That's at least according to Gregory Weiss, a biochemist at the University of California, Irvine, who co-authored a paper describing the process and its significance. It was published today in the journal ChemBioChem.
"Yes, we have invented a way to unboil a hen egg," he said in a statement. However, "it's not so much that we're interested in processing the eggs; that's just demonstrating how powerful this process is."
"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," Weiss added. "The new process takes minutes. It speeds things up by a factor of thousands."
To really understand what the researcher is talking about, you first must understand how exactly an egg hard-boils.
It's strange to say, but chemists actually find eggs very exciting. That's because they are made up of a great deal of orderly and fluid protein structures. On average, nearly 12 percent of egg whites are protein, and the yolk is up to 16 percent protein. Therefore, if you alter the form of these proteins, you can impact the structure of an entire egg. (Scroll to read on...)
When you apply heat to an egg, you are putting it through a process called "denaturation." This disrupts some of the protein bonds that hold molecular shapes in order. Without these bonds, fractured proteins can suddenly clump and tangle.
In this way, you can almost think of egg whites like a ribbon or streamer. When flat and smooth, a ribbon can flutter through the air with fluidity. However, once it's marred by bends, kinks, and knots, its can no longer move as freely.
In the case of egg whites, once their proteins have tangled, they stiffen, becoming the opaque solids that make our breakfasts and salad toppings.
However, denaturation doesn't just occur on the stovetop. The production of cancer antibodies, for instance, often results in the misfolding of protein structures. The result is that "gummy" goo that Weiss mentioned earlier. To avoid this, pharmaceutical companies often choose to create antibodies in the ovary cells of hamsters - an environment that is unlikely to cause a misfold. Unfortunately, this process is extremely lab intensive, and heavily raises the cost of cancer treatments.
Weiss and his colleagues argue that it would be simpler and more cost-effective to merely reverse instances of denaturation instead of taking the pains to ensure it doesn't occur in the first place. That, of course, is where 'unboiling' an egg comes in.
"In our paper, we describe a device for pulling apart tangled proteins and allowing them to refold," the team reported. "We start with egg whites boiled for 20 minutes at 90 degrees Celsius [194 Fahrenheit] and return a key protein in the egg to working order."
According to the study, they accomplished this by first applying a urea substance that forces solid materials into a temporary liquefied state. Even with this done, much of the whites still contain clumped proteins that are largely unusable. That's when Weiss and his team put the boiled whites in a "vortex fluid device" that untangles the proteins using physical stress. Microfluidic films then help the rattled proteins slide back into their untangled, proper forms.
"This method," the researchers write, "could transform industrial and research production of proteins," simplifying processes, saving time, and cutting costs across numerous industries.
And if you just really didn't want your egg boiled, well, they can fix that too.
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