One of the biggest changes we’ve made for our own health is to eliminate gluten and grains from our culinary vocabulary. We’re sure that many of you avoid gluten yourself or know someone who does. Celiac disease and gluten sensitivity diagnoses have risen at least four-fold since the 1950s, and there is a growing body of research that suspects that gluten (and other grains) can cause harm even in individuals who don’t show signs of sensitivity.
In fact, gluten and other related proteins in grains, pseudograins, and legumes are difficult for even the healthiest individuals to digest. Since there is a potential for harm when eating gluten and grains, we’ve chosen to keep them out of our kitchen 100%. This makes our food suitable for celiac patients, NCGS patients, and (of course) everybody else.
CELEBRATE GRAIN-FREE FOOD!
Making the transition to a grain-free lifestyle can be challenging for everyone. But we’re here to help! Here are some easy tips and tricks.
Transform Your Vegetables: Grated carrots, zucchini ribbons, and radish swirls all add flavor-packed oomph to meals. Spiral cutters are great tools for transforming your vegetables, but you really don’t need to shell out for new equipment. Use your cheese grater on all kinds of root vegetables or turn your peeler into a ribbon-izer. Serve zucchini ribbons or shredded carrots under meatballs with nomato sauce or toss them in pesto like pasta.
Fun Flours: We view culinary requirements as creative opportunities. Eliminating grains from our kitchen has made room for all kinds of fun, unique flours that we use for everything from thickeners to grain-free crepes. Right now, our pantry is stocked with acorn starch, arrowroot flour, banana flour, chestnut flour, coconut flour, lucuma powder, mesquite flour, plantain flour, sweet potato flour, and tapioca flour.
Raw Garnishes: Start playing with garnishes. Flowers, pickles, and baby lettuces all add crisp texture and zip to every meal. Recently we’ve been loving lacto-fermented green beans and cucumber pickles made with lemon juice. We also love to use dehydrated vegetables like fennel, cabbage, and lotus root as crunchy toppings. Organic flowers are one of Chef Christian’s favorite finishing touches. Grow them yourself or seek them out at the farmer’s market.
Yucan Crunch: We’ve said it before, and we’ll say it again: We crave CRUNCH! Our crackers made from 100% yuca root add dynamic crunch to just about any meal. They’re a total blank slate for any kind of flavor combination, and they fill any void left by eliminating traditional bread, crackers, and chips.
Explore: There are lots of great resources for grain-free eating out there on the web and in bookstores. We love the blogs Against All Grain, Nom Nom Paleo, and Elana’s Pantry. If you prefer reading books, check out Your Personal Paleo Code by Chris Kresser (he also has a great blog), The Paleo Approach by Sarah Ballantyne, Practical Paleo by Diane Sanfilippo, and The Paleo Solution by Robb Wolf. We’ve also listed more books, blogs, and research at the bottom of this post and on our resources page.
NERD OUT ON GRAINS!
Gluten is the reason why bread rises. It is a large protein molecule that is found in wheat, rye, and barley. It is primarily made up of two (relatively) smaller protein molecules: glutenin and gliadin, each around 1000 amino acids long.
Glutenin and gliadin work together to form the strong, springy gluten matrix. Glutenin forms long chain-like molecules that bond easily with each other. These chains of glutenin molecules link up with each other in long super-chains that are each a few hundred glutenins long. Gliadin molecules, on the other hand, don’t like to bond with each other or with glutenin molecules. Instead, they fold up 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. This structure allows doughs that contain gluten to be both stretchy and springy: They are able to be manipulated, but tend to spring back to their original shape. Kneading doughs changes the alignment of the gluten molecules, bending their natural tendencies to work for us. The more a dough is kneaded, the stronger the gluten structure becomes. Relaxing a glutenous dough (or letting it rest) gives the glutenin coils a chance to become a little less springy, giving the baker an opportunity to shape the dough into a bread shape.
Celiac disease is an autoimmune disease of the small intestine that is caused by a reaction to gliadin. As mentioned above, gliadin is a protein in gluten. It contains a high amount of the amino acids proline and glutamine, and is therefore categorized as a prolamin protein. Because of their size, prolamins are generally hard to digest, but they don’t necessarily cause an autoimmune reaction in healthy individuals. The specific 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.
When a person suffering from celiac disease eats gluten a couple of things happen. When gluten enters the digestive system, an enzyme called 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 of which is the truncation (shortening) of the intestinal villi. Intestinal villi are the primary site 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.
In addition, when celiac patients—as well as gluten sensitive individuals, whom we will address in a moment—eat gluten, they increase the permeability of the small intestine. This condition, also called 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 signals for the production of proteins called zonulins. Zonulins are the proteins responsible for triggering the release of nutrients from the gut into the bloodstream and lymphatic system. If there is an overabundance of alpha-gliadin in the gut, it 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.
Because of 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. 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.
Almost all celiac patients inherit 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.
Non-Celiac Gluten Sensitivity (NCGS):
Not everyone who reacts poorly to gluten has celiac disease. There is a growing body of research that suggests that many people have a sensitivity or intolerance to gluten. The symptoms are similar to celiac disease and include bloating, abdominal discomfort, diarrhea, constipation, muscular disturbances, headaches, migraines, severe acne, fatigue, and bone or joint pain. Often, these symptoms appear less severe than celiac disease, but they can still be harmful to overall health.
Because it has relatively non-specific symptoms, NCGS can be tricky to diagnose. Many people who are indeed sensitive to gluten don’t have any digestive distress. Their symptoms can be concentrated in places like the nervous system or the skeletal system. There are expensive and specific tests that can diagnose NCGS based on the presence of certain antibodies, but 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.
The theory behind eliminating gluten from the diet is that gliadin can cause leaky gut in any individual, not just people with celiac disease. Gliadin has many properties that make it hard to digest including but not limited to the fact that it is a large protein molecule. As we mentioned above, some particular molecules of gliadin (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.
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.
On the other hand, other scientists argue that gluten’s propensity to cause intestinal permeability links it definitively to NCGS and other autoimmune conditions. Because there is a potential for harm when eating gluten, we have chosen to eliminate it from all of our cooking, making our meals suitable for celiac patients, NCGS patients, and completely healthy individuals.
Gluten-containing grains are not the only ones that can cause problems. 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 humans to digest 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 are very (very) 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!
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 incidence of leaky gut and the resulting inflammation.
Agglutinins are proteins that induce the clumping of red blood cells in humans and are used by seeds to protect against fungal infection and insect predation. Crops are often genetically modified to contain higher levels of agglutinin to make them more hardy. Agglutinins are found in wheat and legumes like soy, peanuts, and kidney beans. 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, leading to digestive upset. 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 nutrients in the grain and (once again) limit their absorption once they enter the body.
Grain-Free Flours and Resistant Starches:
Instead of using glutenous and grain-filled flours in our kitchen, we make use of some interesting and flavorful grain-free flours like acorn starch, arrowroot flour, banana flour, chestnut flour, coconut flour, lucuma powder, mesquite flour, plantain flour, sweet potato flour, and tapioca 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 a form of carbohydrate that is not digested in the stomach or intestines. Instead, it is transported to the colon, where it is a source of food for gut bacteria. As it is not digestible, resistant starch functions much like insoluble fiber. In fact, it is often referred to as the third dietary fiber. Sweet potato, plantain, acorn, banana, and tapioca flour are all good sources of resistant starch.
In proper levels, resistant starch is highly beneficial. Resistant starches have been shown to help aid weight loss as they increase satiety after eating, improve fatty acid metabolism, and both increase insulin sensitivity and decrease glycemic response. They also encourage the growth of healthy bacteria in the colon and aid in the production of a short-chain fatty acid called butyrate. Butyrate is the primary source of food for colon cells, and it has been shown to possess anticarcinogenic and anti-inflammatory qualities. Consuming resistant starch could therefore reduce the risk of developing colon cancer. On the other hand, since resistant starch increases the amount of bacteria in the colon, it can lead to digestive upset in people that have IBS, celiac, or leaky gut.
Why is gluten suddenly a problem?
For much of human history, we ate gluten without a rash of disease and intolerance, yet suddenly it has appeared to be a problem. Many researchers point towards a change in the ways in which we grow, manufacture wheat, and eat wheat products to explain this phenomenon.
It is thought that humans first began cultivating wheat 8,000 to 10,000 years ago. Wheat was one of the first cereal grains to be grown on a large scale; it self-pollinates and is therefore a relatively easy agricultural crop. 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!
Over time, humans discovered methods for making wheat more digestible and nutritious. They primarily crushed the grains to make porridge, and eventually discovered that porridge could be turned into bread with a little time and heat. Processing the wheat grains, even on this minor scale, is necessary to overcome the seed’s natural defenses. Each grain of wheat comes fully equipped with all of the necessary tool to propagate offspring. Many of these tools are beneficial to humans as well (complex starches, fiber, vitamin B complex, vitamin E, omega-3s, and carotene). However, 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. The acts of soaking, sprouting, fermenting, and cooking all work to break down these defensive walls of the grain, making the nutrients more bio-available.
In addition, it is thought that the human digestive system adapted to the abundance of these grains in their diet, acquiring digestive enzymes to break apart the wheat grains into their constituent beneficial amino acids, simple starches, and fatty acids. Baking naturally leavened bread further facilitates this process, as it involves soaking, sprouting, fermenting, and cooking.
However, our wheat consumption today looks nothing like it did hundreds and thousands of years ago. Most modern Westerners eat a diet rich in highly processed white flour, which comes along with a whole host of problems.
These modern strains of wheat look totally different than the wheat humans cultivated centuries ago. 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. One 2010 study showed that 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, upping 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 using 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 is even tolerable by people who show a gluten intolerance, as the process begins to break down the molecules of gliadin that cause 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) in wheat 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 make them far more digestible and beneficial.
However, all people have their own levels of tolerance for different food items. Those who are particularly sensitive or have celiac disease may still not be able to tolerate properly prepared grains. It is also important to note that there are many other foods (like meat and vegetables) that contain the same vitamins and minerals at higher proportions. Because we recognize that gluten and all other grains present challenges to many eaters no matter how they are prepared, and because much of this science is in its early stages, we play it safe by avoiding all gluten and grains 100 percent.
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