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Chemists have turned a boiled egg in the raw - VIDEO PDF Print E-mail
Sunday, 01 February 2015 17:09

Egg 90% water and 10% of the proteins, which are long chain amino acids and entangled held together by weak atomic bonds. When the egg is immersed in boiling water, heat destroys these connections, and chains start to break, break down and rebuild.

So under high temperature egg whites changes its structure, becoming transparent and liquid and solid white.

American and Australian chemists have figured out how to reverse the process of protein denaturation, more simply, to return hard-boiled egg in the liquid, again raw, condition.

"In this paper we describe a device which can restore the state of the protein in the crude after egg cooked for 20 minutes at a temperature of 90 degrees Celsius - professor of chemistry and molecular biology and biochemistry Gregory Weiss (Gregory Weiss) of California University in Irvine. - But, of course, our main goal has not been manipulated with boiled eggs - it is only a demonstration of the process. in reality, for example, there is a lot of sticky protein - it takes a long time to clear them from the tube. many would like to receive funds for the restoration of this material. "

At first glance, the discovery may indeed seem useless. But it can significantly reduce the cost of cancer treatment, food production, and will be useful in other areas of the biotechnology industry.



The research team Weiss, like many scientists, seeks to learn how to effectively produce processing securities molecular proteins. This "recycle" can be used in multiple domains.

The ways in which scientists have used so far have been very costly and time-consuming: the equivalent of dialysis at the molecular level would take about four days. The new process converts raw Boiled egg in a few minutes.

To return to "tough" protein in the liquid state, scientists use urea, which is able to "disengage" proteins and dilute the solids. But this is only half of the process: at the molecular level, some groups of proteins were still linked.

California scientists used a centrifuge, developed by Flinders University in South Australia and rotating at a speed of 5 miles per minute. With its help, the proteins were subjected to a certain load, which "undid" the structure and returned to liquid form.

The researchers did not report whether after all these processes consume eggs for food. However, this finding may be useful in various fields. For example, pharmaceutical companies currently produce antibodies to cancer expensive hamster ovary cells, proteins which are often minimized. The ability to quickly and cheaply convert proteins from yeast or E. coli is able to optimize the production of protein and make cancer treatment more affordable.


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