Uncooking Eggs

  • ChemPubSoc Europe Logo
  • Author: ChemViews
  • Published Date: 01 February 2015
  • Source / Publisher: ChemBioChem/Wiley-VCH
  • Copyright: Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
thumbnail image: Uncooking Eggs

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Overexpressed genetically modified proteins are used for a multitude of industrial, pharmaceutical, and agricultural applications. Insoluble and misfolded proteins are a common problem during the production. Efficiently recovering the correctly folded form is a considerable challenge.


Gregory A. Weiss and co-workers, University of California, Irvine, CA, USA, have sucessfully refolded lysozyme from boiled hen egg whites, demonstrating the efficiency of their method of protein recovery. The researchers use shear stress within thin fluid films in a 'vortex fluid device', a rapidly spinning glass tube. The team recovered active lysozyme from previously cooked and thus denatured hen egg whites, as demonstrated by an activity assay, after spinning times of only 5 minutes.


Until now, valuable proteins have to be produced in optimized mammalian cell lines, where misfolding is not a common issue, or recovered by laborious processing of aggregated protein after expression in yeast or Escherichia coli. Compared to overnight dialysis, conventionally used for the latter, the new method is remarkably fast. This approach could dramatically reduce costs for cancer treatments, food production and other segments of the biotechnology industry.


 

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