How to “unboil” eggs

Scientists have figured out a way to do something that seems impossible: unboil an egg. But strange as it may sound, the feat doesn't defy basic laws of science.

Boiling an egg may seem like the simplest part of breakfast, but it involves some interesting chemistry. An egg is 90 percent water and ten percent protein, which is what gives egg whites their gloppy appearance. These proteins are in the form of long chains of amino acids tangled and folded in upon themselves like microscopic piles of yarn held together by weak atomic bonds. When the egg is dropped into boiling water, the heat breaks these bonds and the chains start to unravel and break. The chains then bond with other amino acids and capture water inside the new folds, causing the whites to turn white and gelatinous. Cook them too long, and the chains curl in on themselves; forcing the water out and turning the whites hard and rubbery.

Scientists have found a way to unboil an egg – and the discovery could lead to cost reductions in cancer treatments, food production advancements and other areas of research. The process, developed by University of California and Australian chemists, can turn a hard boiled egg white back into liquid form. And while that might seem like just a cool trick, it’s really a fun way to show the revolutionary process the chemists have developed that can ‘untangle’ protein molecules.

The real problem is there are lots of cases of gummy proteins that you spend way too much time scraping off your test tubes, and you want some means of recovering that material. As soon as an egg is boiled, its proteins are tangled together and form a solid mass. But the chemists discovered that adding urea to the egg, the proteins can be untangled. They boil the eggs for 20 minutes at a temperature of 194 degrees F, then add urea one of the main components of urine,to to recreate a clear protein found in the egg called a lysozyme. The urea then “chews” away at the protein, turning the solid into a liquid.

The protein pieces are still “balled up” at this point, so the pieces are placed in a vortex fluid device—a high-powered machine located 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,” 

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.

This method could transform industrial and research production of proteins. Pharmaceutical companies currently create cancer antibodies in expensive hamster ovary cells that do not often misfold proteins. The ability to quickly and cheaply re-form common proteins from yeast or E. coli bacteria could potentially streamline protein manufacturing and make cancer treatments more affordable. Industrial cheese makers, farmers and others who use recombinant proteins could also achieve more bang for their buck.

It may not sound like the most useful of scientific endeavours, but the methods used to turn a hard-boiled egg back into its liquid state could bring major benefits to areas as diverse as cheese-making and cancer research.

-Dixy