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Found 8 results

  1. GliadinX is a dietary supplement with the highest concentration of AN-PEP, Prolyl Endopeptidase (Aspergillus Niger), the most effective enzyme proven to break down gluten in the stomach. This high potency enzyme formulation is specifically designed to break down gliadin, and unlike other enzyme formulas that claim to do the same, there is a growing body of research that backs up the effectiveness of GliadinX (see Sources below). GliadinX does not prevent and is not a cure for celiac disease, however, extensive scientific research has been conducted at multiple medical centers which has shown that it effectively breaks down gliadin into small, harmless fragments before it can reach the small intestine. GliadinX is perfect for celiacs who still want to eat outside of their home, and not have to worry about cross-contamination, and for those who are gluten sensitive and wish to continue eating gluten. For more info visit their site. Sources: Extra-Intestinal Manifestation of Celiac Disease in Children. Nutrients 2018, 10(6), 755; doi:10.3390/nu10060755 Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model Enzymatic gluten detoxification: the proof of the pudding is in the eating! Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease Degradation of gluten in wheat bran and bread drink by means of a proline-specific peptidase
  2. Celiac.com 12/09/2017 - For those of you who haven't yet heard about GliadinX, it is a dietary supplement with the highest concentration of AN-PEP, Prolyl Endopeptidase (Aspergillus Niger), and, unlike other enzymes, these have been shown in studies to break down gluten in the stomach. I've been using them regularly for months, and I tend to take them whenever I eat out, or eat at a friend's house, so basically whenever I don't have control over my food's preparation. Since I began doing this I haven't had any incidents of upset stomach, which are my typical symptoms if I get any cross contamination. However, it is hard to prove a negative...after all, perhaps I haven't had any issues because all of the food I ate was 100% gluten-free...right? I will now describe a recent glutening incident that involved none other than my Mother, who visited us this past Thanksgiving. How this could happen in my home, after all I'm the owner of Celiac.com, is an embarrassing but true story which I will share here in the hope that it will help you avoid my errors, and perhaps give you a way to recover should something similar ever happen. My brother brought over three pies for Thanksgiving dessert, one was a gluten-free apple pie, and the other two were pumpkin pies: one was gluten-free, but the other was not. What could go wrong, right? My brother's reasoning for bringing a non gluten-free pie into my house was pretty basic: several of the guests were not on a gluten-free diet, so he wanted to offer them what they were used to. What you need to know about my Mother is that she's very gluten sensitive. A tiny amount of gluten leaves her wrecked for days. I think you probably know where I'm going here, but basically everyone was busy socializing, eating, or cleaning while dessert was being served, and a friend grabbed a piece of the gluten-containing pumpkin pie (she assumed that if it was in MY house it was gluten-free) and handed it to my Mother. After she swallowed two bites we realized the mistake, but it was too late. My Mother had the look of horror on her face as she realized that the rest of her trip to California was probably ruined. I immediately flew into action and gave her several capsules of GliadinX, which she took with lots of water. We carried on with the evening, and I checked in with her over the next couple of hours. Amazingly she didn't have any noticeable symptoms or issues, but she was still certain that they were coming, and that she wouldn't get any sleep and would feel horrible the next day. Remarkably, none of her worries came true. She slept fine, and woke up feeling great. We were both amazed because any past similar incidents always ended badly for her. Suffice it to say that my Mother now keeps a bottle of GliadinX with her all the time...just in case! --by Scott Adams Many people have asked Celiac.com how they can order this product, so we've included a "Buy Now" link below to order them directly from the manufacturer: Sources: Scientific publications on AN-PEP enzymes: Extra-Intestinal Manifestation of Celiac Disease in Children. Nutrients 2018, 10(6), 755; doi:10.3390/nu10060755 Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model Enzymatic gluten detoxification: the proof of the pudding is in the eating! Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease Degradation of gluten in wheat bran and bread drink by means of a proline-specific peptidase
  3. GliadinX is a dietary supplement with the highest concentration of AN-PEP, Prolyl Endopeptidase (Aspergillus Niger), the most effective enzyme proven to break down gluten in the stomach. This high potency enzyme formulation is specifically designed to break down gliadin, and unlike other enzyme formulas that claim to do the same, there is a growing body of research that backs up the effectiveness of GliadinX (see Sources below). GliadinX does not prevent and is not a cure for celiac disease, however, extensive scientific research has been conducted at multiple medical centers which has shown that it effectively breaks down gliadin into small, harmless fragments before it can reach the small intestine. GliadinX is perfect for celiacs who still want to eat outside of their home, and not have to worry about cross-contamination, and for those who are gluten sensitive and wish to continue eating gluten. The quote below was made by Dr. Stefano Guandalini, Department of Pediatrics, Section of Gastroenterology, Hepatology and Nutrition, University of Chicago Celiac Disease Center-Comer Children’s Hospital, Chicago, IL, and was published in Nutrients 2018, 10(6), 755: "12. Treatment of the Extra-Intestinal Manifestations of CD the only one that is currently on the market is the gluten-specific enzyme, GliadinX (AN-PEP). Unfortunately, it is only capable of detoxifying 0.2 g of gluten or roughly that of 1/8 of a slice of gluten-containing bread. For this reason, it should only be used as an adjunct to the GFD when there are concerns for accidental gluten contamination and in an effort to ameliorate symptoms, not as a replacement for the GFD." Many people have asked Celiac.com how they can order this product, so we've included a "Buy Now" link below to order them directly from the manufacturer: Sources: Scientific publications on AN-PEP enzymes: Extra-Intestinal Manifestation of Celiac Disease in Children. Nutrients 2018, 10(6), 755; doi:10.3390/nu10060755 Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model Enzymatic gluten detoxification: the proof of the pudding is in the eating! Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease Degradation of gluten in wheat bran and bread drink by means of a proline-specific peptidase
  4. Celiac.com 09/24/2018 - A team of researchers recently set out to investigate the degradation of gluten in rye sourdough products by means of a proline-specific peptidase. The research team included Theresa Walter, Herbert Wieser, and Peter Koehler, with the Deutsche Forschungsanstalt für Lebensmittelchemie, Leibniz Institut in Freising, Germany. Their team monitored gluten content of rye sourdough during fermentation using competitive ELISA based on the R5 antibody. The team noted a decrease in gluten over time, but found that even prolonged fermentation did not bring gluten levels below 20 ppm requirement for gluten-free foods. Interestingly, they did find that Aspergillus niger prolyl endopeptidase (AN-PEP) extensively degraded gluten concentrations of up to 80,000 mg/kg in rye flour, rye sourdough, and sourdough starter under specific temperatures and pH values. Nor did the enzyme inactivate the microorganisms in the sourdough starter. Gluten-free rye flour alone or in combination with sourdough starter was used to produce gluten-free bread, which the team then assessed for its sensory characteristics. Whereas gluten-free sourdough bread lacked any of the favorable qualities of conventional rye bread, the replacement of sourdough by egg proteins yielded gluten-free bread comparable to the conventional rye, and with better qualities than bread made with naturally gluten-free ingredients. This study demonstrates the feasibility of using ANPEP treatment to produce high-quality gluten-free sourdough bread from originally gluten-containing cereals, such as rye. Rye products rendered gluten-free in this manner have the potential to increase the choice of high-quality foods for celiac patients. Source: European Food Research and TechnologyMarch 2015, Volume 240, Issue 3, pp 517–524
  5. Celiac.com 06/26/2017 - Designed to reduce or eliminate symptoms of gluten contamination in gluten-sensitive individuals, the product known as AN-PEP, marketed in the U.S. as Tolerase G, is a prolyl endoprotease enzyme, derived from Aspergillus niger, that has shown promise in breaking down gluten proteins. The latest news comes in the form of a small study that shows the enzyme to be effective in the stomach itself, where harshly acidic conditions render many enzymes ineffective. Speaking to an audience at Digestive Disease Week (DDW) 2017, lead investigator Julia König, PhD, of Sweden's Örebro University, said that the enzyme was special, because…[t]here are a lot of enzymes on the market, but this functions in the stomach where the pH is acidic. Often enzymes don't work in this environment." König was also quick to caution that "you cannot use this enzyme to treat or prevent celiac disease." The enzyme is not intended to replace a gluten-free diet for celiac patients. The enzyme is designed to provide some protection against cross-contamination for people with gluten-sensitivity by breaking down modest amounts of gluten to reduce or prevent adverse immune reaction. A previous study showed that AN-PEP breaks down gluten after an intra-gastrically infused liquid meal in healthy volunteers (Aliment Pharmacol Ther. 2015;42:273-285). In the latest randomized placebo-controlled crossover study, Dr König and her colleagues assessed the ability of AN-PEP to degrade gluten after a normal meal in people with gluten sensitivity. The research team looked at 18 people with self-reported gluten sensitivity, and with no confirmation of celiac disease. On three separate visits, investigators collected gastric and duodenal aspirates with a multilumen nasoduodenal-feeding catheter. Participants then consumed a porridge containing gluten, approximately 0.5 g, in the form of two crumbled wheat cookies. They also consumed a tablet containing AN-PEP at either 160,000 PPi or 80,000 PPi), or placebo. Investigators collected stomach and duodenal aspirates over the following 3 hours. In both the high- and low-dose AN-PEP groups, gluten concentrations in the stomach and in the duodenum were substantially lower than in the placebo group. This study shows that AN-PEP does break down gluten in the stomach, where many enzymes fail. If successfully tested and commercially released, AN-PEP could help people with gluten sensitivity, including those with celiac disease, to reduce or eliminate symptoms associated with casual gluten contamination. Source: Medscape
  6. Celiac.com 10/23/2015 - Just as I finished writing about the failure of current commercial enzymes to effectively degrade gluten, an interesting study on another enzyme suggests that there may be help on the horizon, at least for people without celiac disease. According to the latest press release, in lab conditions, aspergillus niger prolyl endoprotease (AN-PEP) efficiently degrades gluten molecules into non-immunogenic peptides. But so what? If AN-PEP is to be effective in people with celiac disease or gluten-sensitivity, which would seem to be the whole point of an anti-gluten enzyme, it must effectively digest gluten in "non-healthy" subjects. A team of researchers recently set out to assess AN-PEP on gluten degradation in a low and high calorie meal in healthy subjects. The research team included B.N. Salden, V. Monserrat, F.J. Troost, M.J. Bruins, L. Edens, R. Bartholomé, G.R. Haenen, B. Winkens, F. Koning, A.A. Masclee. They are variously affiliated with the Division of Gastroenterology-Hepatology in the Department of Internal Medicine at NUTRIM, Maastricht University Medical Center, Maastricht, the Department of Immunohematology and Blood Transfusion at Leiden University Medical Centre in Leiden, the DSM Biotechnology Centre, Delft, the Department of Pharmacology and Toxicology, CARIM, at Maastricht University in Maastricht, and with the Department of Methodology and Statistics, CAPHRI, Maastricht University Medical Center in Maastricht, all in The Netherlands. The team conducted a randomized, double-blind, placebo-controlled, cross-over study in which 12 healthy volunteers attended to four test days. Each volunteer received a liquid low or high calorie meal (4 g gluten) with AN-PEP or placebo administered into the stomach. Using a triple-lumen catheter the team was able to sample gastric and duodenal aspirates, as polyethylene glycol (PEG)-3350 was continuously infused. Acetaminophen in the meals tracked gastric emptying time. The team used gastric and duodenal samples to calculate 240-min area under the curve (AUC0-240 min ) of α-gliadin concentrations. The team calculated absolute α-gliadin AUC0-240 min using duodenal PEG-3350 concentrations. The teams data showed that AN-PEP lowered α-gliadin concentration AUC0-240 min, compared to placebo, from low and high calorie meals in stomach (low: 35 vs. 389 μg × min/mL; high: 53 vs. 386 μg × min/mL; P < 0.001) and duodenum (low: 7 vs. 168 μg × min/mL; high: 4 vs. 32 μg × min/mL; P < 0.001) and absolute α-gliadin AUC0-240 min in the duodenum from low (2813 vs. 31 952 μg × min; P < 0.001) and high (2553 vs. 13 095 μg × min; P = 0.013) calorie meals. In the placebo group, the high compared to low calorie meal slowed gastric emptying and lowered the duodenal α-gliadin concentration AUC0-240 min (32 vs. 168 μg × min/mL; P = 0.001). These results confirm that AN-PEP significantly enhanced gluten digestion in the stomach of healthy volunteers, while increasing caloric density prolonged gastric residence time of the meal. According to the authors, these results suggest that AN-PEP shows promise as an anti-gluten digestive enzyme for people with celiac disease, but further study is clearly needed. Still, the fact that AN-PEP can effectively break down gluten in the stomach of healthy volunteers is a good start, but it means little if AN-PEP can’t do the same in people with celiac disease, which remains to be seen. Stay tuned for more developments. Source: Aliment Pharmacol Ther. 2015 Aug;42(3):273-85. doi: 10.1111/apt.13266. Epub 2015 Jun 4.
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