Let's unboil a boiled egg..

In working with the denaturation of proteins this week, I thought this article would be relevant.

When an egg is boiled the heat causes the proteins to denture and unfold. The proteins then create new bonds with other proteins causing it to get hard (a boiled egg). Now, have you ever wondered if there was a way to unboil an egg? Some chemists from the University of California -Irvine, have discovered a way to unboil boiled eggs. How is this possible? According to the article, all one needs is a way of denaturing the proteins and letting them refold. Sounds easy and simple, but how does one tell a protein to refold into a desired manner or in this case, to become liquid again? Well, the current method for refolding proteins is a type of dialysis that is done at the molecular level for several days. It seems to be an expensive and long process that not always yields good results. With this new method, however, it can now be accomplished in a matter of minutes (and quite cheaply).

 The chemists introduce a urea substance that dissolves the hard-boiled egg back into its liquid form. Apparently, the addition of urea helps to re-activate the activity of lysozyme which in turn creates a sort of cascade of other proteins being activated as well. Finally, the chemists add some “shear stress” using a “vortex fluid device” to finish unfolding any proteins that are still “folded”.

This method can be beneficial for research, pharmaceutical companies, or even farmers because sometimes proteins that are useful no longer work due to folding incorrectly. This can cause setbacks, or waste of time and money. Therefore, being able to get proteins back to their original state and “re-use” them is exciting.  

http://www.sciencedaily.com/releases/2015/01/150126095911.htm