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Wheat seed, sectioned to reveal endosperm and embryo

Gluten is a composite of the proteins gliadin and glutenin. These exist, conjoined with starch, in the endosperms of some grass-related grains, notably wheat, rye, and barley. Gliadin and glutenin comprise about 80% of the protein contained in wheat seed. Being insoluble in water, they can be purified by washing away the associated starch. Worldwide, gluten is an important source of nutritional protein, both in foods prepared directly from sources containing it, and as an additive to foods otherwise low in protein.

The seeds of most flowering plants have endosperms with stored protein to nourish embryonic plants during germination, but true gluten, with gliadin and glutenin, is limited to certain members of the grass family. The stored proteins of maize and rice are sometimes called glutens, but their proteins differ from wheat gluten by lacking gliadin. The glutenin in wheat flour gives kneaded dough its elasticity, allows leavening and contributes chewiness to baked products like bagels.

Although wheat supplies much of the world's dietary protein and food supply, as much as 0.5% to 1% of the population of the United Statesmarker has celiac disease, a condition which results from an adverse immune system response to gluten. The manifestations of celiac disease range from no symptoms to malabsorption of nutrients with involvement of multiple organ systems. The only effective treatment is a lifelong gluten-free diet.


While there is no evidence of this, legend attributes the discovery of gluten to Buddhist monks in 7th-century China who sought meat-like ingredients for use in their vegetarian diet. With easily available wheat flour and water they made a dough which they submerged in cold water and kneaded. The water dissolved the starchy components of the dough and left behind an insoluble, gummy mass, 70% to 80% of which was gluten.

Gluten is still extracted from flour by washing out the starch by means not fundamentally different from the ancient way; this exploited the fact that starch is water-soluble while gluten is not, and also that gluten binds together strongly, while starch dissolved in cold water is mobile. If a saline solution is used instead of water a purer protein is obtained, with certain harmless impurities going into solution with the starch. However, on an industrial scale, starch is the prime product, so cold water is the favored solvent. To effect the separation, a slurry of wheat flour is stirred vigorously by machinery until the starch dissolves and the gluten consolidates into a mass, which is collected by centrifugation, then carried, by complex machinery, through several stages combined into a continuous process: Approximately 65% of the water in the wet gluten is removed by means of a screw press, and the residue is sprayed through an atomizing nozzle into a drying chamber, where it remains at an elevated temperature only long enough to evaporate the water without denaturing the gluten. This yields a flour-like powder with a 7% moisture content, which is quickly air-cooled and pneumatically transported to a receiving vessel. In the final step, the collected gluten is sifted and milled to make the product uniform.


When dough made with wheat flour is kneaded, gluten forms when glutenin molecules cross-link to make a sub-microscopic network and associates with gliadin, which contributes viscosity and extensibility to the mix. If such dough is leavened with yeast, sugar fermentation produces bubbles of carbon dioxide which, trapped by the gluten network, cause the dough to swell or 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 by hydration.

The development of gluten (i.e., enhancing its elasticity) affects the texture of the baked goods. Gluten's attainable elasticity is proportional to its content of glutenins with low molecular weights because that fraction contains the preponderance of the sulfur atoms responsible for the cross-linking in the network.More development leads to chewier products like pizza and bagels, while less development yields tender baked goods. In general, bread flours are high in gluten while cake flours are low. Kneading promotes the formation of gluten strands and cross-links, so a baked product is chewier in proportion to how much the dough is worked. Increased wetness of the dough also enhances gluten development. Shortening inhibits formation of cross-links, so it is used, along with diminished water and minimal working, when a tender and flaky product, such as pie crust, is desired.

Gluten, dried and milled to powder and added to ordinary flour dough, improves rising and increases the bread's structural stability and chewiness,. Such doughs must be worked vigorously if they are to rise to their full capacity, so a bread machine or food processor may be required for their kneading. The added gluten provides supplemental protein to what would otherwise be high-carbohydrate preparations. The protein content of pet foods is also enhanced by adding gluten. When cooked in broth, gluten absorbs some of the surrounding liquid (including the taste) and becomes firm to the bite, so is widely used in vegetarian, vegan and Buddhist cuisines as a meat substitute. In China, as miàn jin, it is the basis for imitation meats resembling chicken, duck, fish, pork and beef. The Japanese variants, called namafu, yakifu, and seitan, are used in the same way.

Gluten as an additive

The "Codex Alimentarius" set of international standards for food labeling has a standard relating to the labelling of products as "gluten free", however this standard does not apply to "foods which in their normal form do not contain gluten". Gluten is used as a stabilizing agent in products like ice-cream and ketchup, where it may be unexpected. Foods of this kind present a problem because the hidden gluten constitutes a hazard for people with celiac disease: In the United States, at least, gluten may not be listed on the labels of such foods because the U.S, Food and Drug Administration has classified gluten as GRAS (Generally recognized as safe). Requirements for proper labeling are being formulated by the USDA. In the United Kingdommarker, only cereals currently need to be labelled, while other products are voluntary. In fact, in the UK most gluten free food is clearly labelled so, as is non-gluten-free food.

Adverse reactions

Between 0.5 and 1.0 percent of people in the United States are sensitive to gluten due to celiac disease. Celiac disease is caused by an abnormal immune reaction to partially digested gliadin. It probably occurs with comparable frequencies among all wheat-eating populations in the world. Certain allergies and neuropathies are also caused by gluten consumption and inhalation.

Note that wheat allergy and celiac disease are different disorders.

See also


  1. Sahlstrom, S. & Brathen, E. (1997). Effects of enzyme preparations for baking, mixing time and resting time on bread quality and bread staling. Food Chemistry, 58, 1, 75-80. Effects of wheat variety and processing conditions in experimental bread baking studied by univariate and multivariate analyses.
  2. Amendola, J., Rees, N., & Lundberg, D. E. (2002). Understanding Baking
  3. Echkardt, LW & Butts, DC. (1997). Rustic European Breads from your Bread Machine

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