You did it again. It’s Sunday morning, you have a massive hangover and now you have a boiled egg, by accident. “Damnnit, I meant to fry that!”, you proclaim as you proceed to peel off the shell anyway.
“I don’t even like boiled eggs!”, you mumble while continuing to salt it. Shaking your head in defeat, you think to yourself, “Man, they really need a way to unboil an egg.”

Well, your’e in luck! Researchers from the University of California Irvine claim to have unboiled an egg in a recent paper published by ChemBioChem. Except you’re not really in luck, because that’s not entirely true. At the very least, they don’t even have the before and after pictures to prove it!

Alright, so here’s what we got. Essentially, a protein is a long chain of amino acids that is folded into a unique conformation. When you boil an egg, the proteins within it lose that unique conformation and become “mis-folded”, resulting in a delicious and nutritious, solidified breakfast. What the researchers at UC Irvine actually did was take one of the proteins (lysozyme) found in egg whites that becomes mis-folded upon boiling, and “reconstruct” (refold) it using a series of simple, rapid steps. They were able to do this using the protein in a purified form, as well as when mixed in with the parent egg whites. And although they showed that they could do this for two other proteins found in egg whites, they did not take a hard-boiled egg and revert it back to its liquid ancestor. So in the end, we still can’t truly unboil an egg.

What the authors hope to do with this method is use it as an easier way to increase protein yields from cell lines. In other words, scientists often use cells, such as yeast and E. coli, as factories to produce large quantities of a protein of interest. However, when you try to extract the protein product, you lose a lot of it on the way. In a sense, the authors hope to use the method from this study to help decrease those losses.