An enzyme added to foods containing gluten could put an end to the misery of celiac disease for many sufferers, allowing them to eat almost anything they fancy without having to worry about the effects on their digestive system.
Celiac disease is an autoimmune disorder of the small intestine in which an abnormal reaction to the gluten protein in wheat, barley, and rye results in inflammation, which causes a temporary flattening of the nutrient absorbing villi that line the bowel. This prevents sufferers absorbing nutrients effectively from their diet. Until now, the only course of action is to avoid all foods containing gluten.
Now, Frits Koning, of Leiden University Medical Center, in The Netherlands, and colleagues at DSM Food Specialties, in Delft, have investigated the potential of a new enzyme obtained from the black microbial fungus Aspergillus niger developed originally for commercial food processing in making any food gluten free in the stomach. The enzyme, a prolyl endoprotease, breaks down whole gluten molecules as well as the peptides that stimulate the immune system’s T cells causing the symptoms of celiac disease.
The enzyme works optimally under the physiological conditions found in the human stomach, i.e. acidic pH and around 37 Celsius. Importantly, the enzyme works sixty times faster than a previously investigated enzyme and resists the protein-cracking action of pepsin found in the stomach.
“On the basis of our results, there now is a realistic chance that oral supplementation with an enzyme can ensure gluten degradation in the stomach before reaching the small intestine, where it causes problems for people with celiac disease,” explains Koning.
“An effective enzymatic treatment for celiac diseases requires a means of destroying all or at least the vast majority of gluten derived T cell stimulatory sequences,” the researchers explain. The new PEP was extracted from a fungus commonly used to make food grade citric acid and other products but will have to undergo extensive clinical trials in volunteers with celiac disease to determine how effective it will be in practice. The results could soon be implemented in finding a way to stop celiac symptoms, Koning told Reactive Reports, “Timescale is likely to be a few years,” he says, “It is our goal to make some kind of formulation that patients can take before of with their meal but this still has to be worked out.”
Stepniak, D. (2006). Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease AJP: Gastrointestinal and Liver Physiology, 291 (4) DOI: 10.1152/ajpgi.00034.2006