Wheat Rescue

New research suggests that the small intestines of up to 60% of adults with celiac disease never completely heal despite following a gluten-free diet.

This could be due in part to gluten contamination in many “gluten-free” foods. A recent study examined 5,624 foods tested by 804 users and found that 32% of foods labelled “gluten-free” contained measurable amounts of gluten. Interestingly, gluten-free pizzas and pastas were the most likely to test positive for gluten with over 50% of samples showing gluten contamination. However, gluten contamination is simply an additional problem to an already inadequate strategy. In one 2010 study of 241 subjects with celiac disease, only 35% of subjects saw mucosal recovery of the small intestines after 2 years going gluten-free, and only 66% saw mucosal recovery after 5 years going gluten-free. Another study in 2009 examined 465 celiac subjects who adhered to a gluten-free diet for 16 months and found that total restoration of the intestinal damage inflicted by gluten was exceptionally rare (roughly 8%) in adult celiacpatients despite following a gluten-free diet.

Gluten-free diets are thus a strategy for preventing further damage – not a complete treatment.

WheatRescue™ is a unique blend of powerful digestive enzymes and probiotics designed to support complete digestion of gluten and other inflammatory wheat-derived peptides. Apart from those with health problems, research has shown that all people experience transient intestinal permeability when they ingest gluten.

Here’s what it contains:

Blend of Peptidase, Fungal & Acid-Stable Protease – These expertly curated enzymes work in synergy to breakdown the various gliadin and glutenin peptides which have different characters, structures and effects on the body. The blend addresses issues of viability through exposure to trypsin, chymotrypsin and gastric juices, ensuring protein bonds are cleaved, and resulting peptides are broken down into amino acids for complete digestion of gluten. The speed of gluten degradation is also imperative and this blend is able to degrade gluten up to 60x faster than other proteases.

Tolerase® G – A trademarked dietary supplement, containing Aspergillus niger derived prolyl endoprotease (AN-PEP). It is a proline-specific digestive enzyme designed to have optimal activity within the stomach’s harsh conditions. This is of great significance because gluten is proline-rich, yet proline-cleaving proteases are absent in the GI tract. Also, the ability to function and degrade gluten in the stomach prior to reaching the duodenum spares autoimmune activation in the gut. Unlike most commercially available gluten proteases, Tolerase® can withstand extremely acidic conditions and thrives in environments up to 2.5 pH. It is also the first and only enzyme demonstrated to effectively break down residual gluten. Ex vivo studies and a recent randomized, double-blind, placebo-controlled study all demonstrate that AN-PEP leaves nearly none or minimal gluten in the duodenum after degrading it in the stomach.

Lipase – As pancreatic insufficiency is increasingly common especially so in Celiac disease, the consequent maldigestion and diarrhoea that occurs in many cases can be ameliorated largely with lipase.

Betaine HCL – Hydrochloric acid (HCl) is a component of gastric secretions, which aids the digestion of nutrients such as protein. In addition, it kills off pathogens and denatures molecules that may otherwise cause further irritation to the gut and body. Low stomach acid has been proposed as an underlying culprit of gluten sensitivity and Celiac Disease. When gastric pH rises above 4, an enzyme known as pepsin is deactivated. This allows food particles such as gluten to pass from the stomach to the duodenum undigested, causing inflammation and food intolerance. Betaine HCL overcomes this problem.

Proprietary Probiotic Blend – Bacillus Subtilis, Bacillus Coagulans and Saccharomyces Boulardii are able to survive gastric acid and bile salts to colonise, crowd out pathogens and yeast, provide postbiotics like butyrate and lactate which modulate the epithelial response to gluten by improving barrier function and reducing gliadin induced cytokine secretion.

WheatRescue™ is the most comprehensive and effective gluten support formula on the market today.

References:

1. de Souza PM, et al. A biotechnology perspective of fungal proteases. Braz J Microbiol. 2015;46(2):337–346.

2. Caputo I, et al. Enzymatic Strategies to Detoxify Gluten: Implications for Celiac Disease. Enzyme Research. 2010;2010:1-9.

3. Heredia-Sandoval NG, et al. Microbial Proteases in Baked Goods: Modification of Gluten and Effects on Immunogenicity and Product Quality. Foods. 2016;5(3):59.

4. Rizzello CG, et al. Highly efficient gluten degradation by lactobacilli and fungal proteases during food processing: new perspectives for celiac disease. Appl Environ Microbiol. 2007;73(14):4499–4507.

5. De Angelis M, et al. Mechanism of degradation of immunogenic gluten epitopes from Triticum turgidum L. var. durum by sourdough lactobacilli and fungal proteases. Appl Environ Microbiol. 2010;76(2):508–518.

6. Rizzello CG, et al. Use of fungal proteases and selected sourdough lactic acid bacteria for making wheat bread with an intermediate content of gluten. Food Microbiology. 2014;37:59-68.

7. Rey M, et al. Addressing proteolytic efficiency in enzymatic degradation therapy for celiac disease. Scientific Reports. 2016;6(1).

8. Beasley DE, et al. The Evolution of Stomach Acidity and Its Relevance to the Human Microbiome. PLoS One. 2015;10(7):e0134116.

9. Shan L, et al. Comparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue. Biochem J. 2004;383(Pt 2):311–318.

10. Stepniak D, et al. Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease. Am J Physiol Gastrointest Liver Physiol. 2006;291(4).

11. Krishnareddy S, et al. Commercially available glutenases: a potential hazard in coeliac disease. Therap Adv Gastroenterol. 2017;10(6):473–481.

12. Balakireva AV, et al. Properties of Gluten Intolerance: Gluten Structure, Evolution, Pathogenicity and Detoxification Capabilities. Nutrients. 2016;8(10):644.

13. Wieser H, et al. Detoxification of Gluten by Means of Enzymatic Treatment. Journal of AOAC International. 2012;95(2): 356-363.

14. Gordon SR, et al. Computational design of an α-gliadin peptidase. J Am Chem Soc. 2012;134(50):20513–20520.

15. Tsiatsiani L, et al. Aspergillus niger Prolyl Endoprotease for Hydrogen-Deuterium Exchange Mass Spectrometry and Protein Structural Studies. Anal Chem. 2017;89(15):7966–7973.

16. Mitea C, et al. Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model: implications for coeliac disease. Gut. 2007;57(1):25-32.

17. Salden BN, et al. Randomised clinical study: Aspergillus niger-derived enzyme digests gluten in the stomach of healthy volunteers. Aliment Pharmacol Ther. 2015;42(3):273–285.

18. Perri F, et al. Intraduodenal Lipase Activity in Celiac Disease Assessed by Means of 13C Mixed-Triglyceride Breath Test. Journal of Pediatric Gastroenterology & Nutrition. 1998;27(4):407-410.

19. Evans KE, et al. Pancreatic Insufficiency in Adult Celiac Disease: Do Patients Require Long-Term Enzyme Supplementation? Digestive Diseases and Sciences. 2010;55(10):2999-3004.

20. Sadr-Azodi O, et al. Patients with celiac disease have an increased risk for pancreatitis. Clin Gastroenterol Hepatol. 2012;10(10):1136–1142.e3.

21. Leeds JS, et al. Is exocrine pancreatic insufficiency in adult coeliac disease a cause of persisting symptoms? Alimentary Pharmacology & Therapeutics. 2006;25(3):265-271.

22. Lebwohl B, et al. Use of proton pump inhibitors and subsequent risk of celiac disease. Dig Liver Dis. 2014;46(1):36–40.

23. Khalili H, et al. Use of proton pump inhibitors and risk of hip fracture in relation to dietary and lifestyle factors: a prospective cohort study. BMJ. 2012;344:e372.

24. Usai-Satta P, et al. Delayed gastric emptying does not normalize after gluten withdrawal in adult celiac disease. Scandinavian Journal of Gastroenterology. 2016;51(8):923-926.

25. Du L, et al. Impact of gluten consumption in patients with functional dyspepsia: A case-control study. Journal of Gastroenterology and Hepatology. 2017;33(1):128-133.

26. Read NW. Food and hypersensitivity in functional dyspepsia. Gut. 2002;51(Supplement 1):i50-i53.

27. Kines K, Krupczak T. Nutritional Interventions for Gastroesophageal Reflux, Irritable Bowel Syndrome, and Hypochlorhydria: A Case Report. Integr Med (Encinitas). 2016;15(4):49–53.

28. Stein T. Bacillus subtilis antibiotics: structures, syntheses, and specific functions. Molecular Microbiology. 2005;56(4): 845-857.

29. Cho YH, et al. Production of nattokinase by bath and fed-batch culture of Bacillus subtilis. N Biotechnol. 2010;27(4): 341-6.

30. Huang JM, et al. Immunostimulatory activity of Bacillus spores. FEMS Immune Med Microbial. 2008;52:195-203.

31. Dound YA, et al. The effect of Probiotic Bacillus subtilis HU58 on Immune Function in Healthy Human. Indian Practitioner. 2017;70(9): 15-20.

32. Possemiers PD, Van de Genachte N. Evaluation of the Bacillus subtilis strain HU58 in the SHIME technology platform. ProDigest. 2013:1-40.

33. Vinolo MAR, et al. Regulation of Inflammation by Short Chain Fatty Acids. Nutrients. 2011; 3(10): 858–876.

34. Bergey B. Bergey’s Manual of Determinative Bacteriology. 9th ed. Baltimore, MD: The Williams and Wilkens Company; 1993.

35. Bomko TV, Nosalskaya TN, Kabluchko TV, et al. Immunotropic aspect of the Bacillus coagulans probiotic action. J Pharm Pharmacol. 2017;69(8):1033-1040.

36. Kim YM, et al. Studies on the production of beta-galactosidase by Bacillus coagulans. Properties and applications of beta-galactosidase. Korean J Applied Microbiol Bioeng. 1985;13:355-360.

37. Jurenka S. Bacillus coagulans: monograph. Altern Med Rev. 2012;17(1):76-81.

38. Ducluzeau R, Bensaada M. Comparative effect of a single or continuous administration of Saccharomyces boulardii on the establishment of various strains of Candida in the digestive tract of gnotobiotic mice. Ann Microbiol (Paris). 1982;133(3): 491-501.

39. Kollaritsch H, Holst H, Grobara P, et al. Prevention of traveler’s diarrhea with Saccharomyces boulardii. Results of a placebo controlled double-blind study. Fortschr Med. 1993;111(9):152-6.

40. Catagliuolo I, Riegler MF, Valenick L, et al. Saccharomyces boulardii protease inhibits the effects of Clostridium difficile toxins A and B in human colonic mucosa. Infect Immun. 1999;67(1):302-7.

41. Czerucka D, Nano JL, Bernasconi P, et al. Effect of Saccharomyces boulardii on cholera toxin-induced cAMP levels in rat epithelial intestinal cell lines. Gastroenterol Clin Biol. 1989;3:383-7.

42. Buts JP, Bernasconi P, Vaerman JP, et al. Stimulation of secretory IgA and secretory component of immunoglobulins in small intestine of rats treated with Saccharomyces boulardii. Dig Dis Sci. 1990;35(2):251-6.

43. Buts JP, De Keyser N, De Raedemaeker L. Saccharomyces boulardii enhances rat intestinal enzyme expression by endoluminal release of polyamines. Pediatr Res. 1994;36(4):522-7.