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    Jefferson Adams
    Jefferson Adams

    Current Celiac Enzyme Supplements Fail to Fully Break Down Gluten

    Reviewed and edited by a celiac disease expert.
    Current Celiac Enzyme Supplements Fail to Fully Break Down Gluten - Current enzymes come up short in breaking down gluten. Photo: CC--Superfantastic
    Caption: Current enzymes come up short in breaking down gluten. Photo: CC--Superfantastic

    Celiac.com 10/02/2015 - Many people with celiac disease or gluten-intolerance take digestive enzymes, hoping for some protection against accidental gluten-contamination.

    Photo: CC--SuperfantasticPost-proline cutting enzymes have been shown to effectively degrade the immunogenic gluten peptides and have been proposed as oral supplements. Several existing digestive enzyme supplements also claim to aid in gluten degradation.

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    However, not all gluten proteins are the same. The gluten proteins that are particularly active in triggering an adverse immune reaction in celiac disease are known as immunogenic 33-mer from α-gliadin and a 26-mer from γ-gliadin.

    So, how effective are currently available digestive enzyme supplements ineffective in breaking down these specific gliadins that triggers immune reactions in people with celiac disease? A team of researchers recently set out to determine the effectiveness of such existing enzyme supplements in comparison with a well characterized post-proline cutting enzyme, Prolyl EndoPeptidase from Aspergillus niger (AN-PEP).

    The research 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 at Leiden University Medical Centre in Leiden, The Netherlands, DSM Food Specialties, Delft, The Netherlands, and DSM Food Specialties in South Bend, Indiana, USA.

    For their study, the team subjected each of the five commercially available digestive enzyme supplements along with purified digestive enzymes to 1) enzyme assays and 2) mass spectrometric identification. Gluten epitope degradation was monitored by 1) R5 ELISA, 2) mass spectrometric analysis of the degradation products and 3) T cell proliferation assays.

    Their findings show that, due to the high proline content of gluten molecules, gastrointestinal proteases are unable to fully degrade them leaving large proline-rich gluten fragments intact, including an immunogenic 33-mer from α-gliadin and a 26-mer from γ-gliadin.

    Basically, none of the currently available digestive enzyme supplements are effective in degrading immunogenic gluten epitopes. This means that these enzymes are not likely to be helpful to people with celiac disease.

    Share your thoughts in our comments section below.

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    Guest Coloradosue

    Posted

    Just threw my bottle of enzymes away. Sigh.

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    Guest Terry Lynch

    Posted

    From your reference article:

    "Finally, we have investigated a novel type of prolyl endoprotease from the food grade fungus Aspergillus niger (AN-PEP) [6,10,11]. AN-PEP efficiently degrades gluten under the conditions mimicking the gastrointestinal tract [11] and was found to be safe both in animal studies and in humans [10,12]. Thus in vitro and in vivo experiments indicate that enzymes can be identified that degrade gluten proteins efficiently"

    So the glut&go proylyl endopetidase ANPEP by Bricker Labs works and withstands low PH degration in the stomach. I am going to be using this supplement regularly as my intestinal street sweeper of incidental gliadin intake while continuing the gluten free diet. A most valuable of the year supplement for Celiac persons everywhere in my opinion and study should use this tool to keep gliaden free.

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    Guest admin
    Just threw my bottle of enzymes away. Sigh.

    I don't think you need to do that, as they do help break things down, but apparently don't do the job fully.

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    Guest Jefferson

    Posted

    From your reference article:

    "Finally, we have investigated a novel type of prolyl endoprotease from the food grade fungus Aspergillus niger (AN-PEP) [6,10,11]. AN-PEP efficiently degrades gluten under the conditions mimicking the gastrointestinal tract [11] and was found to be safe both in animal studies and in humans [10,12]. Thus in vitro and in vivo experiments indicate that enzymes can be identified that degrade gluten proteins efficiently"

    So the glut&go proylyl endopetidase ANPEP by Bricker Labs works and withstands low PH degration in the stomach. I am going to be using this supplement regularly as my intestinal street sweeper of incidental gliadin intake while continuing the gluten free diet. A most valuable of the year supplement for Celiac persons everywhere in my opinion and study should use this tool to keep gliaden free.

    AN-PEP has only been shown to fully break down gluten in healthy subjects, not in people with celiac disease. Is it better than nothing? Probably, but don't count on it to do the job fully. The maker is working to get AN-PEP to work effectively for celiac patients, but tests don't show success on that yet.

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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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