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  • Jefferson Adams
    Jefferson Adams

    AN-PEP Digestive Enzymes Degrade Gluten Better Than Most Other Digestive Enzymes

    Reviewed and edited by a celiac disease expert.

    The pure enzyme AN-PEP effectively degraded all nine epitopes in the pH range of the stomach at much lower dose.

    AN-PEP Digestive Enzymes Degrade Gluten Better Than Most Other Digestive Enzymes - Photo: CC--SuperFantastic
    Caption: Photo: CC--SuperFantastic

    Celiac.com 06/22/2015 - Currently available digestive enzymes do not fully degrade gluten, and are thus of questionable use for people with celiac disease or gluten intolerance, say a team of researchers. Prior research had shown that post-proline cutting enzyme effectively degrade the immunogenic gluten peptides. Several existing digestive enzyme supplements claim to promote gluten degradation.

    The research team set out to assess the degradation of immunogenic gluten epitopes by currently available digestive enzymes. The team included G. Janssen, C. Christis, Y. Kooy-Winkelaar, L. Edens, D. Smith, P. van Veelen, and F. Koning. They are variously affiliated with the Department of Immunohematology and Blood Transfusion, Leiden University Medical Centre, Leiden, The Netherlands, DSM Food Specialties in Delft, The Netherlands, and DSM Food Specialties in South Bend, Indiana, USA.

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    For their study, they assessed five commercially available digestive enzyme supplements along with purified digestive enzymes. They assessed these enzymes using enzyme assays and mass spectrometric identification. They monitored gluten epitope degradation using R5 ELISA, mass spectrometric analysis of the degradation products, and T cell proliferation assays. 

    They found that the enzyme supplements leave the nine immunogenic epitopes of the 26-mer and 33-mer gliadin fragments largely intact. This is due to the high proline content of gluten molecules, which prevents gastrointestinal proteases from fully degrading them, leaving large proline-rich gluten fragments intact, including an immunogenic 33-mer from α-gliadin and a 26-mer from γ-gliadin.

    These latter peptides can trigger pro-inflammatory T cell responses resulting in tissue remodeling, malnutrition and a variety of other complications.

    In contrast, the pure enzyme AN-PEP effectively degraded all nine epitopes in the pH range of the stomach at much lower dose.

    From these results, the team concludes that most of the currently available digestive enzyme supplements are ineffective in degrading immunogenic gluten epitopes, but the AN-PEP do effectively degrade gliadin fragments.

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    Guest kayakinggal

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    Thank you for this article, very good information.

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    sc'Que?

    Does anyone know: Can something like AN-PEP be added to beer after brewing (but before bottling) to "gobble" gluten without disturbing the inherent qualities of the beer itself (body, flavor, ability to retain carbonation, etc)?  

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  • About Me

    Jefferson Adams

    Jefferson Adams is Celiac.com's senior writer and Digital Content Director. He earned his B.A. and M.F.A. at Arizona State University. His articles, essays, poems, stories and book reviews have appeared in numerous magazines, journals, and websites, including North American Project, Antioch Review, Caliban, Mississippi Review, Slate, and more. He is the author of more than 2,500 articles on celiac disease. His university coursework includes studies in science, scientific methodology, biology, anatomy, physiology, medicine, logic, and advanced research. He previously devised health and medical content for Colgate, Dove, Pfizer, Sharecare, Walgreens, and more. Jefferson has spoken about celiac disease to the media, including an appearance on the KQED radio show Forum, and is the editor of numerous books, including "Cereal Killers" by Scott Adams and Ron Hoggan, Ed.D.

    >VIEW ALL ARTICLES BY JEFFERSON ADAMS

     


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