The Problem
Gluten found in wheat, barley, rye and other cereal grains as well as casein found in dairy foods is difficult for the body to digest which, if not addressed, can result in serious health issues. Gluten (composed of gliadin and glutenin proteins) and casein contain amino acid sequences unusually high in the amino acid, proline. These proline-dense regions exhibit structural features that cause folding and helical cross-linking of the protein.[1] Researchers have identified the structural anomalies of the gluten and casein molecules as preventing hydrolysis by the body’s gastric, pancreatic and intestinal brush border proteases.[2,3] In addition, deficiencies in certain proteases, such as intestinal dipeptidyl peptidase, has been observed in individuals suffering from gluten sensitivities.[4] Incomplete digestion of gluten and casein damages the intestinal villi resulting in malabsorption of nutrients, inflammation with its associated discomfort (gluten intolerance) and, in extreme cases, a systemic immune response (celiac disease).[5,6]