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    By Elinor Higgins Eye on Science, Features, News and FeaturesFebruary 4, 2015

    You can’t unscramble an egg, but can you unboil it?

    It turns out that you can unboil an egg. Based on a method, developed at the University of California, Irvine, one can reverse the effect boiling has on egg whites. After boiling the eggs for 20 minutes to reach a state more solid than an average hard-boiled egg, researchers began experimenting with possible ways to renature the proteins in egg whites to their original state.

    Using a chemical solution that includes urea, an organic compound found in urine, the researchers dissolved the solidified whites. The vortex machine was used to spin the solution until the egg white proteins stretched out and returned to their original form. One of the researchers, Professor Gregory Weiss, described the proteins as rubber bands. The vortex “stretches and unstretches them, and gives them their shape back.”

    To understand this process, it is important to understand the makeup of proteins. A protein is made of a string of subunits, called amino acids, that are folded into a three-dimensional shape. There are different levels of structures, often involving helical-shaped coils and pleated sheets. Every type of protein has its own unique shape that allows it to do its assigned  job.

    Proteins can be rendered useless by adverse conditions such as acidity, salinity or heat.  In the case of a boiled egg white, the heat of the water solidifies the proteins. The egg research was inspired by the volatility present in many lab-made proteins, especially those produced for cancer research. Oftentimes, scientists want to produce proteins associated with cancer in a laboratory for  further study.

    It is not uncommon for these man-made proteins to turn out misshapen due to its unnatural environment. When this happens it can take several days and quite a lot of effort to extract and rebuild any usable proteins from what the scientists described as a “jumbled mess.” This process is costly and inefficient, which is one of the reasons why the new research is important. By reversing the effects of boiling an egg white, the scientists have proven that as long as misshapen proteins have maintained the bonds between the amino acids, they can be restored to their original shape and functionality much more efficiently.

    Cancer research is not the only industry this discovery could help. Farmers and companies involved in cheese production could benefit from as well. Cheese-making involves recombinant proteins, which are proteins that are produced from multiple DNA sources and pieced together The creation of these proteins has traditionally involved some of the same difficulties as the creation of cancer proteins. Pharmaceutical companies are also looking into what this could mean for drug and antibody production.

    Scientists predict that the amount of time saved will lead to much cheaper and more streamlined protein production in the future, but only time will tell how many industries this new technology will truly affect.

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