.22490/24629448.21
• Títulos paralelos:
  • Influence of Carbon Source Over the Expression Of1regulated Proteins in
• Enlaces
  • Texto completo
• Resumen
  • español

    La levadura Pichia pastoris constituye un excelente modelo para la expresión de proteínas heterólogas, lo que se refleja en el gran número de proteínas que han sido obtenidas en este modelo biológico, bajo el control del promotor AOX1. Esto implica que el número de peroxisomas y la enzima alcohol oxidasa es regulada como respuesta a la inducción por metabolitos como el metanol, el glicerol, el etanol, el acetato y vías metabólica como la b-oxidación. En esta revisión, se discuten aspectos relacionados con el metabolismo de estos compuestos y su posible influencia en la producción de proteínas recombinantes, específicamente la Iduronato 2- sulfato sulfatasa humana (IDSh).

  • English

    Influence of carbon source over the expression of AOX1-regulated proteins in Pichia pastoris: The Pichia pastoris yeast is an excellent model for the expression of heterologous protein, thus could be deduce from the greate number of proteins that has been obtain in this biological model under the control of AOX1 promoter. This means that peroxisomes number and the enzyme alcohol oxidase are regulate as response to the induction of different metabolites such as methanol, glycerol, ethanol, acetate and metabolic pathways like the b- oxidation. In this review, aspects related with the metabolism of this compounds and its possible influence in the production of recombinant proteins are discuss, specifically the human Iduronate 2-sulfate sulfatase (hIDS).

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