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ZyGluten™


Scott Adams

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Scott Adams Grand Master

If you are one of the approximately 2-3 million Americans with celiac disease, ZyGluten™ may be taken before you eat out at a restaurant or a friend\'s house, as it may help break down any gluten cross-contamination that you might encounter.

View the full article


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kareng Grand Master

This does say it is for NCGS....so not  for Celiacs.  There is a drug being developed that may actually break down the gluten in the stomach before it hits the intestines.  However, that is still in clinical trials.

kareng Grand Master

So there is this drug being developed.  I believe there may be another, too?  If I have time, I will look and post.  

 

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cyclinglady Grand Master

Sorry, but this product (supplement) is not even certified gluten free.   Seems odd that a product geared to Non-Celiac Gluten Intolerance would not take the extra step of getting certified.   I guess I am a Nervous Nellie, especially after the reports that several probiotics were contaminated with gluten.  

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  • 4 weeks later...
carrieteel Newbie

Has anyone tried this Zygluten product?  I too am concerned that I do not see gluten-free certification.  I'd never intentionally eat gluten but would love to have a little less fear of cross contamination.  

cyclinglady Grand Master
9 hours ago, carrieteel said:

Has anyone tried this Zygluten product?  I too am concerned that I do not see gluten-free certification.  I'd never intentionally eat gluten but would love to have a little less fear of cross contamination.  

The manufacturer of this product doe NOT recommend it for those with celiac disease.  

GFinDC Veteran

Here as article about a couple enzymes that are reputed to help digest gluten.

____________________________________________________________________________________

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A food-grade enzyme preparation with modest gluten detoxification properties.

Open Original Shared Link1, Open Original Shared Link, Open Original Shared Link, Open Original Shared Link, Open Original Shared Link, Open Original Shared Link.

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Abstract

BACKGROUND AND AIMS:

Celiac sprue is a life-long disease characterized by an intestinal inflammatory response to dietary gluten. A gluten-free diet is an effective treatment for most patients, but accidental ingestion of gluten is common, leading to incomplete recovery or relapse. Food-grade proteases capable of detoxifying moderate quantities of dietary gluten could mitigate this problem.

METHODS:

We evaluated the gluten detoxification properties of two food-grade enzymes, aspergillopepsin (ASP) from Aspergillus niger and dipeptidyl peptidase IV (DPPIV) from Aspergillus oryzae. The ability of each enzyme to hydrolyze gluten was tested against synthetic gluten peptides, a recombinant gluten protein, and simulated gastric digests of whole gluten and whole-wheat bread. Reaction products were analyzed by mass spectrometry, HPLC, ELISA with a monoclonal antibody that recognizes an immunodominant gluten epitope, and a T cell proliferation assay.

RESULTS:

ASP markedly enhanced gluten digestion relative to pepsin, and cleaved recombinant alpha2-gliadin at multiple sites in a non-specific manner. When used alone, neither ASP nor DPPIV efficiently cleaved synthetic immunotoxic gluten peptides. This lack of specificity for gluten was especially evident in the presence of casein, a competing dietary protein. However, supplementation of ASP with DPPIV enabled detoxification of moderate amounts of gluten in the presence of excess casein and in whole-wheat bread. ASP was also effective at enhancing the gluten-detoxifying efficacy of cysteine endoprotease EP-B2 under simulated gastric conditions.

CONCLUSIONS:

Clinical studies are warranted to evaluate whether a fixed dose ratio combination of ASP and DPPIV can provide near-term relief for celiac patients suffering from inadvertent gluten exposure. Due to its markedly greater hydrolytic activity against gluten than endogenous pepsin, food-grade ASP may also augment the activity of therapeutically relevant doses of glutenases such as EP-B2 and certain prolyl endopeptidases.

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There may be more recent research, this is just the first article I found.


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