Consider this one of the fundamental truths as I was growing up and taking a number of courses in basic biology (and later, microbiology and chemistry): once you boil an egg, there is no way to unboil that egg. Proteins denature once subjected to heat, and do not re-fold back to their original shape/structure.
Turns out, based on most recent research, that may not necessarily be the case: According to findings published in the journal ChemBioChem,
University of California Irvine and Australian chemists have figured out how to unboil egg whites – an innovation that could dramatically reduce costs for cancer treatments, food production and other segments of the $160 billion global biotechnology industry.
To re-create a clear protein known as lysozyme once an egg has been boiled, he and his colleagues add a urea substance that chews away at the whites, liquefying the solid material. That’s half the process; at the molecular level, protein bits are still balled up into unusable masses. The scientists then employ a vortex fluid device, a high-powered machine designed by Professor Colin Raston’s laboratory at South Australia’s Flinders University. Shear stress within thin, microfluidic films is applied to those tiny pieces, forcing them back into untangled, proper form.
In a paper titled “Shear-Stress-Mediated Refolding of Proteins from Aggregates and Inclusion Bodies,” this is the abstract:
Recombinant protein overexpression of large proteins in bacteria often results in insoluble and misfolded proteins directed to inclusion bodies. We report the application of shear stress in micrometer-wide, thin fluid films to refold boiled hen egg white lysozyme, recombinant hen egg white lysozyme, and recombinant caveolin-1. Furthermore, the approach allowed refolding of a much larger protein, cAMP-dependent protein kinase A (PKA). The reported methods require only minutes, which is more than 100 times faster than conventional overnight dialysis. This rapid refolding technique could significantly shorten times, lower costs, and reduce waste streams associated with protein expression for a wide range of industrial and research applications.
Obviously, this is tremendous news that will seek other labs trying to replicate the study.