Cracked egg. Photo Credit: WashingtonPost.com
Boiled eggs are delicious, I’m pretty sure no one will object to that, but have you ever thought of unboiling eggs? A group of chemists out of UC Irvine and Australia have made this discovery which has the potential to change the biotechnology industry and dramatically reduce the time and cost for production of cancer treatments among other applications!
Now this wasn’t done simply for the sake of unboiling eggs, it was used to demonstrate how powerful this new technique of returning tangled proteins to their original form really is. Proteins are made of chains of amino acids that are folded and arranged in a specific way. Changes in pH and/or temperature disrupt the bonds holding the proteins in their original shape causing it to deform and tangle. So when you cook an egg you are actually tangling proteins which causes them to change from clear to white. The process is known as denaturation and is problematic for scientists who are trying to recycle valuable proteins after use. Previous methods of solving this issue exist but they are time consuming and expensive. This new process, however, gives results in minutes.
Professor Colin Raston’s vortex fluid device. Photo Credit: WashingtonPost.com
In the findings published in ChemBioChem, egg-whites were first boiled for 20 minutes at 90 degrees Celsius (194 deg. F) (plenty of time to tangle the delicious proteins). To revert a protein in the cooked eggs called lysozyme, urea was added to liquefy the solid whites. The resulting substance was then placed in a vortex fluid device which is a high powered machine designed by Professor Colin Raston’s laboratory at South Australia’s Flinders University. This machine applied shear stress to the proteins which encouraged them to untangle and re-fold to their original form.
There is huge potential for this discovery that can streamline protein manufacturing and make cancer treatments more affordable. Think about this next time you’re making omelets. For more information on the findings please visit http://onlinelibrary.wiley.com/doi/10.1002/cbic.201402427/abstract
