Boiling an egg? Been there, done that to perfection, right? But what about 'unboiling' one? In the last couple of weeks, the scientific world has been going gaga about this amazing feat. A team of American and Australian scientists led by Professor Gregory A. Weiss from the University of California, say they did it and published an online paper on just that in the ChemBioChem journal on January 23, 2015.
The confusingly titled "Shear-Stress-Mediated Refolding of Proteins from Aggregates and Inclusion Bodies' explains how proteins can be refolded faster and better using urea and precisely calibrated shearing forces. These scientists claim that their method takes just a few minutes, while older lab processes for refolding proteins took four days. This news could positively impact a $160 billion world market in industrial, pharmaceutical, environmental and agricultural applications, and among other things, could also offer insight on a cure for cancer.
But wait! The heroic scientists may just have egg on their face. Their 'breakthrough' may have poached an old idea. "They found a way to get renaturated proteins, and this is interesting. But it has nothing to do with uncooking an egg, which I was doing decades ago!" announces Hervé This. And he should know a thing or two about esoteric concepts such as this. After all, the French physical scientist has been delving deep into the secrets of cooking processes for almost 30 years. He was the man who introduced the idea of molecular gastronomy to the world as far back as 1986. He's been the inspiration for the likes of top chefs such as Ferran Adrià, Heston Blumenthal, Pierre Gagnaire and many others.
Hervé has been demonstrating the process of unboiling an egg to amazed students and enthusiasts for years now. He sent me this cool podcast on the website of AgroParisTech, Paris, where he conducts all his research. With childlike enthusiasm, he explains the deceptively simple process. Here's the gist of what's on the video: First, he reminds you that an egg white is 90% water and 10% proteins. Then, he explains how an egg gets cooked in the presence of heat, with the protein molecules unravelling and connecting with each other and surrounding the water molecules, changing the consistency of the egg white from viscous to more solid. Next, he explains the various types of bonds needed for this process to happen and how to identify which ones feature in the case of a boiled egg. And then, he demonstrates how a reducing agent such as sodium borohydride (NaBH4) can make the protein molecules separate from each other in about three hours, allowing the egg go back to the same consistency as when it was raw (first whipped and then viscous). He emphasises that you can't eat that egg after adding a chemical like NaBH4 to it but that the same results can be achieved harmlessly by using vitamin C.
"Unboiling takes about 30 seconds when you use NaBH4 (sodium borohydride). It is longer with vitamin C (if the pH is adjusted carefully) but inherently safer if you're trying it at home," twinkles Hervé.