Scientists work out how ‘unboil’ part of an egg

How do you like your eggs in the morning? What about boiled and then unboiled again? Chemists at the University of California, Irvine, have recently published research in the journal ChemBioChem, detailing a process which can do just that – ‘unboil’ a particular protein from a hen’s egg, returning it to its original liquid form.

This may sound like very trivial research, but the functionality of proteins depends hugely on the exact 3D structure, so a significant problem facing scientists working with proteins is their misfolding, or denaturation. At present, reversing this is very costly and time-consuming.

The new method used by this team involves adding a urea compound to the boiled egg white to turn it back to a liquid. This is then placed into a vortex fluid device, which spins the protein and stretches it back to the original structure.

A similar method could be applied to proteins used elsewhere in industry, replacing a 4-day untangling process into one which takes just a few minutes. For example, cancer antibodies are often synthesised in expensive hamster ovary cells, because they are not prone to misfolding there, but this may be a new, cheaper option.

Gregory Weiss, Professor of Chemistry and Molecular Biology and Biochemistry at UC Irvine said, “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,”