Targets Hard-to-Digest Gluten and Casein

Digest. Absorb. Relief.

ProteaseGL™ is a proprietary blend of acid-resistant, non-animal derived digestive enzymes uniquely formulated to provide substantial DPP-IV activity targeted at breaking down hard-to-digest gluten and casein peptides found in grain-containing/dairy foods.*

Get a Quote Why ProteaseGL™ How it Works
  • Breaks Down Gluten & Casein Fast*
  • Helps Reduce Gas, Bloating & Occasional GI Upset*
  • Releases Absorbable Peptides & Amino Acids*
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The Gluten & Caesin Challenge

Gluten in wheat, barley, rye and related grains, and casein in dairy, are unusually hard to break down and—if left unaddressed—can contribute to meaningful health burdens. Both proteins are rich in proline, a feature that promotes tight folding and helical cross-linking; these compact structures physically limit enzyme access and make the peptide chains far more resistant to normal digestion [1]. In practical terms, the body’s frontline proteases in the stomach, pancreas, and intestinal brush border often cannot fully hydrolyze these proline-dense segments, allowing larger, stubborn fragments to persist through the upper GI tract [2,3]. Susceptibility can be amplified when key brush-border proteases—especially dipeptidyl peptidase activity—are reduced, as has been observed in some individuals with gluten sensitivity; with less DPP-IV–type action available to cleave proline-containing bonds, even more intact peptides reach the intestinal surface [4]. Repeated exposure to incompletely digested gluten and casein can injure intestinal villi, diminishing absorptive surface area and disrupting barrier function—changes linked to malabsorption and inflammatory discomfort commonly described as gluten intolerance; in genetically susceptible people, ongoing exposure may help drive a systemic immune response consistent with celiac disease [5,6].*

How it Works


Gastric-Phase Proline Bond Cleavage

A calibrated mix of endo- and exopeptidases targets a broad range of peptide bonds—with emphasis on hard-to-digest proline bonds—promoting more complete breakdown of dietary gluten and casein. The blend survives gastric acidity and begins working immediately in the stomach, hydrolyzing proline-rich segments before they can irritate mucosa and escalate inflammatory responses [10]*. (Formulas lacking proline-cleaving activity tend to only partially digest these proteins, leaving resistant fragments behind.)*

Limits Problem Peptides to Support Neuro Comfort

Incomplete digestion can yield gluteomorphins and caseomorphins, bioactive peptides that interact with opioid receptors in the brain [11–14]. Elevated levels have been linked with adverse CNS effects and neurological conditions, including ADD/ADHD, autism, and schizophrenia [15–17]. By driving fuller protein hydrolysis—especially via proline-specific peptidases—the approach may help reduce these fragments and support balanced responses [18]*.

The ProteaseGL™ Difference

ProteaseGL™ has clinically and scientifically demonstrated the capacity to tackle the most proline-dense regions of gluten and casein while also driving end-to-end proteolysis—reducing whole proteins into smaller peptides and free amino acids that are readily absorbed and used to maintain health. Its highly purified proteolytic enzymes are produced via fermentation of non-genetically modified microorganisms (primarily Aspergillus species) with a long, established record of safe use, yielding a consistent, clean enzyme spectrum. To verify the blend’s proline-targeting capability, ProteaseGL™ is assayed using the DPP-IV method, which directly measures prolyl dipeptidyl peptidase activity responsible for cleaving difficult X-Pro bonds in gluten/casein peptides [19]. Complementing this, the HUT assay provides a general measure of total proteolytic strength under acidic, stomach-like conditions, confirming the blend’s ability to open up large protein structures so that resistant proline sites become more accessible and are subsequently hydrolyzed.* Together, these orthogonal assays (DPP-IV for specificity and HUT for overall gastric-phase potency) support the real-world objective: more complete breakdown of gluten and casein before they reach the intestinal mucosa, promoting comfortable digestion and efficient nutrient uptake [19].*

Approach What It Targets Where It Works Key Takeaways
ProteaseGL™ Gluten (gliadin; proline-rich) + Casein (proline-rich) Acidic Gastric pH → Ongoing Through Small Intestine Comprehensive Gluten & Casein Hydrolysis Into Small Peptides/Amino Acids
DPP-IV Only Proline Bonds Only | Limited Action on Non-Partialroline regions of gluten/casein Less Active in Stomach Acid | Better Near Neutral pH Partial Digestion | Residual Immunogenic Peptides Remain
Generic Protease Broad Protein Cleavage but Poor Proline Specificity | Not Optimized for Gluten/Casein Often Neutral pH | Reduced Activity in Acidic Stomach Incomplete Breakdown of Gluten/Casein Proteins

ProteaseGL™ Assays



A sample of ProteaseGL™ (.0685g) was diluted in pH 4.5 acetate buffer. A portion of this (950µL) was added to a solution (50µL) of purified gliadin substrate. The reaction was allowed to shake in a 37 degree water bath for 45 minutes, as this is the average time food starts to move from the stomach to the intestines. The reaction was then boiled for fifteen minutes to stop the reaction from further degradation and allowed to cool for five minutes. The sample was then run on the VeratoxGliadin R5 ELISA kit and read on a micro-plate reader at 655nm. The percent degradation was determined using a standard curve.

Why ProteaseGL™

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]*

  • Comprehensive Protein Breakdown: Broad-spectrum endo/exopeptidases with strong DPP-IV activity hydrolyze gluten and casein—including proline-rich regions—reducing residual peptides (e.g., gluteomorphins/caseomorphins) and supporting nutrient absorption.*
  • Active Where It Counts: Acid-resistant enzymes start working in the stomach and continue through the small intestine, helping protect the mucosa and relieve occasional gas, bloating, and discomfort from hidden gluten/dairy.*
  • Proven & Consistent: Non-animal, Non-GMO microbial enzymes with potency verified by DPP-IV and HUT assays; clinically/scientifically supported activity under gastric conditions.*

References


  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 FR, Lieberman KW, Rubino RP, Wall 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.