Promotes Complete Digestion of Dairy Proteins
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, helping to enhance its nutritional value and relieve the gastrointestinal discomfort associated with dairy intolerance.*
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.
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]
How ProteaseCW™ Works
A complex blend of both endopeptidases and exopeptidases, ProteaseCW™ helps maximize the digestion of casein and whey proteins found in dairy foods and many high protein supplements.* Casein contains amino acid sequences that are unusually high in the amino acid, proline. These proline-dense regions exhibit structural features that cause folding and helical cross-linking of the protein preventing efficient hydrolysis by the body’s gastric, pancreatic and intestinal brush border proteases.[8,9] The peptidases found in ProteaseCW™ exhibit substantial DPP-IV activity capable of hydrolyzing the difficult proline bonds in casein. The other major dairy protein, whey, primarily contains beta-lactoglobulins and alpha-lactalbumins which are resistant to hydrolysis by gastric pepsin.[11,12] Their compact globular structure and numerous disulfide bonds hinders easy access to the protein sites specific to pepsin action.[2,13,14] The unique blend of proteases in ProteaseCW™ exhibits a wide range of bond specificity at various pH levels so it is capable of optimal effectiveness in the acidic conditions of the stomach. These proteases begin their digestive action immediately upon arriving in the stomach, continuing to hydrolyze whey and casein before it reaches the intestinal mucosa where it can stimulate an inflammatory immune response.[5,15,16]*
ProteaseCW™is exceptionally effective at breaking down casein and whey, providing the body with more nutrition from dairy foods and protein supplements while lowering the risk of dairy protein intolerance.* The powerful combination of highly purified enzymes found in ProteaseCW™ are concentrated from the fermentation of non-genetically modified microorganisms, primarily Aspergillus species with a long history of safe use. This unique blend provides the right proportions of acid-stable, neutral and alkaline proteases and peptidases specifically chosen for their combined ability to efficiently cleave dairy protein at multiple bond locations yielding smaller peptides and single amino acids.
- Layman DK, Lönnerdal B, Fernstrom JD. Applications for α-lactalbumin in human nutrition. Nutr Rev. 2018 Jun; 76(6): 444–460.
- Shrestha AK. Scientific Background of Dairy Protein Digestibility: A Review. J. Food Sci. Technol. Nepal. 2012; 7: 1-8.
- Yu W, Hussey-Freeland DM, Nadeau KC. Food allergy: immune mechanisms, diagnosis and immunotherapy. Nat Rev Immunol. 2016 Dec; 16(12): 751–765.
- Matoori S, Fuhrmann G, Leroux JC. Celiac disease: A challenging disease for pharmaceutical scientists. Pharm Res 2013; 30:619-26.
- Kreil G, et al. Studies on the enzymatic degradation of beta-casomorphins. Life Sci. 1983;33 Suppl 1:137-140.
- Vermeirssen V, Camp JV, Verstraete W. 2004. Bioavailability of angiotensin I converting enzyme inhibitory peptides. Br J Nutr92:357–66.
- Sollid LM, Khosla C. Novel therapies for coeliac disease. J Intern Med. 2011 Jun;269(6):604-13.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001.