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Found 20 results

  1. Celiac.com Sponsor: Banner

    ZYGLUTEN: A Potent Multi-functional Digestive Complex

    Celiac.com 12/01/2018 - ZYGLUTEN is a targeted blend of enzymes, helpful microbes and botanicals designed to support gut-health via complete digestion of a meal containing even problematic foods. It completes most, if not all, of digestion before food leaves the stomach to prevent symptoms like GAS / BLOATING / ABDOMINAL PAIN / DIARRHEA. Twenty-two potent & diverse enzymes, packed at high loading in a tapioca capsule hydrolyze all types of foods containing even gluten/lactose/ FODMAPS/Cross- Reactors before they can cause problems in the gut. Unique microbes kill pathogens in gut and support management of issues like Irritable Bowel Syndrome, Acid Reflux and Leaky Gut. Botanicals turmeric and ginger help reduce inflammation. ZYGLUTEN was developed because Gluten-free diet and other products were not helping suffering consumers, RELIABLY. WHY MULTI-FUNCTIONAL Because root cause of gut health problems is not one but four, as stated below: Undigested food in parts of intestines where it should not be. Intolerance to GLUTEN / LACTOSE / FODMAPS / CROSS-REACTORS. Overgrowth of bad bacteria in gut flora. Inflammation in gut A word regarding root cause (1): Undigested food in some parts of the intestines can enable undesired fermentation producing gas/bloating/abdominal pain/toxins which can lead to infections/inflammation. Effect of root causes(2,3,4) is well known. ZYGLUTEN is multi-functional because its ingredients simultaneously attack all four root-causes. Other products (most are mono-functional) and gluten-free foods can help with one root cause, that too partially sometimes. POTENT GROUP OF ENZYMES In order to avoid ill effects of indigestion, it is critical that the whole meal, especially problematic components, are hydrolyzed before food leaves the stomach. All "culprits" (Gluten, Lactose, FODMAPS, Cross-Reactors) in food are difficult to digest because they are surrounded by a protective "armor" formed via their complexation (hydrogen bonds, Vander Walls forces, non-covalent interactions) with starches, fats, fibers in food. The 22 potent enzymes in ZYGLUTEN are from all families (proteases, lipases, carbohydrases, amylases, cellulases), containing endo as well as exo enzymes, known as well as enzymes that have not been even discovered yet. The proprietary combination of enzymes breaks the armor and completes the digestion in < 60 minutes (means before food leaves stomach). This is shown in graph below using gluten as a marker for % digestion completed. Gluten was selected as marker because it is so difficult to hydrolyze that if it is digested it means everything else is also. In summary, the unique, diverse, fast-acting and potent enzymes along with microbes and herbs packed at a high loading in a tapioca capsule probably makes ZYGLUTEN the most potent and probably the only multi-functional Digestive Complex in the market. UNIQUE MICROBES Helpful microbes in ZYGLUTEN are Lactococcus Lactis subspecies Lactis and Lactococcus Lactis subspecies Cremoris. They kill pathogens(2,10,11,12) in gut and thereby control overgrowth of bad bacteria in the "gut flora/micro-biome". They are also anti-inflammatory(2,3,4,5,11) and safe(5) (used in cheese making(9) industry for hundreds of years). QUICK DISSOLVING TAPIOCA CAPSULE ZYGLUTEN capsule is made of tapioca which dissolves in about 2 minutes in stomach environment vs about 20 minutes for gelatin capsule. This allows 45% longer time for enzymes in ZYGLUTEN to convert food/culprits into nutrients in the stomach, increasing the product effectiveness further. ADDITIONAL HELPFUL INGREDIENTS Both, microbes and the botanical ingredients (Turmeric & Ginger), being anti-inflammatory(7,8,9) implies even higher level of gut health support. ZYGLUTEN DIFFERENTIATORS More enzymes (22) at a higher potency, diversity & loading. Quick dissolving tapioca capsule (2 minutes vs 20) Helpful unique (kill pathogens & anti-inflammatory) microbes Additional anti-inflammatory botanical agents Complete gut-health support because ZYGLUTEN launches simultaneous attack on each of four root causes. Visit their site for more info. REFERENCES Narula AP, MD, FACP, FACG, FACN, AGAF, Evaluation of safety and efficacy of dietary supplement ZYGLUTEN inpatients with gluten sensitivity, Journal of Gluten Sensitivity, Jan 2015; Vol 14(1); Pages 17 to 21 Nuryshev et al., New Probiotic Culture of Lactococcus lactis ssp. Lactis: Effective Opportunities and Prospects, J Microb Biochemic Technol 2016, 8:4 Luerce TD et al., Anti-inflammatory effects of Lactococcus lactis during the remission period of chemically induced colitis, Gut Pathogens, 2014 Jul 29; 6:33 Han KJ et al., Anticancer and Anti-Inflammatory Activity of Probiotic Lactococcus lactis; J Microbiol Biotechnology 2015 Oct; 25 (10); 1697-701 Adelene A Song et al., A review on Lactococcus lactis: from food to factory; Microbial Cell Factories, 2017 16:55 Tuck CJ et al., Increasing Symptoms in Irritable Bowel Symptoms with Ingestion of Galacto-Oligosaccharides Are Mitigated by α-Galactosidase Treatment; American J Gastroenterol. 2018; 113; 124-134 Furtado DN et al., Bacteriocinogenic Lactococcus lactis subsp. Lactis isolated from goat milk: Evaluation of the probiotic potential, Braz J Microbiology 2014; 45(3); 1047-1054 Narula AP, MD, FACP, FACG, FACN, AGAF, (Zygluten) Digestive Enzyme Supplement Therapy for Diabetic Gastroparesis With Gastric Bezoar; American College of Gastroenterology; October 8, 2018, Poster Presentation. Brock TD, Lactococcus Lactis Lactis used in cheese making, Biology of Microorganisms (11th ed.); Prentice Hall; ISBN 0-13-144329-1 Braat H et al., Lactococcus Lactis Lactis benefits in Crohn’s disease. Phase 1 trial with transgenic bacteria expressing interleukin-10 in Crohn’s disease; Clinical Gastroenterology Hepatol. 4 (6): 754-759 Gamal Enan et al., Novel Antibacterial Activity of Lactococcus Lactis Lactis Z11 Isolated from Zabady; Int J Biomed Sci. 2013 Sep; 9(3): 174-180 Bahey M et al., Lactococcus Lactis based vaccines: Current Status and future perspectives; Human Vaccines, 7:1, 106-109 Habtamu LD et al., Occurrence of Lactose Intolerance; J Food Process Technol 6:505 Michele DR et al., Lactose Hydrolysis in Milk and Dairy Whey Using Microbial β-Galactsidase; Enzyme Research Volume 2015, Article ID 806240, 7 Pages.
  2. Celiac.com 10/12/2018 - Ever since I read the study about how caricain enzymes can break down specific gliadin peptides in celiacs on a gluten challenge, I've been hoping for a chance to try out Glutagen's GluteGuard enzymes. The tablets contain Caricain, which is an enzyme that is found in the skin of an unripe papaya fruit. According to the company, GluteGuard can help people manage their gluten-free diet better by supporting "gluten digestion" whenever they may encounter cross-contamination. Celiac.com's standard disclaimer about enzymes: If you have celiac disease AVOID ALL GLUTEN, and do not misuse these in a way that would cause you to knowingly eat gluten, or be less vigilant about your gluten-free diet. Glutagen advises that the supplement is not a treatment or cure for celiac disease, and it is essential that people with celiac disease maintain a strict gluten free diet. My GluteGuard Trial As soon as my sample bottle arrived I began taking them as per the directions on the bottle: One GluteGuard tablet before each meal, and I did this before every meal over a two week period. My goal was to see if I noticed any difference while taking them, in comparison to how I felt before. The first thing I noticed was that my digestion was suddenly kicked into overdrive, which means I had firmer stools, and shorter times in the bathroom. I was surprised to find my digestion improve so much, even when I knew that my diet was not in any way contaminated by gluten (at least as far as I know!), which was an added bonus. Eating Out I normally eat out 1-2 times per week, and I like to believe that I am very careful whenever I do this. However, a recent study has shown that 9 out 10 people are exposed to gluten when attempting to eat gluten-free in a restaurant. I would not call myself a "super sensitive celiac," but I did not notice any difference between eating out vs. eating at home, and more importantly, I had no issues after eating out five times during my trial period. Overall Impression I would recommend GluteGuard to anyone who wishes to improve their digestion, as it definitely improved mine, regardless of whether or not I was ever cross-contaminated during my trial of the product. For those on a gluten-free diet who do continue to eat out, or those who must do so when they travel, definitely consider this product as it may help prevent the very negative effects of cross-contamination. Visit their site for more information.
  3. Celiac.com 06/22/2015 - Currently available digestive enzymes do not fully degrade gluten, and are thus of questionable use for people with celiac disease or gluten intolerance, say a team of researchers. Prior research had shown that post-proline cutting enzyme effectively degrade the immunogenic gluten peptides. Several existing digestive enzyme supplements claim to promote gluten degradation. The research team set out to assess the degradation of immunogenic gluten epitopes by currently available digestive enzymes. The team included G. Janssen, C. Christis, Y. Kooy-Winkelaar, L. Edens, D. Smith, P. van Veelen, and F. Koning. They are variously affiliated with the Department of Immunohematology and Blood Transfusion, Leiden University Medical Centre, Leiden, The Netherlands, DSM Food Specialties in Delft, The Netherlands, and DSM Food Specialties in South Bend, Indiana, USA. For their study, they assessed five commercially available digestive enzyme supplements along with purified digestive enzymes. They assessed these enzymes using enzyme assays and mass spectrometric identification. They monitored gluten epitope degradation using R5 ELISA, mass spectrometric analysis of the degradation products, and T cell proliferation assays. They found that the enzyme supplements leave the nine immunogenic epitopes of the 26-mer and 33-mer gliadin fragments largely intact. This is due to the high proline content of gluten molecules, which prevents gastrointestinal proteases from fully degrading them, leaving large proline-rich gluten fragments intact, including an immunogenic 33-mer from α-gliadin and a 26-mer from γ-gliadin. These latter peptides can trigger pro-inflammatory T cell responses resulting in tissue remodeling, malnutrition and a variety of other complications. In contrast, the pure enzyme AN-PEP effectively degraded all nine epitopes in the pH range of the stomach at much lower dose. From these results, the team concludes that most of the currently available digestive enzyme supplements are ineffective in degrading immunogenic gluten epitopes, but the AN-PEP do effectively degrade gliadin fragments. Source: PLoS One. 2015 Jun 1;10(6):e0128065. doi: 10.1371/journal.pone.0128065.
  4. Celiac.com Sponsor: Review

    How GliadinX Saved My Mom on Thanksgiving

    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
  5. Celiac.com 12/14/2017 - Can enzyme supplements help people with gluten sensitivity, including those with celiac disease? An Australian company is touting the results of a recent randomized, double blind study that supports enzyme supplements might be helpful for celiac patients in certain circumstances. The enzyme supplement was designed for people with celiac disease to use when facing likely or possible exposure to gluten, such as when traveling or eating food prepared outside their direct control. The company is careful to state that "enzyme supplementation won't cure celiac disease, and sufferers still need to avoid gluten." But the evidence from the two most recent studies does suggest that the product does help digest dietary gluten and could make life much easier for many people with celiac disease. The product, called GluteGuard, is based on a papaya fruit enzyme called caricain. This enzyme is shown to be helpful for celiac patients. A 2015 study showed adding caricain to bread dough reduced gluten toxicity to gluten by 90% for celiac patients. GluteGuard was recently evaluated in two clinical studies in Poland. The first study looked at 20 patients with celiac disease who were in clinical remission on a gluten-free diet. In that study, all patients ate one gram of gluten, equal to about one slice of bread, each day for 42 days, with 14 patients also taking GluteGuard and six taking a placebo tablet. Patients noted their symptoms and well-being each day, and received biopsies both before and after the study. Thirteen of the 14 celiac patients (93%) taking GluteGuard showed no adverse changes in clinical symptoms, biopsy results or well-being throughout the 42 day trial. Only one GluteGuard patient withdrew due to celiac-associated symptoms, while 4 of 6 taking placebo withdrew after 14 days due to adverse celiac symptoms. The second Polish study looked at the effectiveness of GluteGuard in patients with dermatitis herpetiformis, a gluten-triggered skin condition common in celiac patients. As with the first study, all patients in these study were in clinical remission. Patients consumed around six grams of gluten daily for seven days, with ten patients also receiving GluteGuard tablets and ten getting a placebo. The GluteGuard showed better results compared with the placebo group, with 81% showing no increase in areas of skin lesions and 71% showing a reduction in the appearance of skin lesions. The GluteGuard group also showed a 38% reduction in skin itchiness. Of the seven patients who withdrew from the study due to gluten symptoms, six were taking placebo. Both clinical trials met high scientific standards. In both studies, participants were randomly allocated to receive the treatment or placebo, and neither the participants nor the researchers knew owhich patient was receiving which intervention. So, yes, enzyme supplements may provide some help for people with celiac disease, especially as a hedge against minor or occasional gluten ingestion. So far though, they are not a magic bullet, and cannot replace a gluten-free diet. Read more at Medicalexpress.com.
  6. I have celiac and have followed a strict gluten-free diet for seven years. Now that we are retired, my husband and I travel a lot and that means dining out a lot. I always inform wait staff of my celiac disease and my need to avoid gluten but still occasionally get glutened and suffer the miserable results. I see ads for enzymes that break down gluten and wonder if they are effective in mitigating the reaction. I understand that they are not designed to allow celiacs to consume gluten freely, but I would like to be able to have an antidote that will at least make the reaction less severe. Has anyone found these to be effective in that way?
  7. Celiac.com 07/25/2017 - Enzymes are playing an increasing part in both the treatment of celiac disease, and in the manufacture of gluten-free baked goods. DSM recently showcased their new rice-based baker's enzyme, Bakezyme, at the annual meeting of Institute of Food Technologists (IFT) in Las Vegas. The product took DSM two years to develop and perfect, and promises to improve the softness and moistness of gluten-free bread. Bakezyme is so good, says DSM, and leaves gluten-free bread so soft and so moist that it can compete with wheat-based breads in texture. Designed to meet an array of manufacturer needs, Bakezyme is available in five different enzyme classes–amylase, protease, xylanase, glucose oxidase and amyloglucosidase. The version with amylase, an anti-staling enzyme, for example, will retain the softness for at least nine days. Fokke Van den Berg, DSM global business manager for baking says that Bakezyme grew out of DSM's efforts to tackle the two biggest consumer complaints about gluten-free bread, the hardness, and the dryness. While most baker's enzymes are derived from wheat, Bakezyme is made of fermentation-derived microorganisms added to rice flour, making it suitable for people with celiac disease and gluten intolerance. Because the enzymes are deactivated during baking, Bakezyme is regarded as a processing aid and thus is not required to be listed as an ingredient. DSM tested Bakezyme on two types of dough, oat and a mixture of potato and rice, with each requiring a slightly different formulation for similar results. Beyond the slight costs of ensuring that Bakezyme is gluten-free, its overall price is on par other enzyme ingredients, partly because such a small amount is needed. One kilo of Bakezyme is enough to produce 10,000 kilos of bread. The company expects most demand to come from the US and UK as well as other European countries, but the gluten-free trend is also spreading to Brazil, Turkey and Morocco, said Van den Berg. Read more at FoodNavigator.com.
  8. Celiac.com 09/25/2017 - There are currently several efforts underway to develop successful commercial enzyme treatments for celiac disease. Efforts include looking at the digestive enzymes in plants, such as the papaya and star fruits, including such predatory plants, such as the pitcher plant. One focus has been on developing enzymes that can break down gluten before it can trigger an immune reaction. This could prove helpful to many people with celiac disease. One such enzyme under development is Latiglutenase, formerly known as ALV003. Latiglutenase is a new name for an enzyme therapy designed to be taken with meals. The idea is that a person with celiac disease would take an enzyme tablet with a meal. If the meal had mild gluten contamination, the enzyme’s two recombinant proteins would break gluten into fragments that are not toxic to the immune system, thereby preventing exposure, and symptoms. But the stomach is a notoriously difficult environment to work in, so what seems like a simple idea quite a challenge from a science and biology perspective. Seeking to explore the ability of Latiglutinase to improve symptoms, a team of researchers recently set out to test latiglutenase on celiac patients who are seropositive despite following a gluten-free diet. The research team included Jack A. Syage, Joseph A. Murray, Peter H. R. Green and Chaitan Khosla. They are variously affiliated with the Division of Gastroenterology and Hepatology, Mayo Clinic, Rochester USA, the Celiac Disease Center at Columbia University, New York, USA, the Departments of Chemical Engineering and Chemistry, Stanford University, USA, and with ImmunogenX, Newport Beach, USA. "Though the ALV003-1221 trial was inconclusive regarding histologic improvement from latiglutenase, the evidence for symptom benefit, which is more quickly achieved, is quite convincing and clinically relevant," Joseph Murray, MD, of the Mayo Clinic in Rochester, Minn., said in a press release. In these trials, patients with celiac disease who were seropositive despite following a gluten-free diet saw major improvement in symptoms when taking latiglutenase with meals, according to a post hoc analysis of the CeliAction study. The team was really hoping to see histological improvement, but they feel satisfied that this trial shows, says Dr. Murray, that a "therapy to help patients struggling with symptoms due to celiac disease is now within reach." Stay tuned for more on efforts to develop effective enzyme treatments for celiac disease. Read more: Dig Dis Sci. 2017 Doi:10.1007/s10620-017-4687-7.
  9. Celiac.com 09/12/2017 - Are we at the beginning of the end for celiac disease? The last few years have seen numerous advances in celiac diagnosis and treatment. People diagnosed recently and in the future face a very different world than that faced by celiacs just five or ten years ago. In the old days, the process of properly diagnosing involved blood tests, endoscopies, and biopsies. In the near future, a simple blood test may do the trick. In the old days, the only treatment was a life-long gluten-free diet. That is still true, but the writing of change is on the wall. Here are five advances that will change the way celiac disease is diagnosed and treated in the future. These advances may well signal the beginning of the end of celiac disease as we know it. Blood Test Diagnosis (Without Biopsy) Researchers are getting better at identifying likely celiac cases using blood tests alone, without biopsy. As these techniques are refined and integrated into medicine, chances are pretty good that in the near future, large numbers of people will be diagnosed for celiac disease without the need for biopsy confirmation. Can Antibodies Spot Celiac Disease in Kids Without a Biopsy? Kids Can Get Accurate Celiac Diagnosis Without Biopsy Celiac Diagnosis Without Biopsy Can Be Useful in Some Cases Portable Gluten Detectors Imagine a future where you can take a bit of food you're not sure about, and pop it in a portable tester that will tell you if the food is gluten-free. A few years ago, that might have been the future of science fiction. With several companies looking to introduce just such kits, that future looks a lot more certain. Innovative Device Eliminates Gluten-Free Guesswork This Device Can Help Tell You If Your Food Is Actually Gluten-Free nimasensor.com Enzymes Enzymes that break down gluten might help people with celiac disease to enjoy a more normal life by protecting them from minor gluten contamination, and allowing them a bit more confidence when eating away from home. A number of manufacturers are currently working on enzyme treatments that are specifically designed to break down gluten for people with celiac disease. AN-PEP Shows Promise in Breaking Down Gluten in Stomach Enzyme Shows Promise In Dissolving Gliadin Peptides in Celiac Patients Could Carnivorous Plant Enzymes Act Like Beano for Gluten? Could Enzymes from Oral Bacteria Treat Celiac Disease Bio-Therapeutics—Hookworms They sound gross. The thought of having their guts infected with a parasitic worm makes people's skin crawl. However, researchers have documented the gut healing abilities of parasites like hookworm. When hookworms are introduced into the gut of people with celiac disease in the right amount, and kept at therapeutic levels, patients see their celiac symptoms disappear and their guts return to a healthy, normal condition. While still very much in the experimental phase, researchers are keen to investigate various strains and to determine the best therapeutic levels for these treatments. If all goes well, treatments based on parasitic worms will likely become more viable and more common in the future. Celiac Patients Tolerate Wheat Spaghetti After Hookworm Treatment Have Celiac Disease? Try a Little Hookworm with that Pasta! Can Bloodsucking Parasites Help Treat Asthma and Celiac Disease? Controversial Pig Parasite May Soon Be Sold In Germany To Treat Disease Bio-Therapeutics—Fecal Transplant Could fecal transplants be used to cure or to treat celiac disease? Much like hookworms, once you get past the 'yuck' factor, fecal transplants are proving to be cheap, easy, reliable way to treat gut conditions like C-Diff and, possibly celiac disease. The idea is to get some healthy poop in your gut to inoculate it with beneficial microbes. The effects are nothing short of astonishing. As they are studied, developed and refined, look for bio-therapeutic approaches like fecal transplant to play a role in treating gut contains like celiac disease. A Case of Refractory Celiac Disease Cured By Fecal Microbiota Transfer Vaccine A vaccine against celiac disease would be a holy grail of sorts. Receive a dose, or maybe multiple doses over time and become immune to the adverse effects of gluten. Several companies are working on a vaccine that would basically eliminate celiac disease. Many of these have moved through the early trial phases and several have shown enough promise to move to trials in humans. This is a very exciting area of research that may pay huge dividends in the near future. Celiac Disease Vaccine Set to Begin Full Human Trials Would You Try a Vaccine for Celiac Disease? Celiac Vaccine Clears First Big Clinical Trial This Vaccine Could Be a Game-Changer for People with Celiac Disease The main takeaway from these developments is that we are now living in an age where the diagnosis and treatment of celiac disease is the focus of tremendous research and development on numerous fronts. Many of these will likely result in products, tests, or treatments for celiac disease that were unimaginable just 5 or 10 years ago.
  10. Hello. I apologize for this being long but I feel I should explain the situation so you better understand where I'm coming from. I am here because I do not have the time or money to be galavanting around to different doctors offices. I spent time doing that already, lost money out of my pay from not working but never found A SINGLE ANSWER. I am a 23 year old female and back when I was about 13-14 I was diagnosed with Mononucleosis. Prior to this, I had been having other issues, or at least the minor problems I had previously considered as 'growing pains' since that's what my primary at the time attributed my pains to. Well now i'm 23 and it's only gone downhill since then. Back then I was told by a GI doctor who had done two or three EDG's and two colonoscopies that I have "the enzymes for crohn's and need to be careful." No other explanation other than eat 'gluten free'..... Now, this was kind of when it was the new 'health fad' for people, so being so young my logic was 'I'm young, I should be able to do what I want and eat what I want without worry!" so that's what i continued to do, despite feeling overall unwell. (I had really always felt unwell so it wasn't really that big of a deal for me) Now that i'm older, i've literally experience an entire swath of issues. The only reason I am here is because I am now thinking back to that conversation with the GI Doctor that maybe she was right. While I do have insurance, I honestly don't really have the money to be shelling out for these tests all over again as I was lucky the first time around when my grandparents had taken me since I was underage. My symptoms over the years and continuing have been: (in full, some may have nothing to do with the another) Lower back problems, feeling like sciatica but never confirmed. X-rays, MRIs, etc show nothing despite the intense pain. Drs now refuse to do more tests for 'nothing'. So I am left to handle feeling like an elephant is sitting on my lower back, right above my tailbone. (I did fall on that around 12 or 13 but doc never called back after testing, assumed i was fine...) Stomach cramping/spasm feelings On and off nausesa, any time of day. Inability to sleep. Constant changes from hot to cold. (Original doctor has said over the years my temperature seems to run higher than normal. I almost always feel feverish even if only slightly.) Headaches/migraines Fatigue Lightheadedness at times Restless legs (DRIVES. ME. INSANE. The muscle relaxers i've been given just made it 1000000x worse! I was so sleepy but couldn't fall asleep due to the restlessness.) On and off diarrhea / constipation (I don't know what a 'normal' bowel movement is) Costochondritis that has come and gone since I was in 4th grade. (I remember the day because it was April Fools day and everybody thought I was faking the serious pain I was in. I could barely breathe, it felt like my tendons/muscles were being torn apart on the inside) . I believe this is what my original DR thought was 'growing pains', except they never stopped even after I was finished growing.. I used to get sick very easily - for about two years it seemed to clear up then i started getting infections non-stop. There are some .... embarrassing things... Such as despite how many times I clean myself I feel like i'm.... leaking.......... Sharp/ache like pains everywhere in my body. There are likely many other things that I'm just so used to I'm not listing because I'm not sure if they're even related. I am just so tired of feeling like dog crap. I've never felt 100%, ever. For as long as I can remember i've always had issues but I come from a family that kind of just.... deals with their problems and not complain 24/7. After years of that, I need help. I am absolutely fed up not being able to do things because I just feel generally crappy. It's seriously depressing and making my depression and anxiety worse. Is testing for a second time worth it? If it is, what tests should I really be focusing on to figure out if this is my problem?
  11. 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
  12. Celiac.com 12/26/2016 - Could gluten-degrading enzymes offer a better future for celiac patients? Rothia mucilaginosa is an oral microbial colonizer that can break down proline- and glutamine-rich proteins present in wheat, barley, and rye that contain the immunogenic sequences that drive celiac disease. A team of researchers recently set out to isolate and identify the enzymes and evaluate their potential as novel enzyme therapeutics for celiac disease. The research team included G Wei, N Tian, R Siezen, D Schuppan, and EJ Helmerhorst. They are variously affiliated with the Department of Molecular and Cell Biology at the Henry M. Goldman School of Dental Medicine in Boston, Massachusetts; the Bacterial Genomics Group, Center for Molecular and Biomolecular Informatics at Radboud University Medical Centre, Nijmegen, the Netherlands; the Division of Gastroenterology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts; and with the Institute of Translational Immunology and Research Center for Immunology, University Medical Center, Johannes-Gutenberg-University, Mainz, Germany. They first extracted and separated membrane-associated R. mucilaginosa proteins using DEAE chromatography. They tracked enzyme activities using paranitroanilide-derivatized and fluorescence resonance energy transfer (FRET) peptide substrates, and by gliadin zymography. They determined epitope elimination in R5 and G12 ELISAs. They identified gliadin-degrading Rothia enzymes by LC-ESI-MS/MS as hypothetical proteins ROTMU0001_0241 (C6R5V9_9MICC), ROTMU0001_0243 (C6R5W1_9MICC), and ROTMU0001_240 (C6R5V8_9MICC). The Rothia subtilisins and two subtilisins from Bacillus licheniformis, subtilisin A and the food-grade Nattokinase, efficiently degraded the immunogenic gliadin-derived 33-mer peptide and the immunodominant epitopes recognized by the R5 and G12 antibodies. This study identified Rothia and food-grade Bacillus subtilisins as promising new candidates for enzyme therapeutics in celiac disease. To do this, the team cleaved succinyl-Ala-Ala-Pro-Phe-paranitroanilide, a substrate for subtilisin with Pro in the P2 position, as in Tyr-Pro-Gln and Leu-Pro-Tyr in gluten, which are also cleaved. Consistently, FRET substrates of gliadin immunogenic epitopes comprising Xaa-Pro-Xaa motives were rapidly hydrolyzed. They found that Rothia subtilisins and two subtilisins from Bacillus licheniformis, subtilisin A and the food-grade Nattokinase, efficiently degraded the immunogenic gliadin-derived 33-mer peptide and the immunodominant epitopes recognized by the R5 and G12 antibodies. Rothia and food-grade Bacillus subtilisins show promise for development as enzyme therapies for celiac disease. Source: Am J Physiol Gastrointest Liver Physiol. 2016 Sep 1;311(3):G571-80. doi: 10.1152/ajpgi.00185.2016. Epub 2016 Jul 28
  13. Celiac.com 10/21/2016 - Researchers at Boston University's Henry M. Golden School of Dental Medicine have identified a metabolic enzyme that alerts the body to invading bacteria, which may lead to new treatments for celiac disease. A research team that set out to isolate and identify the enzymes and evaluate their potential as novel enzyme therapeutics for celiac disease, reports that the enzymes exhibit exceptionally high gluten-degrading enzyme activities, and are "naturally associated with bacteria that colonize the oral cavity." Rothia bacteria, found in human saliva, can break down gluten compounds that cause an exaggerated immune response and that are typically resistant to the digestive enzymes that mammals produce. The team was able to isolate a new class of gluten-degrading enzymes from Rothia mucilaginosa, an oral microbial colonizer. The Rothia enzymes in question belong to the same class as food-grade Bacillus enzymes. The researchers noted that "B. subtilis is food safe and has been consumed for decades, e.g. in a product called natto, a Japanese fermented soy bean dish." B. subtilis and its products have been safely consumed by humans for many hundreds of years, with very few problems reported. They add that the "…food-grade status of B. subtilis, and the already widely consumed natto products, open new avenues for potential therapeutic applications of the subtilisin enzymes." The Rothia subtilisins and two subtilisins from Bacillus licheniformis, subtilisin A and the food-grade Nattokinase, efficiently degraded the immunogenic gliadin-derived 33-mer peptide and the immunodominant epitopes recognized by the R5 and G12 antibodies. This study identified as promising new candidates for enzyme therapeutics in celiac disease. Based on these results, the research team concludes that gluten-degrading Rothia and food-grade Bacillus subtilisins are the "preferred therapy of choice for celiac disease," and that their exceptional enzymatic activity, along with their connection to natural human microbial colonizers, make them "worthy of further exploration for clinical applications in celiac disease and potentially other gluten-intolerance disorders." Their study appears in the American Journal of Physiology—Gastrointestinal and Liver Physiology.
  14. Celiac.com 10/05/2016 - So, you're one of the millions of people with celiac disease, one of those folks who has to avoid gluten and eat a gluten-free diet. Maybe you'd like to be able to safely eat out. Maybe you'd like to safely eat some bread. Imagine a day a few years from now when you take a pill containing enzymes from a carnivorous plant, which allows your gut to fully break down gluten. You take the pill and sit down to that pizza and beer you've been missing for so long. Is such a day really somewhere in the near future? U of C researcher David Schriemer thinks so. "The idea here is that you would take it like Beano," Schreimer said. The enzymes are the product of diligent and meticulous collection by a team of dedicated scientists. They are responsible for carefully extracting the minute amount of digestive liquid in the bottom of each plant within an array of over 1,000 pitcher plants. Each pitcher plant holds just 0.5 millilitres of liquid. To collect enough for their study, Schreimer and his colleagues enlisted the help of three retired women in B.C.'s Lower Mainland who "had a fascination" for carnivorous sundews, Venus flytraps and pitcher plants. These women dedicated an entire greenhouse of roughly 1,000 individual pitchers, each about the size of a thumb, Schreimer said. The University of Calgary researchers supplied those women with vials of fruit flies to stimulate the plants, and the women tapped off small amounts of fluids on a regular basis. After six months, they had collected six litres, enough for the researchers to complete their studies. So, can the enzyme deliver? "We've taken it all the way through to animal trials at this point, and it seems to work," says Schreimer. The next step is trials on humans, followed by commercial development. Stay tuned for these and other results on the development of new drugs and treatment options for celiac disease. Source: cbc.ca
  15. I was wondering if anyone has tried Glutenza? It's a product by this Doctor...Tom O'Bryan, I heard him on underground wellness podcast...he has a product that he claims helps within a 2 hour period to minimize symptoms if you are "glutened". www.thedr.com Anyone tried it and had success? I've tried other probiotics before and had not felt much of a difference but there are ingredients on this enzyme I've not seen before with other probiotics. Thoughts?
  16. Gastroenterology Volume 129, Issue 3, Pages 786-796 (September 2005) Celiac.com 09/14/2005 - Researchers have long thought that the resistance of gliadin prolamines to digestive enzymes is a primary contributor to celiac disease—which leads to the intestinal permeability and inflammation in those who are at risk. Taking prolyl-endopeptidase enzymes (PEP) orally has been proposed and explored as a possible treatment for celiac disease (including extensive research done at Stanford Universitys Celiac Sprue Research Foundation – CSRF). In an effort to determine the feasibility of such a treatment, researchers in France conducted both in vitro (outside a living organism) and ex vivo—using biopsy specimens of active celiac disease patients—studies on the effects of PEP on gliadin peptides. For the in vitro studies the researchers used radio-reverse-phase high-performance liquid chromatography and mass spectrometry to analyze the degradation by PEP of 3H-labeled gliadin peptides 56-88 (33-mer). In the ex vivo studies the researchers added PEP and 3H-peptides together onto the mucosal side of duodenal biopsy specimens that were mounted in Using chambers, and the peptide transport and digestion were analyzed using radio-reverse-phase high-performance liquid chromatography. The results indicate that in both in vitro and ex vivo studies the gliadin peptides were only partly degraded by 20 mu/ml of PEP. This concentration of PEP decreased the quantity of intact gliadin peptides (31-49 and 56-88) that crossed the intestinal biopsy specimens, but did not prevent the intestinal passage of toxic or immunostimulatory metabolites—for this the researchers determined that PEP concentrations of at least 500 mu/ml for at least 3 hours was required to achieve full detoxification of gliadin peptides, and thus prevent intestinal transport of active fragments—unfortunately this finding virtually eliminates PEP as a possible treatment option for those with celiac disease. The researchers conclude optimistically, however: "After prolonged exposure to high concentrations of PEP, the amount of immunostimulatory gliadin peptides reaching the local immune system in celiac patients is decreased. These results provide a basis to establish whether such conditions are achievable in vivo (in living organisms)."
  17. Celiac.com 02/27/2014 - For many people with celiac disease, one of the numerous downsides of the condition is the constant threat of an adverse reaction triggered by accidental gluten consumption. Because reactions to gluten ingestion can be severe for some celiac patients, many clinicians are looking to see if anything can be done to lessen the effects gluten reactions in celiac patients once they have started. A team of researchers sought to provide at least one possible answer by looking into the safety and efficacy of Aspergillus niger prolyl endoprotease (AN-PEP) to lessen effects gluten reactions in celiac patients. The researchers included G.J. Tack, J.M. van de Water, M.J. Bruins, E.M Kooy-Winkelaar, J. van Bergen, P. Bonnet, A.C. Vreugdenhil, I. Korponay-Szabo, L. Edens, B.M. von Blomberg, M.W. Schreurs, C.J. Mulder, and F. Koning. They are all affiliated with the Department of Gastroenterology and Hepatology, VU University Medical Centre, 1007 MB Amsterdam, The Netherlands. For their study, the team enrolled 16 adults with celiac disease as confirmed by positive blood test and biopsy-confirmed subtotal or total villous atrophy. All patients were following a strict gluten-free diet, and showed normalized antibodies and mucosal healing classified as Marsh 0 or I. In their randomized double-blind placebo-controlled pilot study, the team had patients consume wheat toast, totaling about 7 grams of gluten per day, with AN-PEP for a two-week safety phase. After a two-week washout period with adherence of the usual gluten-free diet, 14 patients were randomized to receive gluten with either AN-PEP or placebo for there two-week efficacy phase. Baseline measurements included complaints, quality-of-life, serum antibodies, immuno-phenotyping of T-cells and duodenal mucosa immuno-histology. The team collected both serum samples and quality of life questionnaires during and after the safety, washout and efficacy phase. They conducted duodenal biopsies after both safety and efficacy phases. The primary endpoint was a change in histological evaluation according to the modified Marsh classification. None of the sixteen adults in the study suffered serious adverse events, and no patients withdrew during the trial. Overall scores for the gastrointestinal subcategory of the celiac disease quality (CDQ) remains fairly high throughout the study, indicating that AN-PEP was well tolerated. Through the efficacy phase, CDQ scores for patients consuming gluten with placebo or gluten with AN-PEP remained largely unchanged, and researchers observed no differences between the groups. Moreover, neither the placebo group nor the AN-PEP group developed significant antibody titers, and IgA-EM concentrations remained negative for both groups. The team excluded two patients from entering the efficacy phase because their mucosa showed an increase of two Marsh steps after the safety phase, even though their serum antibodies remained undetectable. A total of 14 patients were considered histologically stable on gluten with AN-PEP. Also after the efficacy phase, the team saw no significant deterioration in immunohistological and flow cytometric values between the group consuming placebo compared to the group receiving AN-PEP. Furthermore, compared to baseline, after two weeks of gluten four out of seven patients on placebo showed increased IgA-tTG deposit staining. In the seven patients receiving AN-PEP, one patient showed increased and one showed decreased IgA-tTG deposits. AN-PEP appears to be well tolerated. However, the primary endpoint was not met due to lack of clinical deterioration upon placebo, impeding an effect of AN-PEP. Source: World J Gastroenterol. 2013 Sep 21;19(35):5837-47. doi: 10.3748/wjg.v19.i35.5837.
  18. Celiac.com 01/23/2012 - After their diagnosis, celiac patients are put on the gluten-free diet, which is the only treatment option currently available. The diet requires total elimination of gluten, a protein found in wheat, barley, and rye, which when ingested causes an autoimmune reaction in celiacs which results in damage to the absorptive finger-like projections that line the small intestine, which are called villi. As diligent as celiacs can be, avoiding gluten can be a challenge, and slip-ups can happen, especially when eating out. In my research, I've come across gluten-digesting enzymes as a new medical treatment option for later down the line and have shared this good news with the gluten-free community. However, gluten-digesting enzymes are already available over the counter to help celiacs and gluten-sensitive people with managing their gluten-free diet. Dr. Nan Kathryn Fuchs, who helped to formulate the Advanced Bionutritionals product, Gluten Sensitivity Formula, shares some information regarding these enzymes and clears up a couple of misconceptions regarding their use. Furthermore, not all enzyme formulas containing DPP-IV are the same in terms of strength. Dr. Fuchs had her supplement creators formulate a gluten-digesting enzyme that was stronger than the other ones available on the market. The result was Gluten Sensitivity Formula. In her pamphlet, "How to Tell If You're Gluten Sensitive.And What to Do About It If You Are," Dr. Fuchs offers advice on how to take the supplement. Dr. Fuchs emphasizes that Gluten Sensitivity Formula isn't intended to replace a gluten-free diet; it is, however, designed to reduce or get rid of a reaction to "small amounts" of what would presumably be unintentionally ingested gluten, such as one may encounter at a restaurant or a dinner party due to cross-contamination. She also recommends taking one or two capsules of the formula "as insurance" before eating meals that might possibly be contaminated with gluten. Dr. Fuchs also clears up a myth regarding hydrocholoric acid (HCl), which has been believed to counteract digestive enzymes; this misconception has led to the incorrect advice that one shouldn't take hydrochloric acid and enzymes together. Hydrochloric acid is taken, according to Dr. Fuchs, in order to help with digesting proteins and minerals, for example calcium and iron. She says the supplement is more common among people over the age of 50. In fact, enzymes can only cancel out the benefits of hydrochloric if they alter the pH of the stomach by neutralizing its acids. Dr. Fuchs says that while animal-based enzymes can accomplish this, they are usually formulated with a protective coating or in a form that will prevent this from occurring. What's more, many enzymes, especially gluten-digesting ones, are made from plants. "So you can take them with HCl," Dr. Fuchs says. According to Dr. Fuchs, taking gluten-digesting enzymes "can make the difference between being successful on a gluten-free diet and failing." When used correctly, it can help alleviate the symptoms of a reaction caused by accidental gluten ingestion or prevent the reaction from occurring. As a celiac myself, I can say that inadvertent gluten ingestion is still a challenge I face on the gluten-free diet, even though I've been on the diet for years. Dr. Fuch's Gluten Sensitivity Formula is thus a welcome product that will make the lives of the gluten-free community a lot easier. Resources: Fuchs, Nan Kathryn, PhD. "How to Tell If You're Gluten Sensitive.And What to Do About It If You Are." Advanced Bionutritionals, 2010. "Digest This: Enzymes Can Help Your Food Intolerance." Living Without: August/September 2010. Food Reactions: Food Intolerance http://www.foodreactions.org/intolerance/index.html
  19. My daughter, diagnosed celiac in November, so gluten free nearly two months now, is having a hard time no matter what she eats. She has a tremendous amount of damage - seen on her endoscopy / colonoscopy - and her GI told us that it will take 6 months to a year for her body to heal. My question is what have are you taking to promote healing? I would like to add digestive enzymes, more probiotics (currently she eats yogurt and drinks kefir), and maybe Vitamin C in addition to the multivitamins she takes. What has worked for you? I can't stand watching her suffer after eating for a year! I know that we probably need to cut out the dairy, but she is very resistant to this. For those of you who have cut out milk, do you have an easier time with cheeses? I am open to suggestions and trying to learn -- all of this is still quite new to us.
  20. Celiac.com 09/12/2006 – A recent study by researchers at Stanford University has found that barley endoprotease EP-B2 is effective at digesting gluten in rats, and should be studied further as an “adjunct to diet control” in human celiac disease patients. This new finding adds to Stanford’s growing body of work on enzyme therapy as a possible treatment for those with celiac disease, and may one day lead to a effective treatment. Effect of barley endoprotease EP-B2 on gluten digestion in the intact rat. J Pharmacol Exp Ther. 2006 Sep;318(3):1178-86. Gass J, Vora H, Bethune MT, Gray GM, Khosla C. Stanford University. Abstract: "Celiac Sprue is a multi-factorial disease characterized by an intestinal inflammatory response to ingested gluten. Proteolytically resistant gluten peptides from wheat, rye and barley persist in the intestinal lumen, and elicit an immune response in genetically susceptible individuals. Here we demonstrate the in vivo ability of a gluten-digesting protease ("glutenase") to accelerate the breakdown of a gluten-rich solid meal. The proenzyme form of endoprotease B, isoform 2 from Hordeum vulgare (EP-B2) was orally administered to adult rats with a solid meal containing 1 g gluten. Gluten digestion in the stomach and small intestine was monitored as a function of enzyme dose and time by HPLC and mass spectrometry. In the absence of supplementary EP-B2, gluten was solubilized and proteolyzed to a limited extent in the stomach, and was hydrolyzed and assimilated mostly in the small intestine. In contrast, EP-B2 was remarkably effective at digesting gluten in the rat stomach in a dose and time dependent fashion. At a 1:25 EP-B2:gluten dose, the gastric concentration of the highly immunogenic 33-mer gliadin peptide reduced by more than 50-fold within 90 min, with no overt signs of toxicity. Evaluation of EP-B2 as an adjunct to diet control is therefore warranted in celiac patients."
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