Complete Digestion of Dairy Proteins

Digest. Absorb. Relief.

ProteaseCW™ is a proprietary blend of acid-resistant, non-animal derived digestive enzymes uniquely formulated to provide substantial proteolytic activity aimed at breaking down the hard-to-digest casein and whey proteins found in dairy foods and protein supplements.*

  • Breaks Down Casein & Whey Fast*
  • Helps Reduce Gas, Bloating, and Occasional GI Upset*
  • Releases Essential Amino Acids and Bioactive Peptides*

The Real Dairy Issue

Dairy foods and many protein supplements contain casein and/or whey, proteins the body has difficulty digesting that often results in not only a significant loss in nutritional value but also gastrointestinal discomfort and, in some cases, serious immune responses. There are large amounts of protein (primarily casein and whey) in dairy products such as milk, cheese, yogurt, and ice cream as well as in popular protein powders and meal replacement drinks. This dairy protein provides essential amino acids, particularly tryptophan, lysine, cysteine and branched chain amino acids, for use by the body in optimizing health.[1,2] Research has also discovered properly-digested dairy protein produces a wide variety of peptides, some with immune-modulating, antibacterial, antiviral, antihypertensive, apoptosis, opioid, mineral-binding and/or antioxidant bioactivities.[3] The digestibility of dairy protein determines not only the nutritional value of the food or supplement but also the body’s ability to tolerate it.[2,4] Intolerances to casein and/or whey, which are often mistaken for an intolerance to dairy lactose, can cause gastrointestinal distress such as bloating, nausea, abdominal pain, and/or diarrhea and, in some cases, more serious immune responses.[5]

How it Works


Targets Casein’s Proline “Knots”

Targets Casein’s Proline “Knots”

A calibrated mix of endo- and exopeptidases with substantial DPP-IV activity attacks the hard-to-cleave X-Pro bonds in casein’s proline-dense segments. These regions tend to fold and cross-link, making them resistant to gastric, pancreatic, and brush-border enzymes; ProteaseCW™ helps open these structures to yield smaller, more manageable peptides [7–10].*

Opens Whey’s Tight Globules

Opens Whey’s Tight Globules

Whey proteins (β-lactoglobulins, α-lactalbumins) are pepsin-resistant due to compact globular folding and stabilizing disulfide bonds. ProteaseCW’s broad bond-specificity across acidic pH expands cleavage beyond pepsin’s limited sites, improving breakdown of these stubborn fractions in the stomach phase [11–14].*

Starts Early to Reduce Reactivity

Starts Early to Reduce Reactivity

Because the blend is effective under acidic conditions, hydrolysis begins immediately upon gastric entry and continues before casein/whey contact the intestinal mucosa helping limit exposure to intact, more antigenic fragments that can drive intolerance and immune activation. Early, pre-intestinal cleavage supports comfort and tolerance downstream [5,15–16].*

The ProteaseCW™ Difference

ProteaseCW™ is purpose-built for dairy proteins (casein and whey) not just lactose so you get more nutrition with fewer intolerance triggers. Its calibrated mix of endo- and exopeptidases with substantial DPP-IV activity cleaves hard-to-digest proline-rich motifs in casein that commonly evade gastric, pancreatic, and brush-border enzymes [7–10]. It also opens pepsin-resistant whey fractions (β-lactoglobulins, α-lactalbumins) whose compact folds and disulfide bonds limit pepsin access [11–12, 2, 13–14]. Because the enzymes are acid-stable, hydrolysis begins immediately in the stomach, reducing intact dairy proteins before they contact the intestinal mucosa—helping limit immune stimulation and intolerance-related discomfort downstream [5,15–16]. Multi-site cleavage across a broad pH range (acid/neutral/alkaline proteases) releases essential amino acids and bioactive peptides, enhancing the usable value of dairy foods and protein supplements [2,4]. The enzymes are highly purified and produced via Non-GMO microbial fermentation with a long history of safe and effective use.*

Approach What It Targets Where It Works Key Takeaways
ProteaseCW™ Casein + Whey (Broad Bond Specificity; DPP-IV) Acidic Gastric pH → Ongoing Comprehensive Dairy Protein Hydrolysis
Lactase-Only Lactose (sugar), Not Protein Mainly Intestinal Helps Lactose Intolerance, Not Casein/Whey
Generic Protease Limited Specificity; Often Neutral pH Less Active in Stomach Acid Incomplete Breakdown of Dairy Proteins

Why ProteaseCW™

ProteaseCW™ is precisely-formulated to assist the body’s own digestive enzymes in thoroughly breaking down dairy protein (casein and whey), releasing essential amino acids and beneficial bioactive peptides as well as minimizing intolerance to dairy protein. Avoiding dairy foods altogether may seem like an easy solution to the problem. However, casein and/or whey 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.[1,6]*

  • Stomach-First Breakdown: Acid-stable endo/exopeptidases (incl. DPP-IV activity) rapidly cleave proline-rich casein and pepsin-resistant whey before they hit the intestine.*
  • Better Tolerance, Less Upset: Pre-intestinal hydrolysis reduces intact dairy fragments that can trigger bloating, gas, and occasional GI discomfort—going beyond lactase-only fixes.*
  • Maximize Dairy Nutrition: Broad pH performance releases essential amino acids and beneficial bioactive peptides; clean, non-GMO microbial enzymes for consistent results.*

References


  1. Layman DK, Lönnerdal B, Fernstrom JD. Applications for α-lactalbumin in human nutrition. Nutr Rev. 2018 Jun; 76(6): 444–460.
  2. Shrestha AK. Scientific Background of Dairy Protein Digestibility: A Review. J. Food Sci. Technol. Nepal. 2012; 7: 1-8.
  3. Kamau SM, Cheison SC, Chen W, LiuXM, Lu Alpha‐Lactalbumin: Its Production Technologies and Bioactive Peptides. Comprehensive Reviews in Food Science and Food Safety. 2010 Feb 16; 9(2):197-212.
  4. Schmidt DG, Meijer RJGM, Slangen CJ,Beresteijn ECH. 1995. Raising the pH of the pepsin‐catalysed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates. Clin Exp Allergy25:1007–17.
  5. Yu W, Hussey-Freeland DM, Nadeau KC. Food allergy: immune mechanisms, diagnosis and immunotherapy. Nat Rev Immunol. 2016 Dec; 16(12): 751–765.
  6. Matoori S, Fuhrmann G, Leroux JC. Celiac disease: A challenging disease for pharmaceutical scientists. Pharm Res 2013; 30:619-26.
  7. Kreil G, et al. Studies on the enzymatic degradation of beta-casomorphins. Life Sci. 1983;33 Suppl 1:137-140.
  8. Vermeirssen V, Camp JV, Verstraete W. 2004. Bioavailability of angiotensin I converting enzyme inhibitory peptides. Br J Nutr92:357–66.
  9. Sollid LM, Khosla C. Novel therapies for coeliac disease. J Intern Med. 2011 Jun;269(6):604-13.
  10. 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.
  11. Almaas H, Berner V, Holm H, Langsrud T,Vegarud GE. 2008. Degradation of whey from caprine milk by human proteolytic enzymes, and the resulting antibacterial effect against Listeria monocytogenes. Small Rumin Res79:11–5.
  12. Nakano T, Simatani M, Murakami Y, Sato N, Idota T. Digestibility and Absorption of Enzymatically Hydrolyzed Whey Protein. Nippon Eiyo Shokuryo Gakkaishi. 1994; 47 (3): 195-201.
  13. N’Negue MA, Miclo L, Girardet JM,Campagna S, Mollé D, Gaillard JL. 2006. Proteolysis of bovine α‐lactalbumin by thermolysin during thermal denaturation.Int Dairy J16:1157–67.
  14. Guo MR, Fox PF, Flynn A. 1995. Susceptibility of β‐lactoglobulin and sodium caseinate to proteolysis by pepsin and trypsin. J Dairy Sci78:2336–44.
  15. Asselin J, Amiot J, Gauthier SF, Mourad W, Hebert J. Immunogenicity and Allergenicity of Whey Protein Hydrolysates. J of Food Science. 1988 July; 53(4):1208-1211.
  16. Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001.