Many products that claim to support gluten digestion might not be fully doing the job!
Celiac and other types of gluten sensitivity
Celiac disease (CD) is the most studied and broadly recognized disease associated with the immune reaction to gluten consumption. Celiac disease is a multifactorial disease characterized by an inflammatory response to ingested gluten in the small intestine. Gluten is a protein found in wheat, rye, spelt, and barley, and is resistant to degradation by enzymes that more easily digest other proteins. In those with genetic susceptibility, gluten elicits an immune response that wreaks havoc in the digestive tract, and beyond.
However, other types of gluten sensitivity also exist. These conditions are broadly known as Non-Celiac Gluten Sensitivity (NCGS). The immune response to gluten proteins is different in this condition, but is being increasingly studied, as is evidenced in the following quote from the journal Nutrients:
“The publications on CD doubled every 20 years from approximately 2500 in the period of 1950–70 to ~9500 in the period 1991–2010, with already more than 2000 papers published between 2011 and 2013. Conversely, there were almost no scientific reports on NCGS before 1970 and only a handful number of papers have been published ever since, most of them after 2005. The increase interest in NCGS is testified by the decreased NCGS/CD publication ratio that dropped from 1:438 in the period 1950–70 to 1:10 in the period 2010–13.”
The diagnosis of NCGS must exclude the possibility of celiac disease and wheat allergy. Beyond this, it is characterized by symptoms that occur after gluten ingestion, with improvements within hours or days after gluten elimination, and relapse after eating gluten again. Individuals with NCGS commonly report a personal history of food allergy and allergic conditions such as allergic rhinitis, asthma, and/or eczema in infancy. Digestive symptoms may manifest similar to irritable bowel syndrome, and relationships have also been suggested between NCGS and neuropsychiatric disorders, particularly autism, schizophrenia, and a vulnerability for dementia. Changes in the normal collection of microbes in the gut in those with NCGS may contribute to gut inflammation, diarrhea, constipation, abdominal pain, metabolic problems, and altered peripheral immune and neuro-immune communication. There is currently no definitive test for NCGS.
Troubleshooting accidental gluten consumption
In the instance of both celiac disease and NCGS the most effective approach for the resolution of symptoms and related complications is the dietary elimination of gluten from the diet. However, such a diet is often difficult to maintain due the frequent usage of gluten in the food industry, and inadvertent trace exposures are common in settings such as restaurants or other food preparation facilities where strict policies to avoid gluten cross-contamination are not imposed.
In settings where trace amounts of gluten may be accidentally ingested, there are thankfully some enzymes that may be of service in mitigating the potential damage. These include protease, which can help digest glutenin, the first protein in the gluten-matrix, and dipeptidyl peptidase IV (DDP IV), an exo-peptidase enzyme involved in the degradation of gliadin. On its own, however, DPP IV has a limited effect and only partially breaks down gluten peptides, as it only can break down bonds at the ends of the larger molecule. Several gluten-specific digestive enzyme combinations containing high amounts of DDP IV with other proteases have been shown to only partly neutralize gluten proteins, permitting fragments known to contribute to the immune response to pass through unscathed. These combinations are not likely to be beneficial for either coeliac disease or NCGS because the enzymes necessary to break down the internal peptide bonds are missing. An additional enzyme that is able to break down the internal peptide bonds in gluten has been isolated and shown to effectively degrade gluten and be well tolerated in individuals with celiac disease.,,
An additional enzyme that is able to break down the internal peptide bonds in gluten has been isolated and shown to effectively degrade gluten and be well tolerated in individuals with celiac disease.
A decrease in intestinal DPP IV activity has been shown to correlate with more damage to the gut lining in patients with celiac disease and other malabsorption syndromes. The level and activity of other digestive enzymes found on the gut brush border is also decreased with the type of digestive damage seen in celiac disease and digestive infections, including small intestinal bacterial overgrowth (SIBO).,,,
For individuals with celiac disease, NCGS, and other digestive disorders which can lead to pancreatic insufficiency, a comprehensive digestive enzyme including both exo- and endo-peptidase for the digestion of gluten, as well as other enzymes including lipase, lactase, amylase, and protease for support in digestion of carbohydrates, fats and proteins may often be beneficial.
Click here to see References
 Kagnoff MF. Celiac disease. A gastrointestinal disease with environmental, genetic, and immunologic components. Gastroenterol Clin North Am. 1992 Jun;21(2):405-25.
 Ciccocioppo R, et al. The immune recognition of gluten in coeliac disease. Clin Exp Immunol. 2005 Jun;140(3):408-16.
 Catassi C, et al. Non-Celiac Gluten sensitivity: the new frontier of gluten related disorders. Nutrients. 2013 Sep 26;5(10):3839-53.
 Mansueto P, et al. Non-celiac gluten sensitivity: literature review. J Am Coll Nutr. 2014;33(1):39-54.
 Daulatzai MA. Non-celiac gluten sensitivity triggers gut dysbiosis, neuroinflammation, gut-brain axis dysfunction, and vulnerability for dementia. CNS Neurol Disord Drug Targets. 2015;14(1):110-31.
 Gopper SS, et al. Advanced Nutrition and Human Metabolism. 5th Ed, 2009.
 Thoma R, et al. Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV. Structure. 2003 Aug;11(8):947-59.
 Janssen G, et al. Ineffective degradation of immunogenic gluten epitopes by currently available digestive enzyme supplements. PLoS One. 2015 Jun 1;10(6):e0128065.
 Tack GJ, et al. Consumption of gluten with gluten-degrading enzyme by celiac patients: a pilot-study. World J Gastroenterol. 2013 Sep 21;19(35):5837-47.
 Mitea C, et al. Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model: implications for coeliac disease. Gut. 2008 Jan;57(1):25-32. Epub 2007 May 9.
 Montserrat V, et al. Influence of dietary components on Aspergillus niger prolyl endoprotease mediated gluten degradation. Food Chem. 2015 May 1;174:440-5.
 Detel D, Persić M, Varljen J. Serum and intestinal dipeptidyl peptidase IV (DPP IV/CD26) activity in children with celiac disease. J Pediatr Gastroenterol Nutr. 2007 Jul;45(1):65-70.
 Prasad KK, et al. Brush border enzyme activities in relation to histological lesion in pediatric celiac disease. J Gastroenterol Hepatol. 2008 Aug;23(8 Pt 2):e348-52.
 Taylor CJ, et al. Ultrastructural and biochemical changes in human jejunal mucosa associated with enteropathogenic Escherichia coli (0111) infection. J Pediatr Gastroenterol Nutr. 1986 Jan;5(1):70-3.
 Agus SG, et al. Acute infectious nonbacterial gastroenteritis: intestinal histopathology. Histologic and enzymatic alterations during illness produced by the Norwalk agent in man. Ann Intern Med. 1973 Jul;79(1):18-25.
 Welsh JD, et al. Intestinal disaccharidase and alkaline phosphatase activity in giardiasis. J Pediatr Gastroenterol Nutr. 1984;3(1):37-40.