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Targets Hard-to-Digest Gluten and Casein

ProteaseGL™ is a proprietary blend of acid-resistant, non-animal derived digestive enzymes uniquely formulated to provide substantial dipeptidyl peptidase IV (DPP-IV) and related proteolytic activity targeted at optimizing the healthy breakdown of hard-to-digest gluten and casein peptides found in grain-containing and dairy foods, respectively, helping to relieve occasional intestinal discomfort.*

The Problem

Gluten found in wheat, barley, rye and other cereal grains as well as casein found in dairy foods is difficult for the body to digest which, if not addressed, can result in serious health issues.

bowl of cereal photo

The Solution

ProteaseGL™ is a powerful combination of proteases and peptidases capable of thoroughly digesting gluten and casein.* Avoiding foods containing grains and dairy may seem like the easiest solution to gluten and casein sensitivities or intolerance. Unfortunately, ingredients derived from grains and dairy are often used for nutritional or processing purposes in other common foods, medications and dietary supplements and may not be clearly identified on the label.[7-9]

How ProteaseGL™ Works

A complex formulation of both endopeptidases and exopeptidases, ProteaseGL™ acts on a broad range of peptide bonds, with particular focus on hard-to-digest proline bonds. Laboratory research indicates the type of enzyme blend found in ProteaseGL™ promotes more complete digestion of dietary gluten and casein.[10]* This unique combination of enzymes begins its digestive action immediately upon arriving in the stomach where it survives gastric acidity, continuing to hydrolyze proline bonds before gluten or casein can damage the intestinal mucosa and stimulate an inflammatory response.* Unless a digestive product contains enzymes capable of cleaving proline bonds, it will only be able to partially breakdown gluten or casein which may, in fact, release more resistant peptides and possibly increase the risk of negative reactions in sensitive individuals. Gluteomorphins and caseomorphins are bioactive peptides formed during incomplete digestion of gluten and casein, respectively, which studies have shown can interact with opioid receptors in the brain.[11-14] Further research indicates these bioactive peptides can adversely affect the central nervous system and abnormal levels have been linked to neurological disorders including ADD/ADHD, autism and schizophrenia.[15-17] More complete digestion of dietary proteins with supplemental enzymes including proline-specific peptidases may be beneficial for these conditions.[18]*

Why ProteaseGL™

ProteaseGL™ has clinically and scientifically demonstrated the ability to not only break down the most resistant proline regions of the gluten or casein molecule but also to digest the entire gluten or casein protein chain into smaller peptides and amino acids the body can absorb and utilize to maintain health.* 

  1. Sollid LM, Khosla C. Novel therapies for coeliac disease. J Intern Med. 2011 Jun;269(6):604-13.
  2. Hausch F, Shan L, Santiago NA, Gray GM, Khosla C. Intestinal digestive resistance of immunodominant gliadin peptides. Am J Physiol Gastrointest Liver Physiol. 2002 Oct;283(4):G996-G1003.
  3. Shan L et al. Structural basis for gluten intolerance in celiac sprue. Science. 2002 Sep 27; 297(5590):2275-9.
  4. Garcia-Horsman JA. Deficient activity of mammalian prolyl oligopeptidase on the immunoactive peptide digestion in coeliac disease. Scand J Gastroenterol. 2007 May; 42(5):562-71.
  5. Matysiak-Budnik T. Alterations of the intestinal transport and processing of gliadin peptides in celiac disease. 2003 Sep; 125(3):696-707.
  6. Sapone et al. Spectrum of gluten-related disorders: consensus on new nomenclature and classification. BMC Medicine 2012; 10:13.
  7. Matoori S, Fuhrmann G, Leroux JC. Celiac disease: A challenging disease for pharmaceutical scientists. Pharm Res 2013; 30:619-26.
  8. Miletic ID, Miletic VD, Sattely-Miller EA, Schiffman SS. Identification of gliadin presence in pharmaceutical products. J Pediatr Gastroenterol Nutr. 1994 Jul;19(1):27-33.
  9. Saturni L, Ferretti G, Bacchetti T.The Gluten-Free Diet: Safety and Nutritional Quality. Nutrients. 2010 Jan; 2(.1): 16–34.
  10. Ehren J et al. A Food-Grade Enzyme Preparation with Modest Gluten Detoxification Properties. PLOS One 2009; 4(7): e6313.
  11. Fukudome S, Yoshikawa M. Opioid peptides derived from wheat gluten: their isolation and characterization. FEBS Lett. 1992 Jan 13;296(1):107-11.
  12. Huebner FRLieberman KWRubino RPWall JS. Demonstration of high opioid-like activity in isolated peptides from wheat gluten hydrolysates. 1984 Nov-Dec; 5(6):1139-47.
  13. Kreil G, et al. Studies on the enzymatic degradation of beta-casomorphins. Life Sci. 1983;33 Suppl 1:137-40.
  14. Loukas S, Varoucha D, Zioudrou C, Streaty RA, Klee Opioid activities and structures of alpha.-casein-derived exorphins. Biochemistry 1983; 22(19):4567-4573.
  15. Whiteley P et al. Gluten- and casein-free dietary intervention for autism spectrum conditions. Front Hum Neurosci. 2013 Jan 4;6:344.
  16. Reichelt KL, Tveiten D, Knivsberg AM, Brønstad G. Peptides’ role in autism with emphasis on exorphins. Microb Ecol Health Dis. 2012 Aug 24;23.
  17. Kalaydjian AE, Eaton W, Cascella N, Fasano A. The gluten connection: the association between schizophrenia and celiac disease. Acta Psychiatr Scand. 2006 Feb;113(2):82-90.
  18. Brudnak MA et al. Enzyme-based therapy for autism spectrum disorders — is it worth another look? Med Hypotheses. 2002 May; 58(5):422-8.
  19. Doumas A, Broek P, Affolter M, Monod M. Characterization of the Prolyl Dipeptidyl Peptidase Gene (dppIV) from the Koji Mold Aspergillus oryzae. Appl Environ Microbiol. 1998 Dec; 64(12): 4809–4815.
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