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You may have noticed a major increase in the number of gluten-free products on store shelves in the past few years. While many people choose to adopt diets without gluten for reasons lacking in clinical evidence, there is a small subset of the population who genuinely can’t tolerate it – this is called celiac disease, and it’s estimated to affect about 1% of Americans.

If you’re not sure what gluten is, just take a bite of any bread made without it, and you’ll immediately comprehend that gluten is what makes baked foods actually taste good. As for a more scientific explanation, gluten is a complex protein present in wheat, rye, and barley. Many non-food products may also contain gluten. People with celiac disease are unable to properly digest gluten, so when they consume it, they experience inflammation in their intestines, which can trigger bloating, diarrhea, and other unpleasant symptoms.

Since the discovery of the condition, the only treatment available for people with celiac disease was to avoid gluten. Over time, manufacturers have employed new ways to eliminate the protein from food preparation, giving more options to people with celiac disease while also giving rise to the idea that gluten-free foods are healthier for the general population. Actually, the opposite is true: gluten-free foods are generally less nutritious than the originals, because they often contain more fat, sugar, and calories and less fiber than their glutenous counterparts. Also, because they’re typically unfortified, gluten-free foods are lacking in folic acid, calcium, and vitamin B.

Because of this, as well as the general challenges posed by having to strictly follow a gluten-free diet, scientists have long sought out alternative solutions for celiac disease. Dr. Ingrid Pultz and her students at the University of Washington believe they may have found the beginnings of one.

For the body to successfully absorb glutenous foods, particular enzymes are needed. Pultz and her team theorized that if there were some kind of consumable enzyme supplement capable of performing that same function, it would allow people with celiac disease to digest gluten the way those without the condition do. This would be similar to the medications used by lactose intolerant people.

In 2011, Pultz and the students decided to try to create such an enzyme themselves. Using a piece of software called the Rosetta Molecular Modeling Suite, they began with an existing enzyme capable of digesting protein in the acidic environment of the human stomach. The scientists were able to modify the structure of the enzyme on the computer so that it broke down gluten particles, and then they created about 100 prototypes. Ultimately, they selected the best aspects of each and combined them all into one singular enzyme, which they called KumaMax. Pultz and the students entered KumaMax into the International Genetically Engineered Machine competition, which it won.

The creators of KumaMax are working on bringing it to the public, and they will soon move testing out of the lab and into individuals with celiac disease. This process of creating new molecular systems is called synthetic biology, and it could very well be the treatment for celiac disease that people have been waiting for.

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