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2018, Número 1

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Rev Educ Bioquimica 2018; 37 (1)


Aspectos metodológicos de la expresión de proteínas recombinantes en Escherichia coli

González A, Fillat MF

Idioma: Español
Referencias bibliográficas: 61
Paginas: 14-27
Archivo PDF: 345.54 Kb.


RESUMEN

Cantidades significativas de proteínas puras, solubles y biológicamente activas son requeridas de modo creciente tanto en proyectos de investigación como para su empleo con fines terapéuticos, diagnósticos o industriales. La purificación de proteínas a partir de sus fuentes naturales no logra suplir en la mayoría de los casos los requerimientos de cantidad, calidad, facilidad de aislamiento o factibilidad económica del proceso. El desarrollo de la tecnología del ADN recombinante desde mediados de la década de los 70 del pasado siglo marcó el comienzo de la era moderna de la biotecnología. Con los conocimientos actuales en genómica, proteómica y bioinformática, el número de proteínas producidas por vía recombinante se ha incrementado exponencialmente. Dado su rápido crecimiento y altos rendimientos de biomasa en medios relativamente económicos, el amplio conocimiento sobre su fisiología y genética, así como su elevada capacidad de producción de proteínas heterólogas, la enterobacteria Escherichia coli continúa siendo el sistema de elección para la expresión recombinante, tanto a escala de laboratorio como en la industria. En el presente trabajo revisamos los aspectos metodológicos más importantes a tener en cuenta para garantizar adecuados niveles de expresión de proteínas recombinantes biológicamente activas, empleando a E. coli como organismo hospedero.


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