SCIENCE : DISCOVERED HOW TO UNBOIL AN EGG !!

Can you unboil an egg?

No, it seems impossible, but UC 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

Eggs are  protein rich food; around 12% of the egg white is protein and the yolk is about 16%. Proteins are made up of chains of building blocks called amino acids which are folded and arranged in a very specific way, and it is this shape, among other characteristics, which bestows the protein its properties.

 When proteins are subjected to changes in pH or temperature, the bonds holding them together in a particular conformation are disrupted, causing the protein to unravel and tangle. This process is known as denaturation and is the reason that egg whites go from clear to white when cooked.

Denaturation presents scientists working in the lab with an issue, since it means that certain valuable proteins can’t be recycled after use. Furthermore, some proteins have a tendency to misfold shortly after they have formed, meaning they can’t be used at all.

“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,” says GREGORY WEISS, professor of chemistry and molecular biology and biochemistry at the University of California Irvine. “In our paper, we describe a device for pulling apart tangled proteins and allowing them to refold.”

Weiss and his colleagues started with an egg white that had been boiled for 20 minutes at 194 degrees Fahrenheit (90 degrees Celsius), until its proteins became tangled clumps. Then they added a substance that ate away at the egg white, effectively liquefying it. Next, they used a machine called a vortex fluid device, designed by Weiss' colleagues at Flinders University in Australia, which used the shearing forces  in thin, microfluidic films to shape the egg white proteins back into their untangled form.

older methods are expensive and time-consuming: The equivalent of dialysis at the molecular level must be done for about four days. "The new process takes minutes," Weiss noted. "It speeds things up by a factor of thousands."
This method … could transform industrial and research production of proteins," the researchers write in ChemBioChem.

For example, 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.