What has gluten in it?

Gluten (from Latin "gluten", "glue") is a composite of storage proteins termed prolamins and glutelins that is stored together with starch in the endosperm (which nourishes the embryonic plant during germination) of various cereal (grass) grains. It is found in wheat, barley, rye, oats and related species and hybrids (such as spelt, khorasan, emmer, einkorn, triticale, etc.), as well as products derived from these grains (such as breads and malts). Glutens, and most especially the Triticeae glutens, are appreciated for their viscoelastic properties, which give dough its elasticity, helping it rise and keep its shape and often leaving the final product with a chewy texture.

Gluten

Wheat, barley, rye and oat prolamins are respectively known as gliadins, hordeins, secalins and avenins; these protein classes are often collectively referred to as gluten. Wheat glutelins are called glutenin. True gluten is limited to the grains listed above. The storage proteins in maize and rice are sometimes called glutens, but they differ from true gluten.
In a small part of the general human population, gluten can trigger adverse autoimmune reactions responsible for a broad spectrum of gluten-related disorders, including coeliac disease, non-coeliac gluten sensitivity, gluten ataxia and dermatitis herpetiformis. Their treatment is the gluten-free diet. The occurrence of oat avenin toxicity depends on the oat cultivar consumed, because the immunoreactivities of toxic prolamins are different among oat varieties. Also, many oat products are cross-contaminated with other gluten-containing cereals.

Gluten is a protein complex that accounts for 75–85% of the total protein in bread wheat. In home or restaurant cooking, gluten is prepared from flour by kneading the flour under water, agglomerating the gluten into an elastic network known as a dough, and then washing out the starch. Starch granules disperse in low-temperature water, and the dispersed starch is sedimented and dried. If a saline solution is used instead of water, a purer protein is obtained, with certain harmless impurities departing the solution with the starch. Where starch is the prime product, cold water is the favored solvent because the impurities depart from the gluten.

In industrial production, a slurry of wheat flour is kneaded vigorously by machinery until the gluten agglomerates into a mass. This mass is collected by centrifugation, then transported through several stages integrated in a continuous process. About 65% of the water in the wet gluten is removed by means of a screw press; the remainder is sprayed through an atomizer nozzle into a drying chamber, where it remains at an elevated temperature for a short time to allow the water to evaporate without denaturing the gluten. The process yields a flour-like powder with a 7% moisture content, which is air cooled and pneumatically transported to a receiving vessel. In the final step, the processed gluten is sifted and milled to produce a uniform product.

Gluten forms when glutenin molecules cross-link via disulfide bonds to form a submicroscopic network attached to gliadin, which contributes viscosity (thickness) and extensibility to the mix. If this dough is leavened with yeast, fermentation produces carbon dioxide bubbles, which, trapped by the gluten network, cause the dough to rise. Baking coagulates the gluten, which, along with starch, stabilizes the shape of the final product. Gluten content has been implicated as a factor in the staling of bread, possibly because it binds water through hydration.

The formation of gluten affects the texture of the baked goods. Gluten's attainable elasticity is proportional to its content of glutenins with low molecular weights, as this portion contains the preponderance of the sulfur atoms responsible for the cross-linking in the gluten network.
Further refining of the gluten leads to chewier doughs such as those found in pizza and bagels, while less refining yields tender baked goods such as pastry products.

Generally, bread flours are high in gluten (hard wheat); pastry flours have a lower gluten content. Kneading promotes the formation of gluten strands and cross-links, creating baked products that are chewier (as opposed to more brittle or crumbly). The "chewiness" increases as the dough is kneaded for longer times. An increased moisture content in the dough enhances gluten development, and very wet doughs left to rise for a long time require no kneading (see no-knead bread). Shortening inhibits formation of cross-links and is used, along with diminished water and less kneading, when a tender and flaky product, such as a pie crust, is desired.

The strength and elasticity of gluten in flour is measured in the baking industry using a farinograph. This gives the baker a measurement of quality for different varieties of flours when developing recipes for various baked goods.

Gluten, when dried, milled and added to ordinary flour dough, may help improve the dough's ability to increase in volume. The resulting mixture also increases the bread's structural stability and chewiness. Gluten-added dough must be worked vigorously to induce it to rise to its full capacity; an automatic bread machine or food processor may be required for high-gluten kneading. Generally, higher gluten levels are associated with higher overall protein content.

Gluten, especially wheat gluten, is often the basis for imitation meats resembling beef, chicken, duck (see mock duck), fish and pork. When cooked in broth, gluten absorbs some of the surrounding liquid (including the flavor) and becomes firm to the bite. This use of gluten is a popular means of adding supplemental protein and variety to many vegetarian diets.

Gluten is often present in beer and soy sauce, and can be used as a stabilizing agent in more unexpected food products, such as ice cream and ketchup. Foods of this kind may therefore present problems for a small number of consumers because the hidden gluten constitutes a hazard for people with celiac disease and gluten sensitivities. The protein content of some pet foods may also be enhanced by adding gluten.

Gluten is also used in cosmetics, hair products and other dermatological preparations.

"Gluten-related disorders" is the umbrella term for all diseases triggered by gluten, which include celiac disease (CD), non-celiac gluten sensitivity (NCGS), wheat allergy, gluten ataxia and dermatitis herpetiformis (DH). Currently, their incidence is increasing in most geographic areas of the world. This can possibly be explained by the growing westernization of diets, the increasing use of wheat-based foods included in the Mediterranean diet, the progressive replacement of rice by wheat in many countries in Asia, the Middle East, and North Africa, the development in recent years of new types of wheat with a higher amount of cytotoxic gluten peptides, and the higher content of gluten in bread and bakery products due to the reduction of dough fermentation time.

Celiac disease (CD) is a chronic, multiple-organ autoimmune disorder primarily affecting the small intestine caused by the ingestion of wheat, barley, rye, oats, and derivatives, that appears in genetically predisposed people of all ages. CD is not only a gastrointestinal disease, because it may involve several organs and cause an extensive variety of non-gastrointestinal symptoms, and most importantly, it may be apparently asymptomatic. Many asymptomatic people actually are not, but have become accustomed to living with a chronic bad health status as if it were normal, and they are able to recognize that they actually had symptoms related to celiac disease after starting the gluten-free diet and improvement is evident, in contrast to the situation prior to the diet. Added difficulties for diagnosis are the fact that serological markers (anti-tissue transglutaminase [TG2]) are not always present and many people may have minor mucosal lesions, without atrophy of the intestinal villi.

CD affects approximately 1–2% of the general population, but most cases remain unrecognized, undiagnosed and untreated, and at risk for serious long-term health complications. People may suffer severe disease symptoms and be subjected to extensive investigations for many years, before a proper diagnosis is achieved. Untreated CD may cause malabsorption, reduced quality of life, iron deficiency, osteoporosis, an increased risk of intestinal lymphomas, and greater mortality. CD is associated with some other autoimmune diseases, such as diabetes mellitus type 1, thyroiditis, gluten ataxia, psoriasis, vitiligo, autoimmune hepatitis, dermatitis herpetiformis, primary sclerosing cholangitis, and more.

CD with "classic symptoms", which include gastrointestinal manifestations such as chronic diarrhea and abdominal distention, malabsorption, loss of appetite, and impaired growth, is currently the least common presentation form of the disease and affects predominantly small children generally younger than two years of age.

CD with "non-classic symptoms" is the most common clinical type and occurs in older children (over 2 years old), adolescents, and adults. It is characterized by milder or even absent gastrointestinal symptoms and a wide spectrum of non-intestinal manifestations that can involve any organ of the body, and very frequently may be completely asymptomatic both in children (at least in 43% of the cases) and adults.

Non-celiac gluten sensitivity (NCGS) is described as a condition of multiple symptoms that improves when switching to a gluten-free diet, after celiac disease and wheat allergy are excluded. Recognized since 2010, it is included among gluten-related disorders, but its pathogenesis is not yet well understood. NCGS is the most common syndrome of gluten intolerance, with a prevalence estimated to be 6-10%. NCGS is becoming a more common diagnosis, but its true prevalence is difficult to determine because many people self-diagnose and start the gluten-free diet, without having previously tested for celiac disease or doctor's recommendations. People with NCGS remain habitually in a "no man's land", without being recognized by the specialists and lacking the adequate medical care and treatment. Most of these people have a long history of health complaints and unsuccessful consultations with numerous physicians, and this is the reason why the majority of them end up resorting to a gluten-free diet and a self-diagnosis of gluten sensitivity.

People with NCGS may develop gastrointestinal symptoms, which resemble those of irritable bowel syndrome or wheat allergy, or a wide variety of non-gastrointestinal symptoms, such as headache, chronic fatigue, fibromyalgia, atopic diseases, allergies, neurological diseases, or psychiatric disorders, among others.

Besides gluten, additional components present in wheat, rye, barley, oats, and their derivatives, including other proteins called ATIs and short-chain carbohydrates known as FODMAPs, may cause NCGS symptoms. The effects of FODMAPs are only limited to gastrointestinal mild discomfort. ATIs may cause toll-like receptor 4 (TLR4)-mediated intestinal inflammation in humans.

People can also experience adverse effects of wheat as result of a wheat allergy. As with most allergies, a wheat allergy causes the immune system to abnormally respond to a component of wheat that it treats as a threatening foreign body. This immune response is often time-limited and does not cause lasting harm to body tissues. Wheat allergy and celiac disease are different disorders. Gastrointestinal symptoms of wheat allergy are similar to those of celiac disease and non-celiac gluten sensitivity, but there is a different interval between exposure to wheat and onset of symptoms. An allergic reaction to wheat has a fast onset (from minutes to hours) after the consumption of food containing wheat and could include anaphylaxis.

Gluten ataxia is an autoimmune disease triggered by the ingestion of gluten. With gluten ataxia, damage takes place in the cerebellum, the balance center of the brain that controls coordination and complex movements like walking, speaking and swallowing, with loss of Purkinje cells. People with gluten ataxia usually present gait abnormality or incoordination and tremor of the upper limbs. Gaze-evoked nystagmus and other ocular signs of cerebellar dysfunction are common. Myoclonus, palatal tremor, and opsoclonus-myoclonus may also appear.

Early diagnosis and treatment with a gluten-free diet can improve ataxia and prevent its progression. The effectiveness of the treatment depends on the elapsed time from the onset of the ataxia until diagnosis, because the death of neurons in the cerebellum as a result of gluten exposure is irreversible.

Gluten ataxia accounts for 40% of ataxias of unknown origin and 15% of all ataxias. Less than 10% of people with gluten ataxia present any gastrointestinal symptom, yet about 40% have intestinal damage.

The "Codex Alimentarius" international standards for food labeling has a standard relating to the labeling of products as "gluten-free". It only applies to foods that would normally contain gluten.

By law in Brazil, all food products must display labels clearly indicating whether or not they contain gluten.

The Canadian Celiac Association estimates that one in 133 Canadians experiences adverse symptoms from gluten in celiac disease. Labels for all food products sold in Canada must clearly identify the presence of gluten if it is present at a level greater than 20 parts per million.

In the European Union, all prepackaged foods and non-prepacked foods from a restaurant, take-out food wrapped just before sale, or unpackaged food served in institutions must be identified if gluten-free. "Gluten-free" is defined as 20 parts per million of gluten or less and "very low gluten" is 100 parts per million of gluten or less; only foods with cereal ingredients processed to remove gluten can claim "very low gluten" on labels.

All foods containing gluten as an ingredient must be labelled accordingly as gluten is defined as one of the 14 recognised EU allergens.

In the United States, gluten is not listed on labels unless added as a standalone ingredient. Wheat or other allergens are listed after the ingredient line. The US Food and Drug Administration (FDA) has historically classified gluten as "generally recognized as safe" (GRAS). In August 2013, the FDA issued a final ruling, effective August 2014, that defined the term "gluten-free" for voluntary use in the labeling of foods as meaning that the amount of gluten contained in the food is below 20 parts per million.

Gluten

Gluten forms when glutenin molecules cross-link via disulfide bonds to form a submicroscopic network attached to gliadin, which contributes viscosity (thickness) and extensibility to the mix. If this dough is leavened with yeast, fermentation produces carbon dioxide bubbles, which, trapped by the gluten network, cause the dough to rise. Baking coagulates the gluten, which, along with starch, stabilizes the shape of the final product. Gluten content has been implicated as a factor in the staling of bread, possibly because it binds water through hydration.

The formation of gluten affects the texture of the baked goods. Gluten's attainable elasticity is proportional to its content of glutenins with low molecular weights, as this portion contains the preponderance of the sulfur atoms responsible for the cross-linking in the gluten network.
Further refining of the gluten leads to chewier doughs such as those found in pizza and bagels, while less refining yields tender baked goods such as pastry products.

The strength and elasticity of gluten in flour is measured in the baking industry using a farinograph. This gives the baker a measurement of quality for different varieties of flours when developing recipes for various baked goods.

Gluten, when dried, milled and added to ordinary flour dough, may help improve the dough's ability to increase in volume. The resulting mixture also increases the bread's structural stability and chewiness. Gluten-added dough must be worked vigorously to induce it to rise to its full capacity; an automatic bread machine or food processor may be required for high-gluten kneading. Generally, higher gluten levels are associated with higher overall protein content.

Gluten, especially wheat gluten, is often the basis for imitation meats resembling beef, chicken, duck (see mock duck), fish and pork. When cooked in broth, gluten absorbs some of the surrounding liquid (including the flavor) and becomes firm to the bite. This use of gluten is a popular means of adding supplemental protein and variety to many vegetarian diets.

Gluten is often present in beer and soy sauce, and can be used as a stabilizing agent in more unexpected food products, such as ice cream and ketchup. Foods of this kind may therefore present problems for a small number of consumers because the hidden gluten constitutes a hazard for people with celiac disease and gluten sensitivities. The protein content of some pet foods may also be enhanced by adding gluten.

Gluten is also used in cosmetics, hair products and other dermatological preparations.

CD with "classic symptoms", which include gastrointestinal manifestations such as chronic diarrhea and abdominal distention, malabsorption, loss of appetite, and impaired growth, is currently the least common presentation form of the disease and affects predominantly small children generally younger than two years of age.

CD with "non-classic symptoms" is the most common clinical type and occurs in older children (over 2 years old), adolescents, and adults. It is characterized by milder or even absent gastrointestinal symptoms and a wide spectrum of non-intestinal manifestations that can involve any organ of the body, and very frequently may be completely asymptomatic both in children (at least in 43% of the cases) and adults.

People with NCGS may develop gastrointestinal symptoms, which resemble those of irritable bowel syndrome or wheat allergy, or a wide variety of non-gastrointestinal symptoms, such as headache, chronic fatigue, fibromyalgia, atopic diseases, allergies, neurological diseases, or psychiatric disorders, among others.

Besides gluten, additional components present in wheat, rye, barley, oats, and their derivatives, including other proteins called ATIs and short-chain carbohydrates known as FODMAPs, may cause NCGS symptoms. The effects of FODMAPs are only limited to gastrointestinal mild discomfort. ATIs may cause toll-like receptor 4 (TLR4)-mediated intestinal inflammation in humans.

Gluten ataxia is an autoimmune disease triggered by the ingestion of gluten. With gluten ataxia, damage takes place in the cerebellum, the balance center of the brain that controls coordination and complex movements like walking, speaking and swallowing, with loss of Purkinje cells. People with gluten ataxia usually present gait abnormality or incoordination and tremor of the upper limbs. Gaze-evoked nystagmus and other ocular signs of cerebellar dysfunction are common. Myoclonus, palatal tremor, and opsoclonus-myoclonus may also appear.

Early diagnosis and treatment with a gluten-free diet can improve ataxia and prevent its progression. The effectiveness of the treatment depends on the elapsed time from the onset of the ataxia until diagnosis, because the death of neurons in the cerebellum as a result of gluten exposure is irreversible.

Gluten ataxia accounts for 40% of ataxias of unknown origin and 15% of all ataxias. Less than 10% of people with gluten ataxia present any gastrointestinal symptom, yet about 40% have intestinal damage.

The "Codex Alimentarius" international standards for food labeling has a standard relating to the labeling of products as "gluten-free". It only applies to foods that would normally contain gluten.

By law in Brazil, all food products must display labels clearly indicating whether or not they contain gluten.

The Canadian Celiac Association estimates that one in 133 Canadians experiences adverse symptoms from gluten in celiac disease. Labels for all food products sold in Canada must clearly identify the presence of gluten if it is present at a level greater than 20 parts per million.

In the European Union, all prepackaged foods and non-prepacked foods from a restaurant, take-out food wrapped just before sale, or unpackaged food served in institutions must be identified if gluten-free. "Gluten-free" is defined as 20 parts per million of gluten or less and "very low gluten" is 100 parts per million of gluten or less; only foods with cereal ingredients processed to remove gluten can claim "very low gluten" on labels.

All foods containing gluten as an ingredient must be labelled accordingly as gluten is defined as one of the 14 recognised EU allergens.

In the United States, gluten is not listed on labels unless added as a standalone ingredient. Wheat or other allergens are listed after the ingredient line. The US Food and Drug Administration (FDA) has historically classified gluten as "generally recognized as safe" (GRAS). In August 2013, the FDA issued a final ruling, effective August 2014, that defined the term "gluten-free" for voluntary use in the labeling of foods as meaning that the amount of gluten contained in the food is below 20 parts per million.

Gluten forms when glutenin molecules cross-link via disulfide bonds to form a submicroscopic network attached to gliadin, which contributes viscosity (thickness) and extensibility to the mix. If this dough is leavened with yeast, fermentation produces carbon dioxide bubbles, which, trapped by the gluten network, cause the dough to rise. Baking coagulates the gluten, which, along with starch, stabilizes the shape of the final product. Gluten content has been implicated as a factor in the staling of bread, possibly because it binds water through hydration.

Gluten

The formation of gluten affects the texture of the baked goods. Gluten's attainable elasticity is proportional to its content of glutenins with low molecular weights, as this portion contains the preponderance of the sulfur atoms responsible for the cross-linking in the gluten network.
Further refining of the gluten leads to chewier doughs such as those found in pizza and bagels, while less refining yields tender baked goods such as pastry products.

The strength and elasticity of gluten in flour is measured in the baking industry using a farinograph. This gives the baker a measurement of quality for different varieties of flours when developing recipes for various baked goods.

Gluten, when dried, milled and added to ordinary flour dough, may help improve the dough's ability to increase in volume. The resulting mixture also increases the bread's structural stability and chewiness. Gluten-added dough must be worked vigorously to induce it to rise to its full capacity; an automatic bread machine or food processor may be required for high-gluten kneading. Generally, higher gluten levels are associated with higher overall protein content.

Gluten, especially wheat gluten, is often the basis for imitation meats resembling beef, chicken, duck (see mock duck), fish and pork. When cooked in broth, gluten absorbs some of the surrounding liquid (including the flavor) and becomes firm to the bite. This use of gluten is a popular means of adding supplemental protein and variety to many vegetarian diets.

Gluten is often present in beer and soy sauce, and can be used as a stabilizing agent in more unexpected food products, such as ice cream and ketchup. Foods of this kind may therefore present problems for a small number of consumers because the hidden gluten constitutes a hazard for people with celiac disease and gluten sensitivities. The protein content of some pet foods may also be enhanced by adding gluten.

Gluten is also used in cosmetics, hair products and other dermatological preparations.

CD with "classic symptoms", which include gastrointestinal manifestations such as chronic diarrhea and abdominal distention, malabsorption, loss of appetite, and impaired growth, is currently the least common presentation form of the disease and affects predominantly small children generally younger than two years of age.

CD with "non-classic symptoms" is the most common clinical type and occurs in older children (over 2 years old), adolescents, and adults. It is characterized by milder or even absent gastrointestinal symptoms and a wide spectrum of non-intestinal manifestations that can involve any organ of the body, and very frequently may be completely asymptomatic both in children (at least in 43% of the cases) and adults.

People with NCGS may develop gastrointestinal symptoms, which resemble those of irritable bowel syndrome or wheat allergy, or a wide variety of non-gastrointestinal symptoms, such as headache, chronic fatigue, fibromyalgia, atopic diseases, allergies, neurological diseases, or psychiatric disorders, among others.

Besides gluten, additional components present in wheat, rye, barley, oats, and their derivatives, including other proteins called ATIs and short-chain carbohydrates known as FODMAPs, may cause NCGS symptoms. The effects of FODMAPs are only limited to gastrointestinal mild discomfort. ATIs may cause toll-like receptor 4 (TLR4)-mediated intestinal inflammation in humans.

Gluten ataxia is an autoimmune disease triggered by the ingestion of gluten. With gluten ataxia, damage takes place in the cerebellum, the balance center of the brain that controls coordination and complex movements like walking, speaking and swallowing, with loss of Purkinje cells. People with gluten ataxia usually present gait abnormality or incoordination and tremor of the upper limbs. Gaze-evoked nystagmus and other ocular signs of cerebellar dysfunction are common. Myoclonus, palatal tremor, and opsoclonus-myoclonus may also appear.

Early diagnosis and treatment with a gluten-free diet can improve ataxia and prevent its progression. The effectiveness of the treatment depends on the elapsed time from the onset of the ataxia until diagnosis, because the death of neurons in the cerebellum as a result of gluten exposure is irreversible.

Gluten ataxia accounts for 40% of ataxias of unknown origin and 15% of all ataxias. Less than 10% of people with gluten ataxia present any gastrointestinal symptom, yet about 40% have intestinal damage.

The "Codex Alimentarius" international standards for food labeling has a standard relating to the labeling of products as "gluten-free". It only applies to foods that would normally contain gluten.

By law in Brazil, all food products must display labels clearly indicating whether or not they contain gluten.

The Canadian Celiac Association estimates that one in 133 Canadians experiences adverse symptoms from gluten in celiac disease. Labels for all food products sold in Canada must clearly identify the presence of gluten if it is present at a level greater than 20 parts per million.

In the European Union, all prepackaged foods and non-prepacked foods from a restaurant, take-out food wrapped just before sale, or unpackaged food served in institutions must be identified if gluten-free. "Gluten-free" is defined as 20 parts per million of gluten or less and "very low gluten" is 100 parts per million of gluten or less; only foods with cereal ingredients processed to remove gluten can claim "very low gluten" on labels.

All foods containing gluten as an ingredient must be labelled accordingly as gluten is defined as one of the 14 recognised EU allergens.

In the United States, gluten is not listed on labels unless added as a standalone ingredient. Wheat or other allergens are listed after the ingredient line. The US Food and Drug Administration (FDA) has historically classified gluten as "generally recognized as safe" (GRAS). In August 2013, the FDA issued a final ruling, effective August 2014, that defined the term "gluten-free" for voluntary use in the labeling of foods as meaning that the amount of gluten contained in the food is below 20 parts per million.

Gluten, especially wheat gluten, is often the basis for imitation meats resembling beef, chicken, duck (see mock duck), fish and pork. When cooked in broth, gluten absorbs some of the surrounding liquid (including the flavor) and becomes firm to the bite. This use of gluten is a popular means of adding supplemental protein and variety to many vegetarian diets.

Gluten

Gluten forms when glutenin molecules cross-link via disulfide bonds to form a submicroscopic network attached to gliadin, which contributes viscosity (thickness) and extensibility to the mix. If this dough is leavened with yeast, fermentation produces carbon dioxide bubbles, which, trapped by the gluten network, cause the dough to rise. Baking coagulates the gluten, which, along with starch, stabilizes the shape of the final product. Gluten content has been implicated as a factor in the staling of bread, possibly because it binds water through hydration.

The formation of gluten affects the texture of the baked goods. Gluten's attainable elasticity is proportional to its content of glutenins with low molecular weights, as this portion contains the preponderance of the sulfur atoms responsible for the cross-linking in the gluten network.
Further refining of the gluten leads to chewier doughs such as those found in pizza and bagels, while less refining yields tender baked goods such as pastry products.

The strength and elasticity of gluten in flour is measured in the baking industry using a farinograph. This gives the baker a measurement of quality for different varieties of flours when developing recipes for various baked goods.

Gluten, when dried, milled and added to ordinary flour dough, may help improve the dough's ability to increase in volume. The resulting mixture also increases the bread's structural stability and chewiness. Gluten-added dough must be worked vigorously to induce it to rise to its full capacity; an automatic bread machine or food processor may be required for high-gluten kneading. Generally, higher gluten levels are associated with higher overall protein content.

Gluten is often present in beer and soy sauce, and can be used as a stabilizing agent in more unexpected food products, such as ice cream and ketchup. Foods of this kind may therefore present problems for a small number of consumers because the hidden gluten constitutes a hazard for people with celiac disease and gluten sensitivities. The protein content of some pet foods may also be enhanced by adding gluten.

Gluten is also used in cosmetics, hair products and other dermatological preparations.

CD with "classic symptoms", which include gastrointestinal manifestations such as chronic diarrhea and abdominal distention, malabsorption, loss of appetite, and impaired growth, is currently the least common presentation form of the disease and affects predominantly small children generally younger than two years of age.

CD with "non-classic symptoms" is the most common clinical type and occurs in older children (over 2 years old), adolescents, and adults. It is characterized by milder or even absent gastrointestinal symptoms and a wide spectrum of non-intestinal manifestations that can involve any organ of the body, and very frequently may be completely asymptomatic both in children (at least in 43% of the cases) and adults.

People with NCGS may develop gastrointestinal symptoms, which resemble those of irritable bowel syndrome or wheat allergy, or a wide variety of non-gastrointestinal symptoms, such as headache, chronic fatigue, fibromyalgia, atopic diseases, allergies, neurological diseases, or psychiatric disorders, among others.

Besides gluten, additional components present in wheat, rye, barley, oats, and their derivatives, including other proteins called ATIs and short-chain carbohydrates known as FODMAPs, may cause NCGS symptoms. The effects of FODMAPs are only limited to gastrointestinal mild discomfort. ATIs may cause toll-like receptor 4 (TLR4)-mediated intestinal inflammation in humans.

Gluten ataxia is an autoimmune disease triggered by the ingestion of gluten. With gluten ataxia, damage takes place in the cerebellum, the balance center of the brain that controls coordination and complex movements like walking, speaking and swallowing, with loss of Purkinje cells. People with gluten ataxia usually present gait abnormality or incoordination and tremor of the upper limbs. Gaze-evoked nystagmus and other ocular signs of cerebellar dysfunction are common. Myoclonus, palatal tremor, and opsoclonus-myoclonus may also appear.

Early diagnosis and treatment with a gluten-free diet can improve ataxia and prevent its progression. The effectiveness of the treatment depends on the elapsed time from the onset of the ataxia until diagnosis, because the death of neurons in the cerebellum as a result of gluten exposure is irreversible.

Gluten ataxia accounts for 40% of ataxias of unknown origin and 15% of all ataxias. Less than 10% of people with gluten ataxia present any gastrointestinal symptom, yet about 40% have intestinal damage.

The "Codex Alimentarius" international standards for food labeling has a standard relating to the labeling of products as "gluten-free". It only applies to foods that would normally contain gluten.

By law in Brazil, all food products must display labels clearly indicating whether or not they contain gluten.

The Canadian Celiac Association estimates that one in 133 Canadians experiences adverse symptoms from gluten in celiac disease. Labels for all food products sold in Canada must clearly identify the presence of gluten if it is present at a level greater than 20 parts per million.

In the European Union, all prepackaged foods and non-prepacked foods from a restaurant, take-out food wrapped just before sale, or unpackaged food served in institutions must be identified if gluten-free. "Gluten-free" is defined as 20 parts per million of gluten or less and "very low gluten" is 100 parts per million of gluten or less; only foods with cereal ingredients processed to remove gluten can claim "very low gluten" on labels.

All foods containing gluten as an ingredient must be labelled accordingly as gluten is defined as one of the 14 recognised EU allergens.

In the United States, gluten is not listed on labels unless added as a standalone ingredient. Wheat or other allergens are listed after the ingredient line. The US Food and Drug Administration (FDA) has historically classified gluten as "generally recognized as safe" (GRAS). In August 2013, the FDA issued a final ruling, effective August 2014, that defined the term "gluten-free" for voluntary use in the labeling of foods as meaning that the amount of gluten contained in the food is below 20 parts per million.

Gluten is often present in beer and soy sauce, and can be used as a stabilizing agent in more unexpected food products, such as ice cream and ketchup. Foods of this kind may therefore present problems for a small number of consumers because the hidden gluten constitutes a hazard for people with celiac disease and gluten sensitivities. The protein content of some pet foods may also be enhanced by adding gluten.

Gluten

Gluten forms when glutenin molecules cross-link via disulfide bonds to form a submicroscopic network attached to gliadin, which contributes viscosity (thickness) and extensibility to the mix. If this dough is leavened with yeast, fermentation produces carbon dioxide bubbles, which, trapped by the gluten network, cause the dough to rise. Baking coagulates the gluten, which, along with starch, stabilizes the shape of the final product. Gluten content has been implicated as a factor in the staling of bread, possibly because it binds water through hydration.

The formation of gluten affects the texture of the baked goods. Gluten's attainable elasticity is proportional to its content of glutenins with low molecular weights, as this portion contains the preponderance of the sulfur atoms responsible for the cross-linking in the gluten network.
Further refining of the gluten leads to chewier doughs such as those found in pizza and bagels, while less refining yields tender baked goods such as pastry products.

The strength and elasticity of gluten in flour is measured in the baking industry using a farinograph. This gives the baker a measurement of quality for different varieties of flours when developing recipes for various baked goods.

Gluten, when dried, milled and added to ordinary flour dough, may help improve the dough's ability to increase in volume. The resulting mixture also increases the bread's structural stability and chewiness. Gluten-added dough must be worked vigorously to induce it to rise to its full capacity; an automatic bread machine or food processor may be required for high-gluten kneading. Generally, higher gluten levels are associated with higher overall protein content.

Gluten, especially wheat gluten, is often the basis for imitation meats resembling beef, chicken, duck (see mock duck), fish and pork. When cooked in broth, gluten absorbs some of the surrounding liquid (including the flavor) and becomes firm to the bite. This use of gluten is a popular means of adding supplemental protein and variety to many vegetarian diets.

Gluten is also used in cosmetics, hair products and other dermatological preparations.

CD with "classic symptoms", which include gastrointestinal manifestations such as chronic diarrhea and abdominal distention, malabsorption, loss of appetite, and impaired growth, is currently the least common presentation form of the disease and affects predominantly small children generally younger than two years of age.

CD with "non-classic symptoms" is the most common clinical type and occurs in older children (over 2 years old), adolescents, and adults. It is characterized by milder or even absent gastrointestinal symptoms and a wide spectrum of non-intestinal manifestations that can involve any organ of the body, and very frequently may be completely asymptomatic both in children (at least in 43% of the cases) and adults.

People with NCGS may develop gastrointestinal symptoms, which resemble those of irritable bowel syndrome or wheat allergy, or a wide variety of non-gastrointestinal symptoms, such as headache, chronic fatigue, fibromyalgia, atopic diseases, allergies, neurological diseases, or psychiatric disorders, among others.

Besides gluten, additional components present in wheat, rye, barley, oats, and their derivatives, including other proteins called ATIs and short-chain carbohydrates known as FODMAPs, may cause NCGS symptoms. The effects of FODMAPs are only limited to gastrointestinal mild discomfort. ATIs may cause toll-like receptor 4 (TLR4)-mediated intestinal inflammation in humans.

Gluten ataxia is an autoimmune disease triggered by the ingestion of gluten. With gluten ataxia, damage takes place in the cerebellum, the balance center of the brain that controls coordination and complex movements like walking, speaking and swallowing, with loss of Purkinje cells. People with gluten ataxia usually present gait abnormality or incoordination and tremor of the upper limbs. Gaze-evoked nystagmus and other ocular signs of cerebellar dysfunction are common. Myoclonus, palatal tremor, and opsoclonus-myoclonus may also appear.

Early diagnosis and treatment with a gluten-free diet can improve ataxia and prevent its progression. The effectiveness of the treatment depends on the elapsed time from the onset of the ataxia until diagnosis, because the death of neurons in the cerebellum as a result of gluten exposure is irreversible.

Gluten ataxia accounts for 40% of ataxias of unknown origin and 15% of all ataxias. Less than 10% of people with gluten ataxia present any gastrointestinal symptom, yet about 40% have intestinal damage.

The "Codex Alimentarius" international standards for food labeling has a standard relating to the labeling of products as "gluten-free". It only applies to foods that would normally contain gluten.

By law in Brazil, all food products must display labels clearly indicating whether or not they contain gluten.

The Canadian Celiac Association estimates that one in 133 Canadians experiences adverse symptoms from gluten in celiac disease. Labels for all food products sold in Canada must clearly identify the presence of gluten if it is present at a level greater than 20 parts per million.

In the European Union, all prepackaged foods and non-prepacked foods from a restaurant, take-out food wrapped just before sale, or unpackaged food served in institutions must be identified if gluten-free. "Gluten-free" is defined as 20 parts per million of gluten or less and "very low gluten" is 100 parts per million of gluten or less; only foods with cereal ingredients processed to remove gluten can claim "very low gluten" on labels.

All foods containing gluten as an ingredient must be labelled accordingly as gluten is defined as one of the 14 recognised EU allergens.

In the United States, gluten is not listed on labels unless added as a standalone ingredient. Wheat or other allergens are listed after the ingredient line. The US Food and Drug Administration (FDA) has historically classified gluten as "generally recognized as safe" (GRAS). In August 2013, the FDA issued a final ruling, effective August 2014, that defined the term "gluten-free" for voluntary use in the labeling of foods as meaning that the amount of gluten contained in the food is below 20 parts per million.

Gluten is the seed storage protein in mature wheat seeds (and in the seeds of closely related species). It is the sticky substance in bread wheat which allows dough to rise and retain its shape during baking. The same, or very similar, proteins are also found in related grasses within the tribe Triticeae. Seed glutens of some non-Triticeae plants have similar properties, but none can perform on a par with those of the Triticeae taxa, particularly the "Triticum" species (bread wheat, durum wheat, etc.). What distinguishes bread wheat from these other grass seeds is the quantity of these proteins and the level of subcomponents, with bread wheat having the highest protein content and a complex mixture of proteins derived from three grass species ("Aegilops speltoides", "Aegilops tauschii strangulata", and "Triticum monococcum").

Triticeae glutens

Triticeae seed proteins fall into four groups:

Of these proteins the last two, prolamin (in wheat – gliadin) and glutelin (in wheat – glutenin) form the classically defined gluten components in wheat.

Triticeae glutens are primarily important to a developing definition 'gluten-free' in dietary treatments for gluten sensitivity which are intended to exclude pathogenic proteins from the diet of susceptible individuals (namely coeliac disease). The poisonous motifs appear to be spread widely in Triticeae, but not other taxa, for most coeliacs. However all four proteins are involved in wheat allergies, and proteins from non-wheats may not be involved in certain gluten allergies, or in idiopathic sensitivities.

Proteins of the Triticeae endosperm that are generally rich in arginine, proline, glutamine, and/or asparagine.

Because of the usefulness of wheat glutens, genetic studies have largely focused on wheat genetics. Wheat has three genomes (AABBDD) and it can encode for many variations of the same protein, even in the gliadin subcategories many types of gliadin per cultivar, "X" = genome (A, B, or D genome chromosomes (1 to 7)). The A and B genomes are derived from wild emmers wheat which in turn is a natural digenomic species that contains a "Triticum monococcum"- and "Aegilops speltoides"-like genome. The D genome is derived from the extant species "Aegilops tauschii strangulatum".The genetic studies indicate that in wheat, each protein type can be encoded by several loci and several different alleles for each loci can be found in different genomes, allowing a great number of uniquely encoded isoforms.Prolamins and to a lesser degree glutelins are excellent substrates for deamidation particularly by mammalian tissue transglutaminases (tTG). Deamidation is a process in which the R-C0-NH2 portion of glutamines (or asparagine) is hydrolyzed to R-CO-OH forming glutamic acid or aspartic acid. In gliadin, the -QQP-, -QVP-, -QLP-, -QYP- tripeptides in the context of favorable adjacent peptides are readily deamidated. Most proteins have few or no such transglutaminase sites; however alpha gliadin has 13 such sites. Human tissue transglutaminase not only deamidates gliadin, but it also crosslinks itself to gliadin, which has immunological consequences. Gliadin also has a small peptide that appears to alter the distribution of transglutaminase in the gut but is not crosslinked, the mechanism of its 'innate' behavior is not clear. tTG also crosslinks gliadin to other proteins via these sites, generating anti-food responses, anti-self protein responses, and self-crossreactive responses to food proteins that result in secondary autoimmunities.
The role of tTG in the extracellular matrix is to crosslink lysine side chains of proteins such as collagen to proteins, however glutens appear to infiltrate into the small intestine, interfering with this process and resulting in a false immune recognition of the matrix and surrounding cells as "foreign", leading, ultimately, to
the destruction of the intestinal mucosa. Seeds of certain plants may elicit the innate and cellular responses as a defensive response to overconsumption of seeds.

While prolamins and glutelins are excellent deamidase and transaminase substrates the highly repetitive motifs, particularly polyproline/glutamine tracts, are often poor substrates for gastroentestinal endoproteases, such as those produced in the GI tract. One clear example is a 33-mer of α-2 gliadin. Another digestion resistant region is a 25-mer
which contains the innate peptide. The alpha gliadins, which bear these sites, specifically are poisonous to young rats when fed at concentrations higher than 1% and the addition of mannosidase inhibitors increases the sensitivity specifically to alpha gliadins. These properties of certain alpha-gliadins appear to have evolved to prevent long-term or dedicated consumption of certain wheat grasses by certain species.
This is one of the ironic properties of wheat, since a major advantage of wheat is the amount of protein in the wheat, however, some of this is wasted to the gut flora (or host immune system) since it cannot be broken down. One suggested remedy to this problem are new enzymes that help specifically break prolamins in the stomach. This may prevent the onset of wheat related disease in susceptible individuals, but no such screening is currently effective and once the clinical state is reached most individuals are so sensitive to wheat gliadins that, effectively, complete digestion in the stomach would be required.

The immunochemistry of Triticeae is important in several autoimmune diseases (see section on Human Disease), and gluten sensitivity and gluten allergy in general. It can be subdivided into innate responses (direct stimulation of immune system), Class II mediated presentation (HLA DQ), Class I meditiated stimulation of killer cells, and Antibody recognition. The DQ restricted class II mediated presentation of gliadin to T-helper lymphocytes appears to be the primary process involved in coeliac disease.

Glutens are an essential part of the modern food industry. The industry of wheat goes back to before the Neolithic period when people process grain berries (or corns) singley by hand. During the early phase of cultivation wheats were selected for their harvestability and growability under various climate conditions resulting in the first cultivars. This industry spread into many areas of western Eurasia during neolithization, carrying the more primitive cultivars. These grains were capable of being used for soups (speltiods) or tediously ground into simple flours and baked goods. During the second phase an Emmer wheat was produced that was an alloquadraploid species and this contained more gluten, making baking more efficient. This also spread during the neolithization but in places such cultivars were a minority.
One variant of emmer wheat is called durum wheat and is the source of semolina flour, used in making pastas and other food pastes. Comparable varieties are found throughout Eurasia. Finally, emmers wheat was combined with a goat grass (Aegilops tauschii) to form allohexaploid bread wheat, which has a soft fine texture after rising and cooking. The industrial properties of this wheat are based in its glutens, glutens of high elasticity, high heat tolerance of other glutens or that change when subjected to heat to produce stronger polymers.

Corn is prepared for breading by boiling in water with alkali, resulting in a de-skinned material called nixtamalized masa. Masa can be used for industrial purposes (tortillas, tamales, chips), but it must be used quickly because its glutens change rapidly and binding decreases rapidly. Masa does not store well and chemicals are added to enhance preservation at the expense of quality. At its peak attempting to use masa as dough generally results in a crumbly flat bread, correctable by regrinding masa to a fine flour and adding gums (such as xanthan gum). In contrast the glutens in wheat have more adhesive properties that change when prepared in different ways. The glutenins, for example, stretch, but can also fix their shape at high temperatures, causing bread to maintain
its characteristic rise.

When the flour is combined with water and yeast the dough can be risen and subsequently fixed by heat resulting in a hard outer shell with a soft palatable interior. This makes bread amicable for both transport and preserves the bread for several days (in dry conditions). Barley can be sprouted for a short period and roasted, the resulting malt can be ground for food or combined with bread yeast (currently a brewers variety) to produce beer and distilled spirits such as whiskey, vodka and sourdough malts. Adding mild acid to rye flour activates it for bread making (Sourdough breads used in northern Europe).

Adding egg to "T. durum" semolina flour can be used to make pastas, or without egg a pasta variant used to make Chinese dumplings. Wheat or semolina flour can be added other ingredients such as fish, meat or milk to create food pastes. Wheat can be further processed to a very fine flour and sifted, alternatively the glutens either can be extracted and readded to other products. While many seed glutens and food gums when combined with food starch, come close to creating the refined products of wheat flour and durum flour, no combination has yet come close to the qualities of these flours at a comparable price.

Some triticeae cultivars, like barley, have relatively low protein values. This makes them more acceptable for brewing without wasting soil nutrients. Seed storage proteins in grass seeds (i.e., gluten in wheat) are designed to help the plant grow during its early life, and among the seed proteins are enzymes that convert starch to sugar. These proteins are activated during sprouting and the starch around the endosperm is converted to sugars. Later the prolamins are broken down to provide the young seeds with a source of nitrogen and energy giving the Triticeae seedling a great boost during early life.

Once the starch is converted to sugar it can be readily fermented by "Saccharomyces cerevisiae". However, first the sprouting process should be stopped. In order to do this, the partially sprouted grains are placed in a roasting oven and roasted until the sprouts are sterilized and dried. This process of sprouting and drying is called malting. Then the roasted sprouts are ground, rehydrated and fermented. This produces a crude beer.

The deamidation potential for wheats is discussed above. Glutens are generated by the wheat starch industry. Glutens however are more difficult to handle once starch and other proteins are removed, for example, alcohol-soluble glutens cannot be mixed with dairy since the alcohol denatures and precipitates dairy proteins. Therefore, gluten is often modified for commercial use by deamidation by treatment with acid at high temperatures, or enzymatic treatment with deamidase or transglutaminases. The increased charge increases the hydrophilicity of gliadins, causing them to stretch out in solution. Deamidation of 20% of glutamine side chains to glutamate suffices to generate a soluble product. This renders gluten soluble enough without alcohol to mix with other products like milk.

Individuals who suffer from gluten-sensitive enteropathy/coeliac disease have an adverse reaction to the gluten in cultivars of Triticeae when eaten. In addition to bread wheat, rye and barley (which have similar glutens) are known to cause symptoms in coeliacs. Between 2 and 10% of gluten sensitive individuals are also sensitive to oats, but it is not clear how much of this is due to contamination of triticeae seeds in oats or allergic responses (versus intolerance). Therefore, when broadly applied the designation of gluten-free applies to foods bearing the seed storage proteins derived from Triticeae.

Wheat gluten has been documented in China since the 6th century. It was widely consumed by the Chinese as a substitute for meat, especially among adherents of Buddhism. The oldest reference to wheat gluten appears in the "Qimin Yaoshu", a Chinese agricultural encyclopedia written by Jia Sixie in 535. The encyclopedia mentions noodles prepared from wheat gluten called "bo duo". Wheat gluten was known as "mian jin" by the Song dynasty (960–1279). Wheat gluten arrived in the West by the 18th century. "De Frumento", an Italian treatise on wheat from 1745, describes the process of washing wheat flour dough in order to extract the gluten. John Imison wrote an English-language definition of wheat gluten in his "Elements of Science and Art" published in 1803. By the 1830s, Western doctors were recommending wheat gluten in diets for diabetics. In the United States, the Seventh-day Adventists promoted the consumption of wheat gluten beginning in the late 19th century. Sanitarium Foods, a company affiliated with John Harvey Kellogg's Battle Creek Sanitarium, advertised wheat gluten in 1882.

Wheat gluten (food)

Wheat gluten is a food made from gluten, the main protein of wheat. It is made by washing wheat flour dough with water until all the starch granules have been removed, leaving the sticky insoluble gluten as an elastic mass which is then cooked before being eaten.

Wheat gluten is an alternative to soybean-based foods such as tofu, which are sometimes used as meat substitutes. Some types of wheat gluten have a chewy or stringy texture that resembles meat more than other substitutes. Wheat gluten is often used instead of meat in Asian, vegetarian, Buddhist, and macrobiotic cuisines. Mock duck is a common use for wheat gluten.

Wheat gluten proteins are deficient in lysine, which is an essential amino acid.

Wheat gluten first appeared during the 6th century as an ingredient for Chinese noodles. It has historically been popular in the cuisines of China, Japan and other East and Southeast Asian nations. In Asia, it is commonly found on the menus of restaurants catering primarily to Buddhist customers who do not eat meat.

The word seitan is of Japanese origin and was coined in 1961 by George Ohsawa, a Japanese advocate of the macrobiotic diet, to refer to a wheat gluten product created by Ohsawa's student Kiyoshi Mokutani. In 1962, wheat gluten was sold as seitan in Japan by Marushima Shoyu K.K. It was imported to the West in 1969 by the American company Erewhon.

Wheat gluten is also called seitan (, ; Japanese: セイタン), mianjin (Chinese: 麵筋), milgogi(Korean: 밀고기), wheat meat, gluten meat, or simply gluten.

Wheat gluten, called "miàn jīn" in Chinese (traditional:, simplified:, literally "dough tendon"; also spelled "mien chin" or "mien ching") is believed to have originated in ancient China, as a meat substitute for adherents of Buddhism, particularly some Mahayana Buddhist monks, who are strict vegetarians (see Buddhist cuisine). One story attributes the invention of imitation meat to chefs who made it for Chinese emperors who, traditionally, observed a week of vegetarianism each year. "Miàn jīn" is often deep fried before being cooked in Chinese cuisine, which confers a crispy rind that enhances the texture of the gluten. There are three primary Chinese forms of wheat gluten.

Oil-fried gluten (, "yóu miàn jīn") is raw gluten that has been torn into small bits, then deep-fried into small puffy balls of around 3–5 cm in diameter and sold as "imitation abalone". They are golden brown in color, and braised or boiled in a savory soup or stew before eating. They are frequently paired with "xiang gu" (black mushrooms). Larger fried balls of gluten, called "miàn jīn qiú" () or "miàn jīn pao" (面筋泡), which may be up to in diameter, are sometimes seen in Asian supermarkets. These are often stuffed with meat or tofu mixtures and served as a dish called "gluten meatballs" (, "Miàn jīn roù wán") or "gluten stuffed with meat" (, "miàn jīn saī roù").

Steamed gluten (, "zhēng miàn jīn"), is raw gluten that has been wrapped around itself to form a long sausage shape which is then steamed. This type of gluten has a dense texture and ranges from off-white to light greenish grey in color. It is torn open into strips before being used as an ingredient in recipes. When this sausage-shaped gluten is thickly sliced into medallions, the resulting form is called "miàn lún" (麵輪, literally "gluten wheels"). Larger blocks of steamed gluten are sometimes colored pink and sold as vegetarian "mock ham."Baked spongy gluten (traditional ; simplified ; pinyin: "kǎo fū") is similar in texture to a sponge, "kao fu" (sometimes labeled in English as "bran puff") is made by leavening raw gluten, then baking or steaming it. These are sold as small blocks in Chinese markets and are then diced up and cooked. This type of gluten absorbs its cooking liquid like a sponge and is enjoyed for its "juicy" character. Chinese "kao fu" has a different texture than its Japanese counterpart, "yaki-fu", due to the relatively larger air bubbles it contains. "Kao fu" is available in fresh, frozen, dehydrated, and canned forms.

"Miàn jīn" is also available in Asian grocery stores in canned and jarred forms, often marinated in combination with peanuts or mushrooms. Such canned and jarred gluten is commonly eaten as an accompaniment to congee (boiled rice porridge) as part of a traditional Chinese breakfast.

Freshly prepared "miàn jīn" can be difficult to find in Chinese restaurants other than those specializing in Buddhist or vegetarian cuisine. Depending on its method of preparation and ingredients used, both fresh and preserved "miàn jīn" can be used to simulate pork, poultry, beef, or even seafood.

In Japanese cuisine, the traditional type of wheat gluten is called "fu" ((), lit. "gluten"), originated from Jiangnan dialect for "". In Japan, the two main types of "fu" are most widely used in Buddhist vegetarian cooking ("Shojin ryori") and tea ceremony cuisine ("cha-kaiseki 茶懐石")(). There are two main forms of "fu", the raw "nama-fu", and dry-baked "yaki-fu".

Raw ("nama-fu" ) is solid gluten which is mixed with glutinous rice flour and millet and steamed in large blocks. It may be shaped and colored in a variety of ways, using ingredients such as mugwort. Popular shapes include autumn-colored maple leaves, bunnies, and other generally "various" forms. Such shapes and colors enhance the attractiveness of the cooked product since steamed gluten has an unappealing grey tone. "Nama-fu" is an important ingredient in Shōjin-ryōri, the Buddhist vegetarian cuisine of Japan. It may also be used as an ingredient in wagashi, Japanese confectionery. Fu-manjū () is a type of manjū made from "nama-fu". Solid gluten is sweetened and filled with various sweet fillings such as red bean paste. They are then wrapped in leaves and steamed in a manner similar to that used to prepare Chinese zongzi.

Dry baked ("yaki-fu" or "sukiyaki-fu" ) is gluten leavened with baking powder and baked into long bread-like sticks. It is often sold in cut form, as hard dry discs resembling croutons or bread rusk. Yaki-fu is typically added to miso soup and sukiyaki, where it absorbs some of the broth and acquires a fine texture that is lighter and fluffier than its Chinese equivalent. It is the most commonly available type of "fu" in Japanese supermarkets.

In Japan, seitan, initially a rather salty macrobiotic seasoning that gradually evolved into a food, is not well known or widely available, despite the macrobiotic diet's Japanese origins. When used, the terms for this food are rendered in katakana as (Romanized "gurutenmīto," from the English "gluten meat"), or, rarely, ("seitan"). Outside macrobiotic circles, these terms are virtually unknown in Japan, and they do not typically appear in Japanese dictionaries.

In Vietnam, wheat gluten is called "mì căng" or "mì căn", and is prepared in a similar fashion to Chinese "miàn jīn". Along with tofu, it is a part of the Buddhist cuisine of Vietnam.

"Seitan", a neologism of Japanese origin, is a food made from wheat gluten in the macrobiotic system of cooking and health, as formulated by the Japanese-born philosopher George Ohsawa (1893–1966). According to the "Oxford English Dictionary", it is said to have been coined by Ohsawa in the early 1960s, but its etymology is uncertain. The first syllable may be from 生 (sei, "be, become"), 正 (sei, "proper, correct"), or 製 (sei, "made of"), while the second syllable is from 蛋 (tan, from 蛋白 (tanpaku, "protein")).

The meaning of the word "seitan" has undergone a gradual evolution. The initial product, imported from Japan in 1969 was a very salty seasoning, the color of soy sauce, sold in a small glass jar or plastic pouch, to be used as a seasoning for brown rice. The name gradually came to refer to any wheat gluten seasoned with soy sauce. The people most responsible for this change are Nik and Joanne Amartseff, who invented Tan Pups in 1972 and John Weissman, who in 1974 invented Wheatmeat (first meatballs then cutlets made of seitan) in Boston. All worked for years to popularize these pioneering products at the Erewhon retail store, and developed a trademark on the Wheatmeat name.

While wheat gluten itself is rather flavorless, it holds a marinade very well and is usually simmered in a "dashi" (broth) made from soy sauce, kombu, ginger, and sometimes also sesame oil.

Since the mid-20th century, wheat gluten (usually called seitan) has been increasingly adopted by vegetarians in Western nations as a meat alternative. It is sold in block, strip and shaped forms in North America, where it can be found in some supermarkets, Asian food markets, health food stores and cooperatives.

The block form of seitan is often flavored with shiitake or portobello mushrooms, fresh coriander or onion, or barbecue sauce, or packed in a vegetable-based broth. In strip form, it can be packed to be eaten right out of the package as a high-protein snack. Shaped seitan products, in the form of "ribs" and patties, are frequently flavored with barbecue, teriyaki, or other savory sauces.

Wheat gluten is also used in many vegetarian products in various countries, for example by The African Hebrew Israelites of Jerusalem, a vegan African American religious sect that operates a chain of restaurants, to produce vegetarian sandwiches. In North America, there are several brand-name meat alternatives, which are used in the restaurant and food service markets.

A powdered form of wheat gluten is produced and sold as an additive for baking or used to make seitan. Vital wheat gluten is nearly all gluten and almost no starch. When used as an additive in baking, its purpose is to add elasticity to flours that would otherwise be low in gluten, such as whole wheat flour or rye. It improves the rise of the raw dough and also improves the texture and chewiness of the final product. Very little is required, generally about 1 Tablespoon (15ml) per 2-3 cups (480-620 ml) of flour.

The powdered form of wheat gluten (vital wheat gluten), is made by hydrating hard wheat flour to activate the gluten and then processing the hydrated mass to remove the starch, leaving only the gluten. The gluten is then dried and ground back into a powder.

Seitan may be made from vital wheat gluten or from hard wheat flour (a.k.a. high-protein flour, high-gluten flour, or gluten flour). When seitan is made from vital wheat gluten, the powder is simply rehydrated to form the gluten and then cooked. Seitan produced from wheat flour is a longer process. First a dough is made by hydrating the flour, then the dough is kneaded under running water to remove the starch from the dough, leaving only the gluten. The gluten is then cut into pieces and cooked via steaming, boiling, frying, or other methods.

Wheat gluten is used both as a protein source and binding ingredient in pet foods. Wheat gluten from China adulterated by melamine was blamed as the cause of the 2007 pet food recalls.