Chemists learn how to unboil eggs — and use the...
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Jan 29, 2015  |  Vote 0    0

Chemists learn how to unboil eggs — and use the process in cancer research

Boiling treats the protein in egg whites “gently,” making it possible to undo. That could have applications in cancer research

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Scientists say they’ve figured out how to unboil an egg, and that this is a very good thing for cancer research and food production.

“We’re going to be using (the same process) to produce cancer-associated proteins, which drive cancer cells to divide and form tumors,” Gregory Weiss, a professor of chemistry and molecular biology and biochemistry at the University of California, Irvine, said in an email interview.

This means harnessing the ability to quickly restore proteins, which would be invaluable in fighting cancer.

“Such proteins are typically impossible to produce,” Weiss said, adding that when they come out of the bacteria cells used in the lab, “they form sticky, tangled protein masses that look like boiled egg whites.”

If you understood that and want to get more technical, you can read the findings outlined in the international journal for chemists ChemBioChem under the title, “Shear-Stress Mediated Refolding of Proteins from Aggregates and Inclusion Bodies.”

Weiss said the research was hatched when he was visiting the laboratory of Prof. Colin Raston at South Australia’s Flinders University. Raston, who holds a PhD in chemistry, specializes in clean technology.

“I realized that a device he had invented to do organic synthesis might be perfect for the problems my lab (and many other labs) were having with gummy proteins appearing after production in standard bacteria cells,” Weiss said.

“After it started working on cancer-associated proteins, I thought about the craziest experiment possible to demonstrate its power. Unscrambling an egg. Hmm. Won’t work. OK, how about unboiling?”

“We were surprised to find that boiling is pretty gentle on eggs,” Weiss said. “The protein connectivity and bonding remains unchanged by boiling, which is why we can reverse the unfolding of the protein lysozyme in boiled egg whites. Most cooking involved chemical transformations, which wouldn’t be so easy to reverse.”

Weiss said the process involves “nasty-tasting urea,” meaning.it’s unlikely to have an application in the kitchen.

“Seriously, it would be tough to make this work for culinary applications,” Weiss said.

The research also promises dramatically lower costs for varied segments of the biotechnology industry, which UC Irvine estimates is worth some $160 billion globally.

“We need to scale this up big-time to make it viable at the industrial scale,” Weiss said.

Toronto Star

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