Science & Technology

Unboiling an Egg

Note: This article is hosted here for archival purposes only. It does not necessarily represent the values of the Iron Warrior or Waterloo Engineering Society in the present day.

Everybody hears it as an example in thermodynamics: “You can’t unbreak a glass. You can’t unboil an egg.”

Now, that example has been proven wrong.

Eggs are full of proteins, which are complex molecules that need to be folded in a particular way in order to work. Heat, changes in pH, and other stresses can change the shape of a protein, rendering it unable to  perform its biological task. This is called “denaturing” the protein. In the case of eggs, it makes them delicious. In the case of proteins used in cancer research, it makes them useless.

Professor Gregory Weiss of the  University of California, Irvine had this problem. However, when he visited Flinders University in Australia and saw that they had a powerful vortex fluid device, he had an idea.

The vortex device generates strong forces that can pull a protein apart – not into pieces, but more like an elastic. Weiss boiled an egg until it was extremely hard, dissolved the whites in a urea solution, and vortexed the mixture.

What came out was, for all intents and purposes, egg white. The enzymes were able to regain about 85% of their effectiveness, although the urea guaranteed that they wouldn’t taste very good.

For Weiss, this is only a proof of concept. The process might be very valuable in the future for analyzing cancer-related proteins. Ultimately, this process could save lives.

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