GliadinX is a dietary supplement with the highest concentration of AN-PEP, Prolyl Endopeptidase (Aspergillus Niger), the most effective enzyme proven to break down gluten in the stomach. This high potency enzyme formulation is specifically designed to break down gliadin, and unlike other enzyme formulas that claim to do the same, there is a growing body of research that backs up the effectiveness of GliadinX (see Sources below).
GliadinX does not prevent and is not a cure for celiac disease, however, extensive scientific research has been conducted at multiple medical centers which has shown that it effectively breaks down gliadin into small, harmless fragments before it can reach the small intestine. GliadinX is perfect for celiacs who still want to eat outside of their home, and not have to worry about cross-contamination, and for those who are gluten sensitive and wish to continue eating gluten.
"12. Treatment of the Extra-Intestinal Manifestations of CD
the only one that is currently on the market is the gluten-specific enzyme, GliadinX (AN-PEP). Unfortunately, it is only capable of detoxifying 0.2 g of gluten or roughly that of 1/8 of a slice of gluten-containing bread. For this reason, it should only be used as an adjunct to the GFD when there are concerns for accidental gluten contamination and in an effort to ameliorate symptoms, not as a replacement for the GFD."
Many people have asked Celiac.com how they can order this product, so we've included a "Buy Now" link below to order them directly from the manufacturer:
Sources: Scientific publications on AN-PEP enzymes:
- Extra-Intestinal Manifestation of Celiac Disease in Children. Nutrients 2018, 10(6), 755; doi:10.3390/nu10060755
- Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model
- Enzymatic gluten detoxification: the proof of the pudding is in the eating!
- Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease
- Degradation of gluten in wheat bran and bread drink by means of a proline-specific peptidase