The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures

Andrea Vera, Nuria González-Montalbán, Anna Arís, Antonio Villaverde

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164 Citations (Scopus)


Protein aggregation is a major bottleneck during the bacterial production of recombinant proteins. In general, the induction of gene expression at sub-optimal growth temperatures improves the solubility of aggregation-prone polypeptides and minimizes inclusion body (IB) formation. However, the effect of low temperatures on the quality of the recombinant protein, especially within the insoluble cell fraction, has been hardly ever explored. In this work, we have examined the conformational status of a recombinant GFP protein when produced in Escherichia coli below 37°C. As expected, the fraction of aggregated protein largely decreased at lower temperatures, while the conformational quality of both soluble and aggregated GFP, as reflected by its specific fluorescence emission, progressively improved. This observation indicates mat physicochemical conditions governing protein folding affect concurrently the quality of the soluble and the aggregated forms of a misfolding-prone protein, and that protein misfolding and aggregation are clearly not coincident events. © 2006 Wiley Periodicals, Inc.
Original languageEnglish
Pages (from-to)1101-1106
JournalBiotechnology and Bioengineering
Issue number6
Publication statusPublished - 15 Apr 2007


  • ATR
  • E. coli
  • GFP
  • Inclusion bodies
  • Protein aggregation
  • Protein quality


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