Ciliac's disease is a debilitating condition where sufferers have an immunologic reaction to gluten, a protein commonly found in wheat, barley, and rye. Consumption of gluten results in severe digestive issues and other health problems. Researchers at Boston University, Headed by Eva Helmerhorst, have described the isolation of a protease from Rothia mucilaginosa that is capable of degrading the epitope in gluten that causes the immune response. After isolation, the enzyme was compared to other known proteins and it was discovered it was of the subtilisin family of enzymes. Tests of subtilisins from Bacillus licheniformis, subtilisin A and the food-grade Nattokinase, were found to also be able to degrade gluten.
Currently, the only treatment for Celiac's disease is by strict adherence to a gluten-free diet. The discovery that subtilisins are capable of degrading the gluten epitope, may make it possible to develop enzyme therapeutics to treat the disease. The existence of a food-grade subtilisin, Nattokinase, an enzyme that has been cleared for human consumption for decades, may speed the development of treatments.