Gluten & Grains

An In Depth Exploration

We partnered with doctors, chemists, and nutritionists to be apart of cutting edge research that explores which foods drive cognitive potential, boost mental awareness, and help your overall performance. Eliminating potentially toxic foods that could divert you from your health journey is essential to our mission.

So what's the deal with gluten and grains?

Gliadin molecules, however, do not like to bond with each other or with glutenin molecules. Instead, they fold into small, round shapes. These molecules run along the super-chains of glutenin, acting like ball bearings. The long chains of glutenin tend to curl up like springs in the center of each molecule, forming temporary bonds between other segments of the chain, and the gliadin keeps the glutenin from bonding with itself too much.

Many of us have baked a loaf of bread or tried our hand at spinning a pizza. If you recall the process, do you remember how tough it can be to shape the dough? When trying to manipulate the dough, it doesn’t always want to stay. Instead, it tries to spring back into itself. Gluten’s molecular structure is responsible for this springy and stretchy behavior. It is during the kneading process that the alignment of the molecules change. The more a dough is kneaded, the stronger the gluten structure becomes. Leaving dough to rest gives the glutenin coils a chance to become a little less springy, and thus giving the baker an opportunity to shape the dough into a bread shape.

The growing pool or research paired with the increased rates of autoimmune disorders, non-celiac gluten sensitivity, and celiac disease points to the array of troubles gluten and grain poses on the human body. Indeed, gluten and grains have been shown to slow down digestion, interfere with nutrient absorption, and even produce serious health conditions.

Gluten is a sequence of proteins found in wheat, rye, barley, and triticale. The large protein molecule is primarily made up of two (relatively) smaller proteins--glutenin and gliadin, with each composed of an approximately 1,000 amino acid chain. Barley is commonly found in malts, soups, and beers. Rye is also found in rye beers, rye breads, and cereals. While triticale is a newer grain, bred by plant geneticists, it is a hybrid of wheat and rye and not commercially available until the late 20th century. You can find triticale in breads, pasta cereals. Wheat is the most commonly known and widely available in pastries and other baked treats, pasta, cereals, sauces, and an array of other items.               

The proteins glutenin and gliadin work together to form the strong, springy gluten matrix. Glutenin forms long chain-like molecules that bond easily with each other. The glutenin chain link with each other to form a long super-chain. 

Why Gluten-Free Can Feel Like a Fad

You may be familiar with the biological inability to digest gluten, called celiac disease. In the United States, nearly 2% of the population has celiac disease. This is a fraction of the population, sure, but when expanding the category to include people who live with conditions and even diseases caused or exacerbated by gluten, the population grows greatly. In fact, when examining who suffers from low-level inflammation reactions to gluten, the percent of Americans affected raises to 7%.

 A lifestyle change to consider detoxing our kitchen and weeding out food from other less talked about agitators can restore health and performance.

Only after a 2003 study, have we known that celiac affects 1 in 133 people, a rate almost 100 times greater than previously thought. Learning how pervasive celiac disease is has been imperative to learning how gluten functions in other gut-related illnesses. There has been a tough, but remarkable journey that has lead scientists to actually be able to isolate the gluten protein molecule as a major contributor to low health. While gluten-free may feel like another fad, identifying gluten as a trigger is among the most important answers to sickness from gut-related ailments to treating a number of autoimmune diseases and even cancers.

There is a growing body of research exploring the effects of wheat allergies and gluten. Subsequently, the pool of people with gluten sensitivities has grown as we learn more about the host of problems directly caused or exacerbated by gluten. It’s important to recognize, gluten sensitivity is not confined to the single autoimmune disease--celiacs--but belongs to an expansive category, including: irritable bowel, depression, osteoporosis, all other autoimmune disorders, and more serious diseases resulting from the gluten protein.

While removing gluten entirely from diets has helped celiac patients to regain their health. We know that we need to treat autoimmune disorders with a holistic approach where gluten is not the only aggressor. Instead we need to rethink how our environment can impact our wellbeings.

       dehydrated fennel adds crisp crunch and fragrant flavor to any meal



dehydrated fennel adds crisp crunch and fragrant flavor to any meal

Exploring the Science Behind Gluten Sensitivity

Non-celiac gluten sensitivity (NCGS) can be tricky to diagnose because of the relatively non-specific symptoms. The symptoms are similar to celiac disease, which can include: bloating, abdominal discomfort, diarrhea, constipation, muscular disturbances, headaches, migraines, severe acne, fatigue, and bone or joint pain. Moreover, there are a number of people that are truly sensitive to gluten, but don’t show or feel any digestive distress. Their symptoms can be concentrated in places like the nervous system or the skeletal system.

While there are expensive and specific tests that can diagnose NCGS based on the presence of certain antibodies, the most commonly used method for diagnosis is an elimination diet. If symptoms improve when gluten is removed and then recur when gluten is reintroduced, a NCGS diagnosis can be made.

Actually, the story of how gluten was identified as an indigestible protein and the protein responsible for making celiac patients sick is quite interesting. In an interview conducted by Chris Kresser with renowned researcher Dr. Alessio Fasano, Fasano describes how one Dutch gastroenterologist finally discovered why people were becoming sick and even dying from celiac disease. 

He describes how during World War II, celiac disease dropped from 35%-40% to nonexistent during the war. However, once the war was over, the mortality rate for celiac disease returned to pre-war era numbers. Trying to understand this devastating shift, he finally realized that it could be due to the availability of grains containing gluten. During the war, wheat flour was instead made with potato starch. After this was recognized as a possible explanation, he conducted a number of studies, including altering the diets of babies exhibiting symptoms of the disease. In this elimination diet, babies were primarily fed bananas. So, in short, that how the trigger of many autoimmune diseases and digestive issues was found.

In order for the body to absorb nutritious amino acids, proteins are broken into smaller pieces and then even smaller pieces until the amino acids are peeled off and absorbed. Dr. Alessio Fasano’s research describes how gluten, however, is an exception. It is broken into pieces, but the body does not produce the necessary enzymes to dismantle gluten into the small pieces required for the body to access all the amino acids.  

If there is an overabundance of alpha-gliadin in the gut, it will continue to signal for more and more zonulin to be produced. The more zonulin in the gut, the more frequently the gut wall will open up, and the more easily large molecules of protein (like gliadin) can be released outside of the gut. Once the gliadin is outside of the gut, it is free to bond with tTG and cause inflammatory reactions. However, if an individual has a leaky gut, larger particles even in digested proteins and bacteria are able to pass through the gut wall.

Some particular molecules of alpha-gliadins have been shown to exacerbate the immune system more than others. However, based on conflicting current research, it is difficult to definitively cite gliadin and gluten as the ultimate source of problems like intestinal permeability; whether, it is possible other molecules compound the problem.

For example, a recent study concluded that NCGS might not be a discrete condition. Instead, they conjectured that its effects might be confounded by the presence of short- chain carbohydrates called FODMAPs (fermentable oligosaccharides, disaccharides, monosaccharides, and polyols). FODMAPs are common ingredients in most of the Western world’s glutenous bread, pasta, and snack products, and are a common irritant for people with digestive issues. In that particular study, the researchers found just as much of a change in symptoms when participants eliminated FODMAPs as when they eliminated gluten.                        

Contrary to the aforementioned, other scientists argue that gluten’s propensity to cause intestinal permeability links it definitively to NCGS and other autoimmune conditions. In any case, the debate is not rested upon is gluten bad for digestion, whether, is it the sole perpetrator?


NCGS is among the pool of diseases and discomforts caused by a reaction to gliadin--an important protein that makes up the macromolecule, gluten. At an even smaller molecular level, gliadin is composed of proline and glutamine, therefore it is categorized as a prolamin protein. Prolamins are generally hard to digest because of their size, but when consumed, they do not necessarily result in an autoimmune reaction in healthy individuals. The gliadin protein is found only in wheat, rye, and barley, but there are other similar prolamins found in grains like corn and oats that can cause cross-reactions in sensitive individuals.

The theory behind eliminating gluten from the diet is that gliadin can cause leaky gut in any individual, especially genetically modified wheat, not just people with celiac disease. As previously noted, gliadin has many properties that make it hard to digest. This can actually pose serious concern.

Studies have shown how gluten and gliadin can increase the permeability of the small intestine. This condition, also referred to as leaky gut, occurs when the junctions between the cells lining the outside of the small intestine are weakened. It is important to note that the gut is designed to be semi-permeable, which means that it should allow certain molecules to pass through the gut wall while keeping others safely inside the gut. When healthy, the gut wall allows small particles like vitamins, minerals, and small molecules of amino acids, fatty acids, and simple sugars to pass through into the bloodstream and lymphatic system. However, if an individual has a leaky gut, larger particles of partially digested proteins and bacteria are able to pass through the gut wall.

How does gluten weaken the gut wall? It turns out that there is one region on certain alpha-gliadin molecules that signal for the production of the proteins, zonulinsZonulins are the proteins responsible for triggering the release of nutrients from the gut into the bloodstream and lymphatic system.

What About Grains?


Grains even without gluten have their problems, too. As it turns out, the same antibodies surrounding the gut that mistake gliadin for a pathogen tend to also misrecognize similar proteins in grains and dairy as pathogens. This phenomenon is known as cross-reactivity, and it is one of the reasons why many people suffering from celiac and NCGS cannot tolerate things like millet, oats, yeast, rice, and corn.                        

In addition, cross-reactivity can occur with foods that are high in carbohydrate-binding proteins called lectins. Beans, seeds, and cereal grains are all high in lectins. (Technically all beans and grains are seeds, as they function as the source for new plant life.) Lectins serve as defense mechanisms for the seed, preventing the seed from sprouting or being digested. As you can probably guess, humans and other mammals have a hard time digesting such defense mechanisms. The hardest lectins for human digestion are prolamins and agglutinins.                        

We’ve already discussed one prolamin (gliadin), but there are many different prolamins in all kinds of seeds and grains: hordein in barley, secalin in rye, zein in corn, kafirin in sorghum, orzenin in rice, and avenin in oats. While they do not all behave exactly like gliadin in our bodies, they all have similar amino acid structures and functions in the grain. The big problem with prolamins is that they incredibly difficult to break down in our bodies. In fact, we contain very few enzymes capable of breaking them down into their constituent amino acids. In addition, most seeds and grains contain inhibitory proteins that prevent the enzymes we do have from doing their job. Grains and seeds simply don’t want to be digested!    


       dehydrated vegetables, for a grain free alternative    



dehydrated vegetables, for a grain free alternative


If the proteins travel through the gut undigested, the bacteria in the lower digestive tract are then tasked with breaking them down. When bacteria munch on proteins, the result is an abundance of gas, which can cause digestive distress. Furthermore, if the gut is already compromised, the large molecules can increase the prevalence of leaky gut and the resulting inflammation.       

If you are gluten intolerant or have a particularly sensitive digestive system, and you eat oats, it’s important to pay close attention the source. Oats are heavily cross contaminated with wheat, which can occur anywhere between the milling to transportation stages.   

Agglutinins are proteins that induce the clumping of red blood cells in humans. They also appear in seeds to protect against fungal infection and insect predation. They are commonly found in wheat and legumes; in fact, crops are often genetically modified to contain higher levels of agglutinin to make them more hardy. However, they are just as difficult to digest as prolamins because they are very stable at both high temperature and low pH, making them resilient even in a hot pan or our acidic stomachs. Again, since they are hard to digest, they inevitably are sent to the digestive bacteria to be broken down, and in turn, creating digestive discomfort. Furthermore, they can cause inflammatory reactions if they leak out of the gut.                     

In addition to lectins, non-glutenous grains and pseudograins also contain digestive- enzyme inhibitors. These inhibitors protect the seed’s store of starches, sugars, and proteins. When they are released in the body, they can decrease the availability of nutrients in the body because they block the work of digestive enzymes. Finally, all grains contain phytic acid, which can bind with free minerals in the body and (once again) limit nutrient absorption.

Biological Inability to Digest Gluten: Celiac Disease and the Evolution of Gluten Sensitivity

Celiac disease is an autoimmune disease of the small intestine that is caused by a reaction to gliadin--an important protein that forms gluten. If a person with celiac disease eats gluten, a number of digestive issues will ensue. When gluten enters the digestive system, the enzyme tissue-transglutaminase (tTG) is called into action to break down the gliadin segments of the protein. During this process, the tTG forms a complex with the gliadin. In celiac patients, this complex is presented as an antigen (or antagonist) to the immune system, which stimulates an inflammatory reaction. This particular inflammatory reaction causes many problems. Perhaps the most detrimental is the truncation (shortening) of the intestinal villi. Intestinal villi are the primary sites of nutrient absorption in the gut. Once the villi are truncated or (worse-) eliminated, the body can no longer absorb nutrients from food. Minerals and fat-soluble vitamins like A, D, E, and K are particularly susceptible. If the body cannot absorb these nutrients, they are discarded as waste, leading to weight loss, anemia, osteopenia and osteoporosis, abnormal blood coagulation, and bacterial overgrowth in the intestine.

Due to the complexity of autoimmune conditions, untreated celiac disease can lead to an increased risk of adenocarcinoma and/or lymphoma of the small bowel. It is also associated with IgA deficiency (a lowered number of antibodies that protect against infections of the mucous membranes lining the mouth, airways, and digestive tract), an underactive spleen, abnormal liver function, and an increased risk of infections, autoimmune disease, dermatitis, growth failure, and pregnancy complications. Some health professionals believe that celiac disease is similarly linked with cerebellar ataxia, peripheral neuropathy, schizophrenia, and autism. Symptoms for celiac disease can manifest in the digestive system, the nervous system, or on the skin. However, some people with celiac disease don’t exhibit symptoms at all; they are considered asymptomatic.                        

Recent studies suggest that the presence of gliadin in the system triggers the initial celiac response, which is most often indicated by digestive upset. As the disease progresses, the modified tTG-gliadin complex triggers the production of antibodies to tTGs, which then leads to the secondary symptoms of the disease like headaches and skin problems.            

Nearly all celiac patients are genetically predisposed with genes that contain a variant code for creating protein receptors in the immune system, which are inclined to bind with gliadin more than other proteins. These particular receptors view gliadin as a pathogen and initiate the immune system. In other words, celiac DNA tells the body to make proteins that potentially mistake otherwise harmless cells for pathogens.

Celiac disease is among the most severe of gluten-related health conditions that poses serious risk and illness as a result of eating gluten. Perhaps this is why celiac disease has been discussed so commonly compared to gluten intolerance or other autoimmune disorders exacerbated by gluten. Whether or not gluten sensitivity has received the airtime it should require, gluten has a serious impact on many lives.

Dr. Fasano--Chair of Pediatrics at Harvard Medical School and Vice Chair of a division within Pediatric Gastroenterology and Nutrition at Massachusetts’ Hospital for Children--argues that the human body cannot break down the springy, elastic protein molecules completely. We simply don’t have the enzymes in our gut or intestines to break down it’s mapping. His idea speculates gluten is toxic for everyone, but not everyone will get sick. We stress the importance of the effects gluten can have on any body. Folks that have weak digestive systems or are trying to heal a leaky gut are susceptible to declining health if they choose to keep gluten in their diets.


Gluten Sensitivity: Not just your average trend


But, why is gluten suddenly a problem? For much of human history, we ate gluten without widespread disease or intolerance. While there have been written works about wheat allergies and descriptions of celiac-related deaths, unhealthy responses to wheat were never as pervasive as we’re seeing today.

Many researchers point toward a change in the ways in which we grow, manufacture, and eat wheat products to explain this phenomenon. Wheat was one of the first cereal grains to be grown on a large scale; it self-pollinates making it a relatively easy agricultural crop. In fact, the act of growing wheat is said to have led to the founding of large settlements and cities. After all, it is challenging to settle in one place if you’re constantly hunting and foraging for food! Subsequently became a popular mark of wealth, alongside oil, wheat didn’t go bad and there was an array of uses. Wheat has been important for a number of years, it’s not surprising that humans have altered its genetic composition.

So in addition to a genetic factor, there has to be an environmental factor that has attributed to the pervasiveness of celiac disease. Meaning, there needed to be a trigger to ignite an immune response. The gluten protein was only introduced into the human diet around 10,000 years. In the scale of human evolution (over the course of 2.4 million years), 10,000 years is a relatively tiny portion of time. Compounded with the our bodies evolving without gluten, the wheat crop itself has evolved, making the time that we have had to evolve together even substantially less. There has been three strains of wheat, with the last strain only being in our food systems for approximately 400 years.

All the way back in the 1500s, the wheat seed crop was mostly stock (nonedible), with seed accounting for only 5% of the crop. On top of that, it yielded just once a year. What we see today is a crop that yields 30% seed with 70% stock, and the ability to seed more than once. Moreover, as we mentioned above, grains are not built to give these nutrients away to predators like humans. Grains come packed with enzyme inhibitors and large, complex proteins like gluten that are difficult for humans to digest.

Looking at Standardized U.S. American Bread


The acts of soaking, sprouting, long fermentation, and cooking all work to break down these defensive walls of the grain, making the nutrients more bio-available. However, wheat consumption in the United States today, looks nothing like it did hundreds and thousands of years ago. Mass agriculture and food processing changed the modern strains of wheat from what it was centuries ago. In tandem with the Standard American Diet (SAD), which is rich in highly processed white flour, a whole host of problems are created and and further worsened by altered wheat strains.      

Our common American bread wheats have been bred specifically to contain high amounts of both gluten and simple starches in order to make mass bread production more efficient. Modern wheat varieties also exhibit an increase in the types of gliadin that most regularly stimulate inflammatory immune reactions. Most damningly, these inflammatory wheat varieties and their processed glutens are being used everywhere in food processing—not just in bread. As a whole, humans are consuming greater and greater numbers of wheat products and processed foods, raising their total intake of inflammatory gliadin molecules to a toxic level. The increased prevalence of these wheats is highly likely to have contributed to the increase in celiac disease and NCGS over the past few decades.                  

White flour also lacks almost any nutritive value—it has been stripped of both the bran and germ. The germ of the wheat grain is, in fact, the home to just about every nutrient in the grain (short of the fiber found in the bran). In addition, all of wheat’s beneficial enzymes are found in the germ, which means that sensitive eaters have little hope for digesting white flour on its own. A study out of the University of Minnesota found that even enriched white flours are not as beneficial as the whole grain itself.                     

This white flour is also most often used to bake breads leavened solely with commercial yeast. Commercial yeast is good for only one thing: baking bread quickly. It does little to improve taste, texture, and nutrients. Before the advent of large-scale food manufacturing and commercial yeast, most bread-eaters made their bread at home using natural sourdough leavening. Sourdough bread is not only more flavorful than bread made with commercial yeast; it has also been shown to be a far more effective method than yeast for disabling natural enzyme inhibitors in the grain and enabling nutrient absorption by neutralizing phytic acid. Sourdough also contributes its own beneficial yeasts and bacteria: think of it as the raw milk cheese of the bread world.           

Furthermore, some recent studies and anecdotal evidence has shown that sourdough bread made with extended fermentation might be tolerable by people who show a gluten intolerance, since the process begins to break down the gliadin molecules, the cause of so many problems. Lowering the toxicity of wheat via sourdough is an exciting prospect: while it likely won’t provide a source of wheat products for celiac patients, the study of low-toxicity wheat may help prevent the spread of the disease.                        

Many of these problems (and consequent solutions) wheat produces can be carried over to grains and seeds in general. All grains and seeds contain similar digestive inhibitors and phytates as well as large, hard-to-digest proteins like prolamins and agglutinins. Properly preparing these items by sprouting and fermenting can ease digestibility and make them far more beneficial. With that being said, it’s still important to keep an eye out for genetically modified ingredients and remaining cautious if engaged in a therapeutic diet to heal the gut.                     

Even so, how people tolerate food exists on an enormous spectrum, with no two people  same. Those who have celiac disease or have a particularly sensitive digestive system may still not be able to tolerate even the most properly prepared grains. We recognize that gluten and all other grains present challenges to many eaters, no matter how they are prepared so we play it safe in the kitchen by avoiding all gluten and grains 100%.

The alternatives: A delicious change in the right direction

When opting into a gluten-free lifestyle, it doesn’t mean making a mad dash to the gluten-free aisle. While many folks are recognizing bodily discomfort or sickness when eating gluten, companies have taken note of the trend, subsequently producing a plethora of options tailed to whatever the equivalent of a sweet tooth for bread is. But the reality of the gluten-free aisle is not much better than the gluten-filled crackers on the shelf below. They shouldn’t be considered an alternative, but amongst the ranks of food using fillers and processed additives that are remarkable unhealthy.

For example, fillers and additives can be found in looking at the simplest gluten-free product. 

"Water, modified tapioca starch, corn starch, potato starch, egg whites, canola oil and/or safflower oil, and/or sunflower oil, brown rice flour, tapioca starch, sugar, molasses, salt, poppy seeds, xantham gum, flax seed, sesame seeds, sugar beet fiber, sunflower seeds, glucono-delta-lactone, sodium bicarbonate, caramelized sugar, modified cellulose, calcium sulphate, enzymes

We think a diet based on whole foods and no chemicals is the best route to healthy and productive performance! We added an example for you to take a look at the ingredient list that reveals the processed fillers and chemicals found in gluten-free foods.

So, we’re not sorry we are so critical to foods that label themselves as healthy, especially when there are so many healthy options that are food-based! Instead of using glutenous and grain-filled flours in our kitchen, we make use of some interesting and flavorful grain-free flours like acorn flour, arrowroot flour, banana and plantain flour, chestnut flour, coconut flour, lotus root flour, lucuma powder, mesquite flour, sweet potato flour, tigernut flour, cassava starch, and whole cassava flour.

We’ve chosen these flours for many reasons (practical cookery included), and we pay especially close attention to the levels of resistant starch in the flour. Resistant starch is not digestible and functions much like insoluble fiber and the nutrient density. In fact, it is often referred to as the third dietary fiber. Sweet potato, plantain, acorn, banana, and cassava flour are all good sources of resistant starch.

We are currently delving through research to create a resource guide to resistant starch. Stay tuned for this article, as we think you’ll want to learn more about all the benefits and science behind resistant starch.