Unboiling an egg is like putting the paste back into its tube, it’s impossible, but not really. I mean, it is theoretically possible. If boiling is just disordering a configuration of molecules by thermal means, couldn’t one reorder this configuration by some other means? However, to describe the reversal as “arduous” would be an understatement.
That being said, scientists have now found a quick way to restore the original configuration and therefore unboil an egg, sort of. They have managed to reverse the effects of thermal energy with mechanical energy.
If you think this is the most fatuous of scientific endeavors and doesn’t deserve to be a headline (unless from The Onion), you should know that it does have some serious implications on microbiology and cancer research. Cancer researchers predict that the technology could save as much as $160 billion of the money that pharmaceutical industries spend on fighting cancer. $160 billion.
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The Boiled Egg
An egg is basically just a mixture of proteins suspended in water. The proteins float like cereal in milk, like clumps of inextricably entangled threads separated by water. However, when an egg is boiled, the heat will untangle these threads, such that the egg is no longer cereal-floating-in-milk, but rather a large serving of spaghetti. Soon, the liberated threads, like slithering vines, cling to each other and coalesce to form a rigid solid. The result is a pudgy, hard-boiled egg.
To unboil this boiled egg, we must therefore separate the protein threads and re-tangle them back into clumps, as they existed in the egg’s unboiled composition. The order violently disturbed by thermal energy can be restored with the diligent use of mechanical energy.
The Unboiled Egg
If the pungency of eggs weren’t enough, the process requires the proteins to be dissolved in urea, the primary ingredient in urine. The urea acts as a lubricant that facilitates the movement and therefore the eventual separation and reorientation of the threads. The solution is then fed to a Vortex Fluid Device (VFD), an emergent technology that essentially comprises a tube rotating at tremendous velocities. A VFD rotates the protein-urea solution at a vertiginous velocity of 5,000 rpm!
Now, because centripetal force is proportional to radius, the fluid at the edge of the vessel experiences a greater force than the fluid closer to the center. The relative forces act as shearing stresses, meaning that one component is pushed in one direction, while the other component is pushed in another direction. Separation of the threads is achieved as they are gently pulled apart. The threads, however, snap back as soon as they are stretched, occasionally into their natural, clumped shapes!
It would be quixotically ambitious to expect that an actual hard-boiled egg could be successfully unboiled. Gregory Weiss, the professor of molecular biology and biochemistry at the University of California, Irvine, who achieved this feat with his colleagues, did not technically unboil a hard-boiled egg, but the white completely liquified in water and urea after the egg was boiled for 20 minutes at 90ᵒC. This is because the unfolding of proteins can only be achieved if the solution is spread throughout the VFD’s chamber.
The takeaway here is that VFD can unfold and refold a variety of proteins in only a few minutes, something which previously took several days. The development of indispensable protein-based medicines is impaired by the frustrating tendency of proteins to “misfold”. Biochemists toil for hours and spend billions of dollars on intricate tools to untangle and refold them into a desirable shape. However, VFD technology will enhance the efficiency of this tinkering by a thousand times! As Weiss remarked, “I can’t predict how much money it will save, but I can [predict] this will save a ton of time, and time is money.”
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