In addition, the enzyme operates best in just the kind of physiological environment found in the human stomach and works 60 times faster than an earlier promising enzyme, which was not effective in acidic conditions and was inactivated by pepsin, both of which are 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," according to Frits Koning, researcher at the Leiden University Medical Center, The Netherlands, who headed the team that has published a new research paper on its work.
The paper, "Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease," is in the online American Journal of Physiology- Gastrointestinal and Liver Physiology, published by The American Physiological Society. Research was by Dariusz Stepniak, Liesbeth Spaenij-Dekking, Cristina Mitea, Martine Moester, Arnoud de Ru, Renee Baak-Pablo, Peter van Veelen and Frits Koning of Leiden University Medical Center, the Netherlands, and Luppo Edens of DSM Food Specialties, Delft.
Clinical trials are likely next step
The new prolyl endoprotease (PEP) that was studied is derived from Aspergillus niger (AN), a common fungus. Strains of A. niger are used in industrial production of citric and gluconic acid as well as producing several food grade enzymes.