Big news for people who are wishy-washy about what they want to eat for breakfast. Investigators working in Australia and the US announced they have the know-how and the want-to at hand to unboil an already-cooked egg. So if you are two minutes into preparing that three-minute egg, soon you will be able to change your mind without consequence!

Sort of.

The report in the scientific journal, ChemoBioChem, actually goes by a particularly unsexy title: “Shear-Stress-Mediated Refolding of Proteins from Aggregates and Inclusion Bodies.” The future, it seems, is not in Plastics at all, but in folding, unfolding, and refolding proteins.

According to the authors, this protein folding problem is a whopper: “Overexpressed recombinant proteins for industrial, pharmaceutical, environmental, and agricultural applications annually represent a more than $160 billion world market.” In other words, like laundry, it pays to fold things correctly the first time.

They surely are correct about the size of the potential market. “Recombinant proteins” are used every day for patients in hospitals everywhere for tests and in treatments. A recent headliner was the flashing superstardom of Z-Mapp, the wonder drug for Ebola. Z-Mapp was a collection of proteins produced by splicing animal genes into plants (tobacco actually) and harvesting the product, purifying it, and injecting it into actual living patients (Kent Brantly most famously). But treatments for cancer and arthritis and countless other conditions are now increasingly reliant on this approach.

Indeed one of the great achievements in science in the last few decades has been kidnapping bacteria (and plants and yeasts), splicing in a specific human gene then sitting back and letting the usually docile E coli produce a human protein as directed by the grafted gene.

The problem is that the system is often too damn good—the deus ex bacteria production of human proteins is overly exuberant. It’s like Costco: they have what you want but in sizes and volumes of no human use. In this case, rather than the three gallon bottle of Rose’s Lime Juice, the engineered E coli makes too many long strands of the desired protein too fast; so many in fact that the proteins start to fold over and accrete and form “inclusion bodies” (sort of like little protein crystals). Plus in this new messy form, the proteins begin stick to the instruments. Eventually they gum up production and require a purge, both to restore the fabrication to normal but also to reclaim all the precious wrongly-folded proteins caked onto the walls.

The new egg unboiler won’t change any of this, but it will allow companies to scrub away all that superfluous protein-turned-glop from the fancy production instruments and fold it correctly so that it is a product that can be used. Sort of like getting same bottle of scarcely used Rose’s Lime Juice and freshening it up to newness as often as you want.

According to the authors, previously this scrub-rinse-spin-refold cycle previously took days and days but their new approach can accomplish this in one-one-hundredth the time. Their trick is to use a “vortex fluid device (VFD) to apply shear forces for rapid equilibration of protein folding.” Basically a high-end centrifuge, the spinning of the dissolved proteins creates a thin film of fluid that flows with the glass tube, eventually unfolding then refolding the precious protein. Sort of like popping open a crumpled paper bag.

What does this mean for cancer treatments and new drugs for infections like Ebola? Like all “breakthroughs“ that appear in orthodox science magazines, this is the first step of hundreds if not thousands to a useful new SOP for producing therapeutics. And most of these early steps will fail sooner or later, bogged down by cost or technical problems or the locomotive screech of a better faster cheaper new answer to the same problem. In other words, the unboiling of the egg does not signal a victory in the war on cancer.

Then what about the boiled or unboiled egg? Egg whites, as every dieter knows, are pure protein—and cooking them “denatures” them, transforming the egg white from the clear slightly frightening gelatinous ooze we all know to the snow-white rubbery morsel we eat for breakfast. At a microscopic level, this denaturing is in fact a process of taking nicely organized proteins and folding them into a messy heap, the equivalent of clothes in a teenage boy’s bedroom.

To prove the power of their new approach to protein re-education and refolding, the press coverage has claimed the scientists had successfully taken a chewy egg white and returned it to its primitive gelatinous state. Yet I have read the article many times, including the figures and the asides, and can’t quite find the section on this though big words and high concepts were flying left and right.

So it is possible that I missed the egg white part. Or it is possible that a small step for man is in fact a small step for man but a good PR company can inflate just about anything. More likely though, is that the implicit message of the purported scientific achievement—Thomas Wolfe was wrong all these years! You can go home again!—was too irresistible; the notion of rolling back time a little bit and getting a chance to reorganize our lives at the protein level (whatever that means) has made a routine industrial innovation article into a hot ticket. But that’s OK – in the midst of scientists taking heat for miscalculated blizzards and being dragged into discussing deflated footballs, it’s nice to see hard-core, really tedious science get a chance to crow.