The Gluten Solution: Aspergillus Niger-Derived Enzyme May Make "Gluten-Free" Redundant - Enzyme Supplementation Reduces the Amount of Gliadin in the Duodenum by 80-90%

Can a pill simulate "gluten-free"?

The problem with gluten (if there is one, after all we are not all suffering from coeliac disease) is that its proline-peptides cannot be digested by any of the enzymes in the human intestinal tract. Therefore, the long proline-rich gluten peptides reach the small intestine intact after ingestion where they are the driving motors of coeliac disease in 1% of the population, in whom the specific amino acid sequences of such poorly digested proline-rich gluten peptides triggers an abnormal immune response.

More recently, though, studies have shown that less pronounced adverse reactions to gluten consumption can occur even in subjects who don't suffer from coeliac disease. As Salden et al. point out, "[p]resently non-coeliac gluten sensitivity has been clinically recognised as a separate condition in which neither allergic nor autoimmune mechanisms are involved" (Salden. 2015). Accordingly, the results of the latest study from the Maastricht University Medical Center are relevant for much more than just 1% of the population (West. 2003; Mäki. 2003; Fasano. 2003; Bingley. 2004).

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Now I got you curious, right? Ok, here's what the Dutch scientists did: In their randomized, double-blind, placebo-controlled, cross-over study 12 healthy volunteers attended to four test days with at least one week washout in-between. On day 2-3, a liquid low or high calorie meal (4 g gluten) with Aspergillus niger prolyl endoprotease (AN-PEP | 6.1 mL of AN-PEP corresponding with 1.600.000 Protease in a total of 100 mL water) or placebo was administered into the stomach.

Table 1: Recipe and nutritional composition of the low and high calorie test meal per 300 g portion (Salden. 2015).

Table 1 shows the composition of the meals. All test meals contained 5.2 g of gluten powder, of which 4.0 g was gluten protein (Syral, Aalst, Belgium). Encapsulated refined olive oil powder (VanaGrasa 80B; FrieslandCampina, Kievit B.V., Meppel, The Netherlands) was used as fat source for the meals and together with maltodextrin as additional energy source for the high calorie meal, and sodium caseinate (DMV, Veghel, The Netherlands) was used to match both meals for protein content. The dry meal powders were dissolved in a total volume of 300 mL tap water of 40 °C by stirring with a spoon and subsequently mixing with a Turrax (Ultra Turrax T25; IKA, Staufen, Germany). Low and high caloric meals were not blinded to the investigator.

The gastric emptying was tracked with acetaminophen and a triple-lumen catheter was used to get the gastric and duodenal samples that were used to calculate the 240-min area under the curve (AUC0–240 min) of α-gliadin concentrations.

Figure 1: Total alpha-gliadin in the duodenum (µg x min | left) and western blot showing degradation of water-insoluble gliadin over time in the stomach and duodenum in low and high calorie meals with and without AN-PEP (Salden. 2015).

As you can see in Figure 1, the addition of the Aspergillus niger prolyl endoprotease worked it's magic on the indigestible gluten peptides and reduced the amount of potentially pro-inflammatory alpha-gliadin that made it into the duodenum by 91% and 81% depending on the size of the meal. That's huge and as the scientists point out the first time that someone observed in vivo that the AN-PEP enzyme efficiently degrades gluten from a meal in the stomach of human subjects.

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Bottom line: You probably already realized why the results of the study at hand are important. If one could add sufficient amounts of AN-PEP to gluten-containing products and / or take a supplement that contains Aspergillus niger prolyl endoprotease (AN-PEP) with every gluten-containing meal, we could minimize, probably even totally prevent any pro-inflammatory effects of gluten in both coeliac patients and subjects with non-coeliac gluten intolerance.

Ok, it's questionable whether it's feasible to put a gliadin digesting enzyme into goods without impairing their quality (gluten is after all added for its ability to "glue" things together; putting AN-PEP into the dough may thus ruin it).

A pill with Aspergillus niger prolyl endoprotease (AN-PEP), on the other hand, could make the life of people who risk developing diarrhea or other symptoms of gluten intolerance whenever they eat out significantly easier... ah, and it could be big business in view of the contemporary gluten-scare, which brings me to the sponsors of the study (DSM Nutritional Products AG) who are about to use the study to advertise their AN-PEP products which have already been approved by the French Agency for Food, Environmental and Occupational Health & Safety | Comment on Facebook!

References:

• Bingley, Polly J., et al. "Undiagnosed coeliac disease at age seven: population based prospective birth cohort study." Bmj 328.7435 (2004): 322-323.
• Fasano, Alessio, et al. "Prevalence of celiac disease in at-risk and not-at-risk groups in the United States: a large multicenter study." Archives of internal medicine 163.3 (2003): 286-292.
• Mäki, Markku, et al. "Prevalence of celiac disease among children in Finland." New England Journal of Medicine 348.25 (2003): 2517-2524.
• Piper, Justin L., Gary M. Gray, and Chaitan Khosla. "Effect of prolyl endopeptidase on digestive-resistant gliadin peptides in vivo." Journal of Pharmacology and Experimental Therapeutics 311.1 (2004): 213-219.
• Salden et al. "Randomised clinical study: Aspergillus niger-derived enzyme digests gluten in the stomach of healthy volunteers." Alimentary Pharmacology and Therapeutics (2015): Accepted manuscript.
• West, J., et al. "Seroprevalence, correlates, and characteristics of undetected coeliac disease in England." Gut 52.7 (2003): 960-965.