You really shouldn’t…but that piece of cheesecake looks so good, and it’s been so long since you last had a slice — so you go for it. But shortly thereafter, you feel the rumbling of stomach and intestinal discontent, and — groan — you wish you had resisted.

A cast-iron stomach no more
When you were younger it seemed like you had a castiron stomach and could eat almost anything without having to pay the piper — but that’s not the case anymore, right? Now, indigestion, including heartburn, bloating and gas, seem to be the mainstay. And it’s especially true if you consume dairy products, grainbased foods (bread, pasta, etc.) containing gluten, or beans and greens (especially cruciferous vegetables like broccoli, cabbage and cauliflower). Look, it’s really not your fault. It’s due to your aging pancreas.

The old pancreas ain’t what it used to be The pancreas is the gland that secretes most of the enzymes you need to digest your food effectively. However, as you age, your pancreas begins to shrink.¹ Not surprisingly, clinical research has shown that the effectiveness of the pancreas also reduces with age.² The fact is, digestive enzyme secretion decreases in concentration as well as in output starting around age 30³ — although it’s really after 40 that these changes become more noticeable. In one study, middle-aged subjects (40–70 years) had 30 percent less frequent secretion of digestive enzymes than subjects less than 40 years old, and elderly subjects (over 70) had 108 percent less frequent secretion of digestive enzymes than subjects less than 40 years old! Oh well, there’s nothing you can do about it. You just have to accept indigestion, right? Wrong. In fact, there’s a great deal you can do about it.

If your vision isn’t what it used to be, do you just accept it? Of course not — you get glasses or contacts and you see better again! Why wouldn’t you do the same thing with your enzymes? If you don’t make as much digestive enzymes as you used to, with indigestion being the result, don’t accept it as inevitable. You can compensate, with outstanding results!

Digestive enzymes
Supplementation with the right type of digestive enzymes can help you digest virtually any foods you eat, including those with dairy products and gluten. Ideally, you can use enzymes that act in two locations in your gastrointestinal tract: 1) your stomach, and 2) your small intestine. The result will likely be more optimum digestion with a happy stomach and gut.

Digestion in your stomach While most digestive enzymes work in the more alkaline environment of your intestines, pepsin is different. Pepsin is the digestive enzyme produced in the stomach and released there to work alongside hydrochloric acid to begin the process of digesting complex proteins in smaller protein chains. Without sufficient pepsin to perform this role, further digestion by pancreatic protein enzymes will be far less effective. However, as with pancreatic enzymes, pepsin secretion also decreases with age. In fact, people 65 and older were shown in research to have a 40 percent reduction in pepsin secretion. Consequently, supplementation with pepsin will help assure that this vital first step in protein digestion is optimized.

Digestion in your small intestine
The inadequate production of digestive enzymes from the pancreas can be addressed by supplementing with proteases (protein-digesting enzymes), amylases (starch-digesting enzymes) and lipases (fat-digesting enzymes). One popular source of such enzymes is pancreatin, an extract from the pancreas of cows or pigs. However, another effective sources are microbial enzymes, which have activities similar to pancreatin. Microbial enzymes have been the subject of various studies evaluating their effects on lactose intolerance, impaired pancreatic enzyme production, excess fat in the feces, celiac disorder and a variety of other digestive issues, with positive results.^4,5,6,7,8,9

One of the most valuable attributes of microbial enzymes is that they appear to possess unusually high stability and activity throughout a wide range of pH conditions (from a pH of 2–10).¹⁰ This enables them to be more consistently active and functional for a longer distance as they are transported through the digestive tract. Also, since microbial enzymes are not derived from animal sources, they are perfectly appropriate for use by vegetarians — and research shows that are virtually non-toxic.^11,12,13 Supplementation with a broad range of microbial proteases, amylases and lipases will safely and effectively assist in the digestion of protein, carbohydrates and fats from many food sources, including foods that contain dairy products, gluten, beans and greens.

Gluten sensitivity
Gluten (from Latin gluten, “glue”) is a mixture of proteins found in wheat, barley and rye.¹⁴ For many, gluten can be difficult to digest; with the result being gastrointestinal upset (abdominal pain and tenderness, irregular bowel habits: constipation or diarrhea or alternating bowel movements) as well as nongastrointestinal issues.¹⁵ The good news is that there is a combination of gluten digesting enzymes called Glutalytic, which has been tested in a double-blind, placebo-controlled study¹⁶ (the “gold standard” in research). The results showed a statistically significant improvement when compared to the placebo group in the following categories: pain, bloating, emptying of bowels, hunger pains, rumbling of stomach, lower energy levels, headaches, and food cravings.

Dairy sensitivity
Dairy sensitivity can be due to lactose intolerance, the inability to digest the milk sugar lactose, and/or difficulty in digesting milk proteins. The result may include gas, cramps, diarrhea or constipation.

Lactose intolerance is the result of the body discontinuing the production of the digestive enzyme lactase, which digests lactose. Since only one-third of all people retain the ability to digest lactose into adulthood, lactose intolerance is prevalent.¹⁷ Research has shown that supplementing with the lactase enzyme can reduce pain, bloating and total symptoms associated with lactose intolerance.^18,19,20

The digestion of some milk proteins can take time. In fact, some research shows that a milk protein may remain in the stomach up to six hours before it is released into the intestines for further digestion.²¹ Difficulty in digesting milk proteins can result in constipation for some individuals.²² Luckily, supplementation with protease enzymes can help effectively digest milk proteins, thereby avoiding the effects of inadequate milk protein digestion.

Alpha-galactosidase
Bloating and gas are not fun to experience. Nevertheless, this experience is not unusual after eating beans and cruciferous vegetables (e.g. broccoli, cabbage and cauliflower). The reason is that these healthy foods contain goodly amounts of fiber, which can ferment in our gut. However, if these fibers can be broken down effectively, you’re less likely to experience bloating and gas. That’s where the enzyme alpha-galactosidase comes into play. In a double-blind, placebo-controlled study²³ on intestinal gas production and gas-related symptoms, the microbial enzyme alpha-galactosidase was given to healthy volunteers after a meal containing about 15 ounces of cooked beans. The result was that there was a reduction in gas formation, severity of bloating, abdominal pain, discomfort, flatulence, and diarrhea. Beneficial results were also seen in a similar study.²⁴

Conclusion
Indigestion, including heartburn, bloating and gas, are not fun. Avoiding foods that contain dairy and gluten, or even beans and cabbage, is likewise not fun. It may be possible to make your digestion more like it was when you were younger, with the use of a broad range of digestive enzymes.

1. Chantarojanasiri T, Hirooka Y, Ratanachu-Ek T, Kawashima H, Ohno E, Goto H. Evolution of pancreas in aging: degenerative variation or early changes of disease? J Med Ultrason (2001). 2015 Apr;42(2):177–83.
2. Herzig K-H, Purhonen A-K, Räsänen KM, Idziak J, Juvonen P, Phillps R, Walkowiak J. Fecal pancreatic elastase-1 levels in older individuals without known gastrointestinal diseases or diabetes mellitus. BMC Geriatrics. 2011;11:4.
3. Laugier R, Bernard JP, Berthezene P, Dupuy P. Changes in pancreatic exocrine secretion with age: pancreatic exocrine secretion does decrease in the elderly. Digestion. 1991;50(3-4):202–11.
4. Alternative Medicine, the Definitive Guide. Future Medicine Publishing: Puyallup, WA. 1993;215–22.
5. Griffin SM, et al. Acid resistant lipase as replacement therapy in chronic pancreatic exocrine insufficiency: a study in dogs. Gut 1989;30:1012–15.
6. Schneider MU, et al. Pancreatic enzyme replacement therapy: comparative effects of conventional and enteric-coated microspheric pancreatin and acid-stable fungal enzyme preparations on steatorrhea in chronic pancreatitis. Hepato-gastroenterol 1985;32:97–102.
7. Rosado JL, et al. Enzyme replacement therapy for primary adult lactase deficiency. Gastoenterol 1984;87:1072–82.
8. Barillas C, Solomons NW. Effective reduction of lactose maldigestion in preschool by direct addition of beta-galactosidases to milk at mealtime. Pediatrics 1987;79(5):766–72.
9. Phelan JJ, et al. Celiac disease: the abolition of gliadin toxicity by enzymes from Aspergillus niger. Clin Sci & Mol Med 1977;53:35–43.
10. Griffin SM, et al. Acid resistant lipase as replacement therapy in chronic pancreatic exocrine insufficiency: a study in dogs. Gut 1989;30:1012–15.
11. Garvin, P.J. & Merubia, J. Unpublished report. Submitted to WHO by Baxter Laboratories, Inc; 1959.
12. Garvin, P.J., Willard, R., Merubia, J., Huszar, B., Chin, E., & Gilbert, C. Unpublished report. Submitted to WHO by Baxter Laboratories, Inc; 1966.
13. Garvin, P.J., Ganote, C.E., Merubia, J., Delahany, E., Bowers, S., Varnado, A., Jordan, L., Harley, G., DeSmet, C., & Porth, J. Unpublished report from Travenol Laboratories, Inc., Morton Grove, IL, USA. Submitted to WHO by Gist-brocades NV, Delft, Holland; 1972.
14. Lamacchia C, Camarca A, Picascia S, Di Luccia A, Gianfrani C. Cereal-based gluten-free food: how to reconcile nutritional and technological properties of wheat proteins with safety for celiac disease patients. Nutrients. 2014 Jan 29;6(2):575–90.
15. Mansueto P, Seidita A, D’Alcamo A, Carroccio A. Non-celiac gluten sensitivity: literature review. J Am Coll Nutr. 2014;33(1):39–54.
16. Hudson M, King C. Glutalytic Clinical Trial for Normal Consumption of Gluten Containing Foods. Department of Biology, Kennesaw State University, Kennesaw Georgia. 2015: 4 pgs.
17. Gudmand-Hoyer E. The clinical significance of disaccharide maldigestion. Am J Clin Nutr 1994; 59(3):735S–41S.
18. Ramirez FC, Lee K, Graham DY. All lactase preparations are not the same: results of a prospective, randomized, placebo-controlled trial. Am J Gastroenterol 1994;89:566–70.
19. Sanders SW, Tolman KG, Reitberg DP. Effect of a single dose of lactase on symptoms and expired hydrogen after lactose challenge in lactoseintolerant subjects. Clin Pharm 1992;11:533–8.
20. Lin MY, Dipalma JA, Martini MC, et al. Comparative effects of exogenous lactase (beta-galactosidase) preparations on in vivo lactose digestion. Dig Dis Sci 1993;38:2022–7.
21. Ross RP, Fitzgerald GF, Stanton C. Unraveling the digestion of milk protein. Am J Clin Nutr. 2013 Jun;97(6):1161–2.
22. Daher S, Tahan S, Solé D, Naspitz CK, Da Silva Patrício FR, Neto UF, De Morais MB. Cow’s milk protein intolerance and chronic constipation in children. Pediatr Allergy Immunol. 2001 Dec;12(6):339–42.
23. Di Stefano M, Miceli E, Gotti S, Missanelli A, Mazzocchi S, Corazza GR.The effect of oral alpha-galactosidase on intestinal gas production and gas-related symptoms. Dig Dis Sci 2007;52(1):78–83.
24. Patil AG, Kote NV, Mulimani V. Enzymatic removal of flatulence-inducing sugars in chickpea milk using free and polyvinyl alcohol immobilized alpha-galactosidase from Aspergillus oryzae. J Ind Microbiol Biotechnol

Those of you that haven't cooked or baked with healthy alternative flours are often intimidated because they do respond and cook differently. We, at our Anti-Inflammation Cooking Institute, did all the testing for you to bring you easy-to-cook delicious variations of your favorite foods that use conventional wheat flours that convert to sugar, feed yeast, play havoc with blood sugar and thyroid health, and cause or accelerate inflammation.

When patients and readers begin a healthy anti-inflammatory lifestyle, the FIRST question I'm often asked is, "What constituents in coconut flour make it anti-inflammatory?" The answer; coconut flour contains 4g of nourishing fats (coconut oil) - incredibly potent as it's not only anti-microbial, anti-fungal, anti-bacterial and anti-inflammatory, it's also high in metabolism-boosting medium-chain fatty acids.

The SECOND question I'm often asked is, "What other varieties of healthy flours do you use and recommend?" I always reply, "The Super Five" - flours that have the most health-enhancing benefits, do not induce inflammation, accelerate or cause any of the conditions mentioned above, they include:

1. Almond flour
2. Coconut flour
3. Buckwheat flour (especially good for those with Celiac Disease)
4. Teff flour
5. Quinoa flour

The THIRD question I'm asked is, "What is Coconut Flour and how is it made?"

Producers of coconut flour originally sold the nutritious coconut milk by-product to farmers in the form of coconut meal. Farmers (particularly those practicing healthy farming and livestock) understood that coconut meal was an excellent source of organic fertilizer and animal feed supplement. As more research emerged supporting the numerous health benefits of coconut flour, human consumption of the valuable superfood also increased in the past few decades and continues to do so.

Coconut flour is derived from grating the meat of fresh coconuts - it is then dehydrated and de-fatted (the oil is extracted). The result is a fine powder that looks and feels similar to wheat or other grain flours. The most pure and organic form may even fool a seasoned foodie because of its lack of coconut flavor.

A Functional Super Food
Coconut flour has various health benefits from those of other coconut products - such as the oil for instance - and it offers a great gluten-free and very low carbohydrate alternative to conventional flour. Considered a functional food, coconut flour exhibits properties that significantly benefit health and is a valuable source of nutrition. Many people are beginning to learn how to bake with coconut flour and we at the Cooking Institute have made it easy for you with our recipes and cooking videos.

As a functional food, it's a great source of dietary fiber, high in protein, does not contain gluten and has a low glycemic index (GI). If you haven't considered baking or cooking with coconut flour, I'll take you by the hand (so to speak) into Dr. Gloria's Kitchen and make it easy via our upcoming cooking videos.

As a functional and super food, coconut flour is especially recommended for those with inflammatory issues as a result of consuming wheat or gluten. Coconut flour is safe for consumption in individuals with Celiac disease or gluten sensitivity, leaky gut syndrome, as well as those with diabetes - the reason I recommend its use for my patients and those seeking proactive measures to insure wellness.

Coconut Flour Nutrition
Ongoing research is being conducted regarding the many health benefits coconut flour promotes…AND…studies support that the nutrition in the coconut meat is not lost in the process of converting it into flour nor in its baking or cooking - one more reason to bake with coconut flour!

Looking Forward
In subsequent articles, I'll be detailing the "Super Five" flours, their health-enhancing properties and some historical perspective of the individual grains.

In the next issue of Total Health Magazine, I'll outline the specific vitamins, amino acids, electrolytes and minerals in coconut flour and their health benefits…stay tuned.

Making these healthy lifestyle modifications is what enables us to "Age Without Feeling or Looking Old" because we're avoiding inflammatory foods and ingredients that age us prematurely while robbing us of quality of life and then propel disorders and diseases that shorten our life-span.

In many older detective stories, the punch line famously is, "the butler did it." In the minds of many contemporary Americans, gluten is the "butler." Increasingly, when individuals experience symptoms such as fatigue, headaches and gastrointestinal distress, including gas, bloating and diarrhea, gluten is called out as the culprit. The passage of partially digested or undigested gluten through the intestines and the gut barrier may also contribute to additional symptoms not limited to those involving the development of food sensitivities and intolerances. The answer in this paradigm is to avoid all gluten-containing foods, such as wheat, oats, rye, barley and spelt. The problem with this paradigm is that other than for a quite small percentage of the populace, there is little evidence that gluten per se is the culprit or that gluten avoidance will solve all or even most gluten-associated issues. This topic often leads to heated debates. Readers should be aware that the gluten-as-villain story has quite serious skeptics.^1,2

Who Reacts to Gluten?
Gluten, a protein, is a large, complex molecule that contains thousands of folded amino acid sequences composed of globulans, albumins, glutenin and gliadin, with the gliadin fraction believed to cause most of the symptoms associated with gluten sensitivity. Gluten's exceptionally rich proline content contributes to resistance to digestion. When this big ball of peptides is insufficiently broken down, amino acid bonds within each molecule remain resulting in a partially-degraded protein that can lead to an array of symptoms. Some authorities suggest that if gluten is a sufficiently rich component of the diet (a rare situation), it will lead to reactions even in those otherwise tolerant as a result of these difficulties in digestion.

There is a spectrum of gluten-related disorders, including celiac disease, gluten sensitivity, and wheat allergy, the latter affecting only on the order of 0.1 percent of individuals in Westernized countries.^3,4 Non-celiac gluten intolerance involves heightened immunologic reaction to gluten in genetically susceptible people whereas celiac disease involves a complex autoimmune response in the small intestine to gluten ingestion.^5,6 The estimated prevalence of celiac disease is approximately one percent of the populace.⁷

This is where things start to become very interesting in ways that suggest that the "gluten did it" scenario may be a bit misleading. As summarized in a fine article a few years back in the New York Times, "roughly 30 percent of people with European ancestry carry predisposing genes, for example. Yet more than 95 percent of the carriers tolerate gluten just fine. So while these genes (plus gluten) are necessary to produce the disease, they're evidently insufficient to cause it."⁸

This observation becomes more intriguing in light of recent blood serum studies. In one, an examination of 9,133 frozen blood samples taken from US Air Force recruits between 1948 and 1954 for the antibody that people with celiac disease produce in reaction to gluten found that only about one in seven hundred tested positive, or 0.2 percent. This was compared to rates of celiac disease among 12,768 people who either had similar years of birth (i.e. were born around 1930) or who were of a similar age to the original donors at the time of sampling (i.e. young adults today). The rates of celiac disease were 0.8 percent and 0.9 percent respectively, or a 4 to 4.5-fold increase. In other words, in populations that genetically were virtually identical, celiac rates had increased more than 400 percent in a mere 50 years.⁹ Another study that analyzed blood serum from more than 3,500 Americans who had been followed since 1974 found that by 1989 the prevalence of celiac disease in this cohort had doubled.¹⁰

More recent studies have confirmed the rising risk of developing celiac among otherwise similar groups in the past. So have cross-national comparative studies. The populations in adjacent Russian Karelia and Finland are equally exposed to grain products and share partly the same ancestry, but live in completely different socioeconomic environments. The two study populations are culturally, linguistically and genetically related with predisposing gene variants are similarly prevalent in both groups. Examination of 5,500 subjects yielded a prevalence of roughly one in 100 among Finnish children whereas the same diagnostic methods indicated only one in 500 among their Russian counterparts.¹¹

More Intrigue
In line with a number of studies looking at the prevalence of asthma and other forms of autoimmune disease, the Finnish/ Russian data suggest modern sanitary and dietary practices are leading to poorer health in unexpected ways. For instance, three of four Russian Karelian children harbored Helicobacter pylori in comparison with one in 20 Finnish children. H. pylori can cause ulcers and stomach cancer, but mounting evidence suggests that exposure also reduces the incidence of asthma. The author of the New York Times article mentioned above notes that one author of the Finnish study suspects that Russian Karelians' microbial wealth (exposure to a much larger variety of microbes compared to more Westernized and metropolitan populations) protects them from autoimmune and allergic diseases by strengthening the arm of the immune system that guards against such illnesses. Similarly, Yolanda Sanz, a researcher at the Institute of Agrochemistry and Food Technology in Valencia, Spain, makes a compelling case for the importance of intestinal microbes. "Years ago, Dr. Sanz noted that a group of bacteria native to the intestine known as bifidobacteria were relatively depleted in children with celiac disease compared with healthy controls. Other microbes, including native E. coli strains, were overly abundant and oddly virulent."

Quite a number of authors have noted a possible role for longer breast-feeding of infants in helping to confirm bifidobacteria in a more dominant role in the large intestine in children and later life as well as controlling E. coli growth. Other changes in Western practices similarly may influence the role of foodstuffs. For example, a study published in 2011 found that a specially fermented wheat flour-derived product did not lead to any sort of toxic reaction after being given to celiac patients for 60 days. This is in line with research indicating that the manufacture of wheat and rye breads or pasta with durum flours by using selected sourdough lactobacilli markedly decreases the toxicity of gluten. In Western countries, cereal baked goods typically are manufactured by fast processes. As noted by researchers, this avoids the traditional long fermentation by sourdough—a cocktail of acidifying and proteolytic lactic acid bacteria—and has replaced fermentation with chemical and baker's yeast leavening agents. Under these conditions, cereal components are not degraded during manufacture.¹²

Again, a number of researchers have uncovered evidence that keeping bifidobacteria and lactobacilli at sufficiently high levels in the appropriate areas of the intestines strongly influences tendencies toward autoimmune diseases.

Other Contributors to the Modern Gluten Intolerance

Gluten has been in the human food chain for thousands of years, yet gluten intolerance has become widespread in recent decades. Along with some items already mentioned, here is an extended list of possible culprits:

• Changes in baking techniques; to speed processing and reduce costs, modern breads almost never are fully yeast-raised as in the past, a process that makes gluten more digestible; similarly, the long steaming of wheat and rye breads typical of Central and Eastern Europe makes breads more digestible
• Changes in the gluten content of wheat—since the 1950s the USDA, without public notice, has been involved in wheat breeding to increase gluten content
• Novel processing techniques when using gluten-derived compounds in foodstuffs, such as deamidation involving removing an amino group (NH2); this makes the peptides more soluble and smaller, but also increases their chances of breaching the gut lumen and activating immune responses
• Changes in refrigeration and storage, which, in turn, change our gut bacteria and lead to novel intolerance reactions to foods
• Reduced breast-feeding and altered feeding and weaning practices; changes in infant formulas; suspected changes in mother's milk itself at the populace at large becomes more prone to overweight and obesity plus the foods consumed by mothers change
• C-sections becoming more common, which tends to alter the bacteria babies inherit (or do not inherit) from the mother via the birth canal
• Reduced exposure to various dusts and other challenges from the natural world that help train the developing immune system and reduce autoimmune overreactions
• GMOs and the chemicals linked to these are ubiquitous in the food supply

Although, as indicated above, heightened sensitivity to gluten extends back several decades, GMOs may be true game-changers for future generations. According to Jeffrey Smith and the Institute for Responsible Technology (IRT), a "possible environmental trigger [for gluten intolerance] may be the introduction of genetically modified organisms (GMOs) to the American food supply, which occurred in the mid-1990s," describing the nine GM crops currently on the market. In soy, corn, cotton (oil), canola (oil), sugar from sugar beets, zucchini, yellow squash, Hawaiian papaya, and alfalfa, "Bt-toxin, glyphosate, and other components of GMOs, are linked to five conditions that may either initiate or exacerbate gluten-related disorders." It's the Bt-toxin in genetically modified foods that kills insects by "puncturing holes in their cells." The toxin is present in ‘every kernel' of Bt-corn and survives human digestion, with a 2012 study confirming that it punctures holes in human cells as well.

According to an IRT report, GMO-related damage is linked to five different areas: intestinal permeability, imbalanced gut bacteria, immune activation and allergic response, impaired digestion, and damage to the intestinal wall. The IRT release also indicated that glyphosate, a weed killer sold under the brand name 'Roundup,' was found to have a negative effect on intestinal bacteria. GMO crops contain high levels of this toxin at harvest. "Even with minimal exposure, glyphosate can significantly reduce the population of beneficial gut bacteria and promote the overgrowth of harmful strains."^13,14

Sometimes the Villains Aren't Bad Guys and How To Promote the Good Guys
A word of caution is in order regarding gut bacteria. Just as gluten may not be the primary actor in its own drama, so, too, are some "bad" bacteria not so bad after all. Above, the case of H. pylori was presented as perhaps not quite as black-and-white as normally argued. Another example is E. coli. Which E. coli? Recent research has uncovered that small molecules produced by the microbiota and related to indole extend healthspan in geriatric worms, flies, and mice.¹⁵ According to the authors of this research, the term "healthspan" describes the length of time a human or animal, while aging, can stay active and resist stress. In this research, the focus is on whether the animals live healthier, but not necessarily longer. The study identified indole and related molecules as compounds released by E. coli bacteria. Indoles may be keeping the intestinal barrier intact and/or limiting systemic inflammatory effects. Moreover, there are specialty E. coli strains that are well-researched as excellent probiotics useful in treating a number of gastro-intestinal disorders and even helping to maintain remission in patients with ulcerative colitis.^16,17 The trick is to encourage the presence of the right E. coli to limit the growth of the wrong E. coli.

What about daily foods that boost good gut microbiome, including diversity in the gut? It is important to be able to promote gut health via daily food habits rather than relying on prebiotic supplements alone. Here are some everyday choices according to a 2016 survey conducted in Europe:¹⁸

Good foods for boosting the gut microbiome

• Fruit and vegetables
• Yogurt
• Coffee
• Tea
• Red wine

• A high-calorie diet
• A high-carbohydrate diet
• Sugar-sweetened beverages
• Frequent snacks

Medications have the biggest influence on gut microbiome diversity. Antibiotics, proton-pump inhibitors and metformin (a common diabetes drug) all are linked to lower microbiome diversity.

Conclusion
Blaming gluten for GI-tract issues, allergies and even weight gain is akin to the pharmaceutical world's "magic bullet" approach once encapsulated as "one disease, one drug." In reality, in the modern Western world a host of changes have taken place in food growing and processing along with changes in personal habits and some of these changes have led to an otherwise and previously relatively innocuous protein, gluten, becoming a source of health issues. Eliminating gluten from the diet (along with wheat, oats, rye, barley and spelt) is not the answer to environmental mistakes, such as the growing prevalence of poor bread-making practices and the use of GMOs. A better approach is to learn the nature of the non-health- promoting practices and then to find alternatives.

References:

1. Gaesser GA, Angadi SS. Gluten-free diet: imprudent dietary advice for the general population. J Acad Nutr Diet. 2012 Sep;112(9):1330–3.
2. Shewry PR, Hey SJ. Do we need to worry about eating wheat? Nutr Bull. 2016 Mar;41(1):6–13.
3. Piezak M. Celiac disease, wheat allergy, and gluten sensitivity: When gluten free is not a fad. JPEN J Parental Enterol Nutr. 2012;36(suppl 1):68S–75S.
4. Sapone A, Bai JC, Ciacci C, et al. Spectrum of gluten-related disorders: Consensus on new nomenclature and classification. BMC Med. 2012; 10:13.
5. Hadjivassiliou M, Grunewald RA, Davies-Jones GAB. Gluten sensitivity as a neurological illness. J Neurol Neurosurg Psychiatry. 2002;72(5): 560–3.
6. Briani C, Samaroo D, Alardini A. Celiac disease: From gluten to autoimmunity. Autoimmunity Rev. 2008;7(8):644–50.
7. Catassi C, Fassano A. Celiac disease. Curr Opin Gastroenterol. 2008;24(6):687–91.
8. Moises Velasquez-Manoff. Who Has the Guts for Gluten? New York Times. February 23, 2013.
9. Rubio-Tapia A, Kyle RA, Kaplan EL, Johnson DR, Page W, Erdtmann F, Brantner TL, Kim WR, Phelps TK,
10. Lahr BD, Zinsmeister AR, Melton LJ 3rd, Murray JA. Increased prevalence and mortality in undiagnosed celiac disease. Gastroenterology. 2009 Jul;137(1):88–93.
11. Catassi C, Kryszak D, Bhatti B, Sturgeon C, Helzlsouer K, Clipp SL, Gelfond D, Puppa E, Sferruzza A, Fasano A. Natural history of celiac disease autoimmunity in a USA cohort followed since 1974. Ann Med. 2010 Oct;42(7):530–8.
12. Kondrashova A, Mustalahti K, Kaukinen K, Viskari H, Volodicheva V, Haapala AM, Ilonen J, Knip M, Mäki M, Hyöty H; Epivir Study Group. Lower economic status and inferior hygienic environment may protect against celiac disease. Ann Med. 2008;40(3):223–31.
13. Francavilla R, De Angelis M, Rizzello CG, Cavallo N, Dal Bello F, Gobbetti M. Selected Probiotic Lactobacilli Have the Capacity To Hydrolyze Gluten Peptides during Simulated Gastrointestinal Digestion. Appl Environ Microbiol. 2017 Jun 30;83(14).
14. GMOs linked to gluten disorders plaguing 18 million Americans https://www.rt.com/usa/gmo-gluten-sensitivitytrigger-343/
15. Are Genetically Modified Foods a Gut-Wrenching Combination? http://responsibletechnology.org/glutenintroduction/
16. "Chemicals from gut bacteria maintain vitality in aging animals: Indoles help worms/flies/mice live stronger for longer." ScienceDaily. ScienceDaily, 21 August 2017. www.sciencedaily.com/releases/2017/08/170821151052.htm.
17. Fuchssteiner H, Nigl K, Mayer A, Kristensen B, Platzer R, Brunner B, Weiß I, Haas T, Benedikt M, Gröchenig HP, Eisenberger A, Hillebrand P, Reinisch W, Vogelsang H. [Nutrition and IBD-Consensus of the Austrian Working Group of IBD (Inflammatory Bowel Diseases) of the ÖGGH]. Z Gastroenterol. 2014 Apr;52(4):376–86. 17. Enck P, Zimmermann K, Menke G, Klosterhalfen S. Randomized controlled treatment trial of irritable bowel syndrome with a probiotic E.-coli preparation (DSM17252) compared to placebo. Z Gastroenterol. 2009 Feb;47(2):209–14.
18. Zhernakova A, Kurilshikov A, Bonder MJ, Tigchelaar EF, Schirmer M, Vatanen T, Mujagic Z, Vila AV, Falony G, Vieira-Silva S, Wang J, Imhann F, Brandsma E, Jankipersadsing SA, Joossens M, Cenit MC, Deelen P, Swertz MA; LifeLines cohort study, Weersma RK, Feskens EJ, Netea MG, Gevers D, Jonkers D, Franke L, Aulchenko YS, Huttenhower C, Raes J, Hofker MH, Xavier RJ, Wijmenga C, Fu J. Population-based metagenomics analysis reveals markers for gut microbiome composition and diversity. - Science. 2016 Apr 29;352(6285):565–9.