AN-PEP Enzyme
AN-PEP (aspergillus niger prolyl endopeptidase), a dietary supplement is available and has been studied. Unnlike other enzyme supplements on the market, it has been shown to break down gluten in the stomach. However, it has not gone through clinical trials and been proven to help those with Celiac Disease or Gluten Sensitivity. In fact, one study failed to show an effect in people with CD, although the study authors believe that was due to the study design (see below for further information). AN-PEP is by no means a substitute for the Gluten-Free diet. It does not completely degrade gluten It is intended only to help with cross-contamination, and there is reason to believe that it would be effective for that purpose (see research articles below).
The scientific name of the enzyme is Aspergillus Niger prolyl endoprotease, or AN-PEP.
The trade name is Tolerase G
Here is a video from the manufacturer.
Tolerase G is available in a number of products, including:
GliadinX
GlutnGo™ (GlutnGo is on Amazon*)
SpectraZyme® Gluten Digest
Gluten Rid
See this article: Are Enzymes Safe for the Celiac Disease Community? Researchers Set the Record Straight
The trade name is Tolerase G
Here is a video from the manufacturer.
Tolerase G is available in a number of products, including:
GliadinX
GlutnGo™ (GlutnGo is on Amazon*)
SpectraZyme® Gluten Digest
Gluten Rid
See this article: Are Enzymes Safe for the Celiac Disease Community? Researchers Set the Record Straight
Research on AN-PEP (Tolerase G)
2017: A unique enzyme could be a game-changer for gluten-sensitive patients
2015: Randomised clinical study: Aspergillus niger-derived enzyme digests gluten in the stomach of healthy volunteers.
2015: Letter (regarding above study) Gluten digestion in the stomach and duodenum by Aspergillus-derived enzyme - things to ponder
2015: Author's reply to Letter: gluten digestion in the stomach and duodenum by Aspergillus niger-derived enzyme – things to ponder.
2015: Influence of dietary components on Aspergillus niger prolyl endoprotease mediated gluten degradation.
From the abstract:
2013: Consumption of gluten with gluten-degrading enzyme by celiac patients: A pilot-study
This study failed to prove an effect, but the authors believe the study design may have contributed to that. From the Discussion section: "the primary aim of the study was not met as the placebo arm did not show any deterioration after
2 wk of gluten consumption. With hindsight, the study should possibly have been designed for a much longer period of time with many more patients".
2008: Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model: implications for coeliac disease.
2006: Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease.
2015: Randomised clinical study: Aspergillus niger-derived enzyme digests gluten in the stomach of healthy volunteers.
2015: Letter (regarding above study) Gluten digestion in the stomach and duodenum by Aspergillus-derived enzyme - things to ponder
2015: Author's reply to Letter: gluten digestion in the stomach and duodenum by Aspergillus niger-derived enzyme – things to ponder.
2015: Influence of dietary components on Aspergillus niger prolyl endoprotease mediated gluten degradation.
From the abstract:
- AN-PEP optimal dosage was 20 proline protease units (PPU) per gram of gluten.
- The addition of a carbonated drink strongly enhanced AN-PEP activity because of its acidifying effect.
- Fat did not affect gluten degradation by AN-PEP.
- The presence of food proteins slowed down gluten detoxification.
- Raw gluten was degraded more efficiently by AN-PEP than baked gluten.
- Therefore, meal composition influences the amount of AN-PEP needed for gluten elimination.
2013: Consumption of gluten with gluten-degrading enzyme by celiac patients: A pilot-study
This study failed to prove an effect, but the authors believe the study design may have contributed to that. From the Discussion section: "the primary aim of the study was not met as the placebo arm did not show any deterioration after
2 wk of gluten consumption. With hindsight, the study should possibly have been designed for a much longer period of time with many more patients".
2008: Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model: implications for coeliac disease.
2006: Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease.
Other Enzymes in Development
KumaMax
2017: Latiglutenase, also known as IMGX003 and formerly as ALV-003 has recently completed Phase IIb trials with mixed results:
2015: Ineffective Degradation of Immunogenic Gluten Epitopes by Currently Available Digestive Enzyme Supplements
Note: This title does not refer to AN-PEP. Five other enzyme supplements, containing DPPIV and on the US market in 2012, were tested and shown to be ineffective).
2009: A Food-Grade Enzyme Preparation with Modest Gluten Detoxification Properties
2017: Latiglutenase, also known as IMGX003 and formerly as ALV-003 has recently completed Phase IIb trials with mixed results:
- 2017: No Difference Between Latiglutenase and Placebo in Reducing Villous Atrophy or Improving Symptoms in Patients With Symptomatic Celiac Disease
- 2017: Disappointing Results in Celiac Disease Drug Trial But Future Hopeful
2015: Ineffective Degradation of Immunogenic Gluten Epitopes by Currently Available Digestive Enzyme Supplements
Note: This title does not refer to AN-PEP. Five other enzyme supplements, containing DPPIV and on the US market in 2012, were tested and shown to be ineffective).
2009: A Food-Grade Enzyme Preparation with Modest Gluten Detoxification Properties
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