Induction optimization and scale-up of the fermentative process for the p-41 protein expressed in Escherichia coli

Abstract

A representative region of the gp41 transmembrane protein from the Human Immunodeficiency Virus (HIV) was expressed in Escherichia coli under control of the tryptophan promoter. Upon analysis of the influence of induction conditions on the production of the p-41 protein, it was noticed that while the expression levels were independent from the amount of the inducer at concentrations higher than 20 μg/mL of 3-β indoleacrylic acid, both the expression levels and the production showed a marked dependence on the concentration of tryptophan, used as a corepressor. A fermentative process for production of the p-41 protein was established, based on derepression of the tryptophan promoter by the addition of 10 μg/mL of tryptophan to the culture medium. This process was scaled-up to 200 L, obtaining high levels of expression (25%) and production (321 mg/L) of the p-41 recombinant protein.

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Cite this paper

@inproceedings{Narciandi2005InductionOA, title={Induction optimization and scale-up of the fermentative process for the p-41 protein expressed in Escherichia coli}, author={Ram{\'o}n E Narciandi and Jos{\'e} Motolongo and Luis J. Dominguez Perez and Ra{\'u}l D{\'i}az}, year={2005} }