If someone were to ask you to unboil a boiled egg you would think that such a process is impossible, however turning a boiled egg back to its original liquid form is in fact possible. In this article we will be finding a way to unboil an egg and even try to cook an egg with no heat.
Understanding the concept
Egg whites and egg yolks are made up of proteins and proteins are basically long molecules made of amino acids, now these proteins are not a long and stretched out when placed in water they tend to fold up in structures that resemble huge clumps. A raw egg is liquid and this causes all the proteins to just slide past each other however, when you heat up an egg the proteins vibrate a little, and due the constant vibration the proteins are unable to stay together in clumps and due to the heat, the molecules start to stretch out and begin to unravel, this is called denaturing. So, when the proteins denature, they all get tangled out with one another and this prevents them to slide past each other making them all move together therefor when an egg is cooked, they all become one giant solid chunk.
So, if we want to turn the cooked solid egg into raw liquid egg, we will have to find a way to untangle all the proteins.
Well fortunately there is a chemical that can help us with the untangling, this chemical is called Urea. Urea in a chemical that can make the proteins unstick. For this step we will have to dissolve a bunch of Urea in water, we then have an 8-molar solution of Urea.
Next, we need to finely grind a cooked end, which will then be submerged into the Urea solution. This process will dissolve the egg white, this means that each protein will be pulled apart which will render them separated, a cool fact you’ll learn while conducting this experiment is that protein folding is reversible, once a protein is denatured and then separated when they go back into water they will return to their original shape. In this way the egg will return back to their protein structure. You can add a little phosphorous buffer to it so that the solution can maintain a correct neutral ph.
Once you have dissolved the eggs you will realize that the proteins are still for the most part denatured, therefore, they are still in long chains and not coiled into their original shape, this is because the Urea is keeping them apart. To tackle this, we will need to dilute the Urea.
To dilute the Urea, we will need to take our concentrated egg white solution and some buffered water. We will need to pour the egg white solution into the buffered water. This should be diluted enough where the proteins have separated from each other and spontaneously fold back together. To understand this process better, before the solution was diluted the proteins where just strings floating, with the Urea holding them apart however after they were diluted the Urea is not holding them apart anymore and they have an appropriate amount of water around them, that they start to fold back into clumps. The solution we get from this process is the same as that if would drop a little raw egg white into water. Now that we have understood how to unboil an egg we can try to cook with without any heat.
As mentioned earlier when an egg is heater the proteins unravel and stretch out, this same process can be acquired without heat being involved. To do this we need to put it into a basic solution, the basic solution contains a ton of ions in the water that will pull the proteins apart, stretching it out and denaturing it.
For this you will need some raw egg yolk and a concentrated solution of potassium hydroxide. Pour the egg yolk into the solution, this will solidify the egg yolk, this will give you a cooked egg yolk. If you were to pour the same egg yolk into plain water the yolk would just disperse around and not clump together but the egg yolk in the solution solidifies and stays together in one big clump, with all the stretched-out strings are sticking together.
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