How to De-Boil an Egg

You can't unboil an egg; it's so clear that it's virtually proverbial. It turns out, though, that you can, sort of. Eleanor Nelsen demonstrated how mechanical energy can reverse the effects of thermal energy.

It's nearly a proverb because it's so apparent. An egg cannot be unboiled. It turns out that you kind of can. Mechanical energy can reverse the effects of heat energy on the molecules of the eggs. Water and proteins make up the majority of an egg. The proteins initially fold themselves into complex forms that are held together by flimsy chemical links.

These connections are broken by heat, allowing the proteins to freely unfurl, uncoil, unwind, and wriggle. Denaturing is the name of this procedure. As the heat rises, the newly released proteins collide with one another and begin to establish new links with one another. Eventually, they get so intertwined that they solidify into a solid mass, a cooked egg. Although it may seem so, that entanglement is not permanent.

The principle of microscopic reversibility is a chemical concept that states that anything that occurs, such egg proteins seizing up, can theoretically be reversed if you go back and follow your original steps. The solution is to spin the proteins incredibly quickly because increasing the heat will only further tangle the proteins and decreasing the temperature will only cause them to freeze. I am not joking. This is how it goes.

First, urea, a tiny molecule that functions as a lubricant, is used to dissolve boiled egg whites in water. By coating the long strands of the proteins, urea makes it simpler for them to glide past one another. After that, they quickly spin the solution in a glass tube at 5000 rotations per minute to spread it out into a thin film. Here's the important bit. The solution closest to the wall rotates more quickly than the solution in the center.

The proteins are repeatedly stretched and contracted by the enormous strains produced by the velocity differential, until eventually they snap back into their original shapes and remain there. The egg white has returned to its initial, unboiled state by the time the centrifuge stops spinning.

All types of proteins can be used using this method. Larger, messier proteins may be harder to separate, so researchers attach a plastic bead to one end of the protein to increase tension and induce folding first. Since the solution must spread across a cylindrical chamber, this method of unboiling won't work with an egg that is entire and still in its shell. However, the uses go far beyond uncooking your breakfast.

Many medications are made up of proteins that are very expensive to create, in part because they clump together like cooked egg whites and become tangled aggregates that must be untangled and refolded in order for them to function. This spinning procedure might make it simpler, less expensive, and quicker to refold proteins than current methods, which could speed up the process of developing new drugs for a wider audience.

Before attempting to uncook all of your food, there is one more thing you should bear in mind. Despite the fact that heating alters the way proteins are formed and bonded together, boiling an egg does not actually alter the chemical composition of the protein.

The majority of cooking is more akin to the well-known Maillard process, which causes chemical alterations that transform proteins and sugars into wonderful caramel crunchiness and are much more difficult to reverse. I'm sorry to announce that while you might be able to unboil your egg, you can't unfry it just yet.