I just boiled some eggs for lunch - making an egg salad sandwich. And honestly, I can't imagine any reason on earth why I'd need to unboil them.
But apparently, chemists at the University of California, Irvine, do. They've developed a technique for pulling apart egg white proteins that become entwined when the egg is boiled and hardens.
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That technique could reduce costs for both cancer treatments and food production, which require certain proteins in their liquid, non-tangled form.
"The real problem is 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," said Gregory Weiss, UCI professor of chemistry and molecular biology and biochemistry.
To test their new process, Weiss and his colleagues boiled egg whites for 20 minutes at 194 degrees Fahrenheit. Next, they added urea, which begins to chemically untangle the protein, known as lysozyme.
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Lastly, they put the solution in a vortex fluid device, a high-powered machine designed by Colin Raston's laboratory at South Australia's Flinders University.
The urea, in addition to the stresses inside the vortex machine, returned the hardened egg whites to their liquid state.
Having the ability to quickly and cheaply re-form proteins could help streamline protein manufacturing used to make cancer antibodies. It could also be adopted by industrial cheese makers, who use recombinant proteins in their manufacturing process.
I'll stick with egg salad, thanks.