Skip to main content Skip to Search Box

Definition: gluten from The Hutchinson Unabridged Encyclopedia with Atlas and Weather Guide

Protein found in cereal grains, especially wheat and rye. Gluten enables dough to expand during rising. Sensitivity to gliadin, a type of gluten, gives rise to coeliac disease.

Summary Article: Gluten and Modified Gluten from Encyclopedia of Food Grains

Gluten is the proteinaceous material remaining after removal of starch from cereal flour or meal. In particular, it most commonly refers to the protein isolated from wheat. Wheat gluten is the main cause of the symptoms of celiac disease, although structurally similar proteins from barley, rye, triticale, and oats may also have this effect in some individuals. Vital gluten is produced commercially as the by-product of the production of starch from wheat. There are a number of different processes to achieve this, all of which take advantage of the insoluble, viscoelastic, and cohesive properties of gluten. The output of this commercial production is used for a number of purposes, ranging from flour fortification for baking and other wheat-based products to a growing use in artificial meat and fish products. There is also a growing market for modified glutens for use in items that often would not normally contain gluten itself. In developing economies, increasing affluence is creating a demand for foods where the addition of gluten will result in a higher or more consistent quality in traditional foods. An increasing taste for Western-style foods also provides the demand for gluten for addition to lower-protein flours.


Flour fortification, Gliadin, Glutenin, Protein denaturation, Protein polymerization, Protein separation, Protein solubilization, Wheat protein

Topic Highlights

  • Gluten is the storage protein component of wheat.

  • The commercial production of gluten is a by-product of the wheat starch industry.

  • It is gluten that gives wheat flour its unique properties for bread-making.

  • Gluten may be added to low-quality flours to allow the manufacture of higher-quality products.

  • Gluten may also be added to foods and feeds as a source of protein.

  • The nutritional value of gluten is reduced because of low amounts of some essential amino acids.

  • Demand for Western-style foods or improved quality of traditional foods is driving an increasing use of gluten in developing economies.

Learning Objective

  • To achieve an understanding of the nature of gluten and how its properties are useful for improving quality in foods.

What Is Gluten?

A nontechnical definition of gluten describes it as ‘the sticky, viscous residue after removal of starch from flour.’ This definition would include corn gluten, the protein residue from isolation of starch from corn. However, this material is quite different to wheat gluten, the residue from production of wheat starch from flour. In the technical sense, the term ‘gluten’ usually refers to wheat gluten. However, there are many people with food intolerance to cereals, and for them, ‘gluten’ includes the equivalent proteins from rye, triticale, barley, and possibly oats. The most commonly recognized intolerance to gluten is celiac disease. There is also a syndrome known as ‘nonceliac gluten sensitivity’ although there is evidence that this condition, in some people at least, is not caused by gluten but by a group of sugars known as ‘fermentable oligosaccharides, disaccharides, monosaccharides, and polyols.’ People with gluten intolerance need to consume a diet that excludes ‘gluten’ from any of the cereals listed earlier. The term ‘gluten-free food’ refers to a food product free from these cereal proteins or whose cereal protein content is less than a defined amount, usually <200 ppm for a cereal-based food and <20 ppm for a food not naturally containing gluten.

For the purposes of this article, only the properties and uses of wheat gluten will be discussed. Gluten may thus be defined technically as the “cohesive, viscoelastic, proteinaceous material prepared as a by-product of the isolation of starch from wheat flour” (Figure 1). A more theoretical definition may define it as the “storage proteins of the wheat grain.” Both definitions are correct but neither tells the whole story, and for the purposes of this article, gluten is the commodity isolated on a commercial scale and sold for a variety of purposes in many countries of the world. In particular, ‘vital wheat gluten,’ the dry form of the product in which the functional properties may be regenerated by rehydration, will be mainly considered.

Figure 1 Gluten prepared from wheat flour, showing its cohesive and viscoelastic nature.

Courtesy of Colin Wrigley.

Composition of Gluten

Although sold as a protein, gluten contains more than just protein. The commodity usually contains ~ 75% protein, 8% moisture, and varying amounts of starch, lipid, and fiber. The starch and fiber become entrapped in the cohesive matrix of the protein and become more difficult to remove as the protein content increases. The amount of starch varies, and more extensive washing can reduce the starch and fiber content and increase the protein content. The extra water needed for this creates its own problems by producing a larger amount of effluent from the process and increasing the biological oxygen demand of that effluent (see in the succeeding text). Consequently, gluten of higher protein content is only produced as a special order and at a premium price. The lipid content is unaffected by additional washing. Most of the lipid content of the flour becomes associated with the protein during the washing process. The proteins are hydrophobic and the lipids bind to the hydrophobic areas of the protein as they are repelled by the water used in the washing. Lipids bind strongly to gluten and are removed with much more difficulty than from the original flour. The lipid content of gluten is primarily determined by the lipid content of the flour from which it came and is unaffected by additional washing. The final lipid content of gluten may be decreased by using a solution of certain salts (e.g., sodium, potassium, or ammonium chlorides), but the presence of these salts in the effluent may also create environmental problems.

The protein that makes up gluten is actually a complex mixture, containing many, perhaps several hundred, polypeptide species. A typical amino acid analysis of the complex mixture is shown in Table 1. The individual proteins are divided into two main classes – monomeric and polymeric. These terms can be confusing in that any protein is a polymer of amino acids. In gluten, monomeric refers to individual, discrete polypeptide species, whereas polymeric refers to chains formed from individual monomeric proteins by cross-linking them with disulfide bonds of cystine residues in adjoining chains. The monomeric proteins are often called gliadin and the polymeric ones are called glutenin. It should be noted that some of the glutenin subunits do exist in gluten in the monomeric form.

Table 1 Amino acid composition of commercial vital wheat gluten

Amino acid


a Values expressed as g amino acid/100 g protein.

b Glutamic acid and aspartic acid are predominantly in the amidate form, with ~ 90% existing as glutamine and asparagine, respectively.





Aspartic acidb




Glutamic acidb


























How Is Gluten Made?

Gluten was first prepared from flour almost 300 years ago by an Italian named Beccari, who conducted a simple water-washing experiment with wheat flour. This discovery, which can be easily reproduced in the home kitchen, has become the basis of a major cereal industry, utilizing millions of tonnes of wheat annually in North America, Europe, and Australia (Figure 2). The commercial process is basically an efficient repetition of Beccari's experiment. Most commercial operations use variations of either the ‘batter process’ or the ‘Martin process.’

Figure 2 Gluten prepared in a commercial process.

Originally, gluten was produced as a by-product of the wheat starch industry. There is a high demand for starch for both food and nonfood uses, and in those areas where wheat was the major crop, it became the main raw material in the preparation of the starch required for various industrial purposes. Gluten became an embarrassing by-product. In some cases, its disposal was in municipal sewers and drains, but this soon became an undesirable practice. It was also dried in a variety of ways to yield a protein-rich material used in animal feeds, and wet gluten was also used to fortify bread and other baked products made from flour. The shelf life of wet gluten, usually only a few hours, severely restricted its use in this form. It was not until the application of ring drying that a dry vital gluten product could be prepared in significant amounts, allowing its trade as a valuable commodity.

Martin Process

In this method, a wheat flour dough is washed with water while it passes through a tumbling cylindrical agitator. The work applied to the dough is not dissimilar to the effect of kneading a dough under water in that starch comes out of the dough and the protein content increases. The tumbling action moves the dough along the cylinder and the starch passes through small holes in the wall, while the protein remains inside, receiving further washing until it tumbles out at the end.

Batter Process

In this process, a thick suspension or batter of flour is stirred slowly in a tank for several hours, during which time the starch separates from the protein. The mixture is then passed through a fine sieve, which allows the starch granules to pass through but retains the curds of gluten on the screen. This gluten is then washed with water to remove further starch in a similar manner to the Martin process and then dried.

The Martin process is a continuous process, while the nature of the batter process makes it more suited to batch operation.

Other Processes

Most commercial operators use one or other of the previous methods with modifications, but there have been many other processes suggested for production of gluten. While mosthave not made it past the laboratory curiosity stage, others, for example, the Alfa-Laval/Raisio process, have been applied in full-scale production facilities. The basis of these other processes varies, and some use centrifugal techniques, which may involve either conventional industrial centrifuges or hydrocyclones to separate the starch from the protein. Many operators use hydrocyclones as the principal way of cleaning the starch and, in some cases, in the actual separation of the starch and gluten.

Many of the newer methods utilize whole grain as the raw material, avoiding the production of flour in a dry-milling step. This allows a more complete isolation of the starch fraction from the wheat, but cleaning the protein and starch of residual bran is a major disadvantage of these types of methods. Improved milling processes have reduced the amount of endosperm remaining in the bran and offal fractions in conventional milling, so there is little advantage to be gained in wet milling for starch and gluten recovery. There is also the need to dry the bran unless it can be processed on the spot or at least locally, and this cost will usually exceed the economic benefit of improved starch yield. Thus, despite these newer methods, modifications of the traditional processes have remained the preferred choice for almost all the gluten produced worldwide.

Dry Gluten

Gluten is very susceptible to heat when wet, and relatively low temperatures destroy the cohesive, viscoelastic properties (‘vitality’), which make it unique among food proteins. Attempts to dry gluten while retaining these properties were unsuccessful until the application of the ring drier to gluten in the firsthalf of the twentieth century. This drying process has since been the basis of gluten production. Prior to this, vital gluten was only available in a wet form and could only be used in this form for a short time after production. The principle of the ring drier is that simple wet gluten with a moisture content of ~ 70% is mixed with sufficient dry, vital gluten to reduce the moisture to ~ 20%. This lowered-moisture material is comminuted and subjected to flash drying in a ring drier. A portion of the dried gluten is removed and packaged, while the rest is returned to the drying cycle to reduce the moisture content of more wet gluten. The procedure is still very sensitive to excessive heat, but with careful control of the temperature, a vital wheat gluten is produced.

An alternative way of drying to prepare a vital gluten is to disperse the gluten in aqueous ammonia or acetic acid and then spray-dry this dispersion. The resulting product retains the viscoelastic properties of gluten, and it may be used for most of the same purposes as normal vital gluten. The cost of this drying procedure, together with environmental concerns from the emission of ammonia or acetic acid vapors, limits its application except for special reasons. Another dry gluten product is known as ‘devital gluten.’ This material has lost its cohesive, viscoelastic properties but retains the insolubility and water-binding capacity of vital gluten. It is commonly used where the cohesiveness of vital gluten can actually be a disadvantage.

Waste Products from Manufacture of Gluten

The amount of water required for each tonne of flour varies according to the operator. All processes have a significant waste stream that consists of the wash water plus soluble protein, damaged starch, and sugars plus some fiber. Disposal procedures for this waste vary, depending on the manufacturer, and methods include fermentation to produce ethanol or methane, isolation by drying for use in animal feed, and discharge into the sewerage system. The last option is becoming less common as environmental concerns grow worldwide.

Properties of Gluten

The most important properties of gluten are its solubility (or rather its lack of solubility) and its rheological functionality. By the nature of its preparation, gluten is a protein that is insoluble in water. While there are small amounts of water-soluble proteins trapped in the gluten matrix, these are essentially not extractable into water under normal conditions. Despite its insolubility and its hydrophobic nature, gluten absorbs an amount of water approximately twice its dry weight to form a hydrated gluten. This material is effectively the same as the wet gluten first isolated from flour. In the case of commercially prepared gluten, drying conditions may cause some deterioration of the functional properties, but gluten prepared in the laboratory shows no change in its properties after freeze-drying and rehydration.

The principal components, gliadin and glutenin, are both insoluble in water. Gliadin can be solubilized in 70% ethanol, one of the steps of the Osborne fractionation of wheat proteins, and the residue after this extraction is considered to be glutenin. Isolation of the dissolved material, however, yields a protein, which has lost most of its functional properties. Both gliadin and glutenin may be solubilized to a certain degree by the use of acidic conditions. By careful control of the pH, gluten may be separated into a number of fractions. Reprecipitation by pH adjustment, or by drying the acidic solution directly, gives products that maintain their functional properties. This can be shown by reconstituting flour through recombining the starch, the isolated protein fractions, and the water-soluble components prepared during the extraction of gluten. Doughs prepared by careful reconstitution show little change in dough strength compared to that of the original flours.

The rheological properties of gluten are the basis of its functional uses. It is these properties that give wheat flour doughs the characteristics that allow the production of breads, cakes, biscuits, and noodles. Thus, gluten can be considered to be like a dough in which the diluting effect of starch is no longer present. In the wet state, the protein molecules form a cohesive matrix, which, in dough, also holds the starch granules within it. This matrix is also elastic, allowing it to stretch and expand. In aerated doughs, this elasticity permits the expansion of gas bubbles, which produce the texture of bread and cakes. If the gluten matrix is too weak, or the protein content is too low to form an effective matrix, the bubbles expand beyond the elastic limit and burst, reducing the overall volume of a baked product.

How Is Gluten Used?

The uses of gluten worldwide vary from country to country, but the most common usage in Western countries is addition to flour in baked goods of various types (Table 2). The second largest use is in pet foods. Here, gluten is added as a protein source to improve the nutritional quality of the pet food. Its hydration and lipid-binding properties also assist in improving the overall properties of the product. A growing market for gluten is as an ingredient in aquaculture feed, where its cohesive properties hold the feed together when it is put into water.

Table 2 Usage of gluten in different regions (as percentage of total usage for region)

N. America (%)

EU (%)

Australia (%)

Japan (%)

China (%)

a Includes gluten used for synthetic fish products.






Flour fortification




Pet food








Breakfast cereals












Foods (in general)










Gluten is used in other countries in a variety of ways. Perhaps the major use is as a meat replacement in vegetarian foods and in the production of artificial forms of expensive foods such as crab meat. It is also used in the preparation of soy sauce extenders and the manufacture of monosodium glutamate. The high glutamine content of gluten makes it an ideal starting material for this latter product.

There are developing markets for gluten in countries with rapidly growing economies. The increasing affluence has created a demand for Western-style foods, many of which are based on wheat and for which the properties of gluten are essential. In addition, gluten may be used for flour fortification in traditional food, allowing the use of lower-quality flours or improving the quality of the product.

China has emerged as one of the three most important economies in the world. Significant changes have taken place in consumption patterns and market trends following economic reform and opening its markets to the world. Wide varieties of ethnic, frozen, bread, bun, and bakery food products are in the marketplace today. The use of frozen dough has been of great interest since the 1960s; ithas now appeared in traditional steamed bread chain stores as well as in bakery chain stores in China's markets, indicating a trend in the dough products industry. Gluten is often used at 1–2% level for increased dough strength, cryoprotective property, and steaming or baking performance. The use of gluten in combination with so-called bioingredients such as enzymes can also reduce the use of chemical oxidants in dough to satisfy consumers’ food safety and health concerns. In addition to modern bakery products and traditional steamed bread products, gluten is used in other food products such as noodles, extruded snacks, sausages, fried gluten balls, and fish meat balls. There are about 30 gluten manufacturers operating in China. Ithas been estimated that 76% of all gluten used in China goes to foods, while 19% goes to feeds, including pet foods and aquaculture feed. Nonfood uses represented ~ 5% in China (Table 2).

India is another major wheat-producing country where increased affluence has created a demand for wheat-based foods with improved quality. There is already one gluten producer operating in India and there is a growing demand for vital wheat gluten for incorporation into foods. It is added to a variety of wheat-based products, including traditional ones such as chapattis.

Baked Goods

Wheat-based products, in which gluten is used to fortify flours of lower-than-desirable protein content, have been and continue to be the main application of gluten. There is a concern about the effects of gluten on people with celiac disease and others with wheat protein allergies, but its incorporation into foods that already contain gluten cannot be questioned. Increasing the protein content of a flour by adding vital gluten improves the quality of the flour to be equivalent to one with the higher protein content. This fortification may be necessary because the flour has a naturally low protein and a higher protein content is needed to make quality products or because the addition of gluten provides a particular property sought in the food by improving the quality of the protein. Addition of gluten to a flour of low protein content improves the texture and shelf life of bread prepared from it, but it is useful in other applications as well. For example, addition of ~ 1% gluten to flour reduces pretzel breakage in the finished product, but the addition of too much gluten may result in pretzels that are too hard to eat. Addition of gluten to pasta-type products will also reduce breakage. However, the desire of consumers for pasta of 100% durum wheat origin means that fortification with gluten for this purpose is more limited.

Other Uses

In addition to its use in pet foods, gluten is commonly added as a binder in meat products for human consumption. Here, the desired property is its ability to bind fat and water while at the same time increasing the protein content. Gluten and modified glutens have also been used in calf-milk replacements.

A number of nonfood uses have also been suggested for gluten. These include adhesives, paper coating, detergent formulations, slow-release pharmaceuticals, medical bandages, construction materials, and binding of heavy metals in industrial processes. The use of gluten in films has also been tried. Gluten-based films may be cast from solutions of gluten in ammonia. Production of gluten films with satisfactory properties could provide a new biodegradable film for widespread use.

Modifying Gluten

Gluten is a protein, intermediate in price between low-value commodities suitable only as animal feed without further processing and high-value materials such as casein and soy isolates. This gives significant scope for modification of its properties for value addition. Various threatened surpluses in the market for gluten have turned the attention of manufacturers to ways of converting gluten into products with vastly different properties.

Chemical Modification

The main modification applied to gluten is solubilization. Gluten becomes soluble in a variety of chemicals including urea solutions, lactic acid, soaps and detergents with or without urea, acetic acid, hydrochloric acid, sodium hydroxide, 70% ethanol, and 2-chloroethanol to name just some. Many of these are incompatible with food products, but for nonfood purposes, there are few limitations other than cost, safety, and environmental concerns.

Solubilization by deamidation is the major method applied. This may be achieved with either acid or alkali. Approximately 90% of the glutamic acid in gluten is in the form of glutamine (Figure 3). Removal of the amide group of these residues to form the corresponding carboxylic acid changes the potential ionic charge on the protein, thus increasing its solubility above a certain pH. In acidic deamidation, there is also a degree of peptide hydrolysis to form lower-molecular-weight polypeptides, which are usually more soluble than larger ones. In alkali solutions, peptide hydrolysis does not occur as readily as in acid. However, there is the possibility of alkaline attack on the disulfide bonds of cystine, with the subsequent opportunity of creating cross-links due to the formation of lysinoalanine (Figure 3). The use of temperatures close to ambienthas shown no formation of lysinoalanine. The reaction mixtures of acid or alkali deamidation require neutralization before the products can be used for their final purpose, a step that produces significant amounts of salts, which usually need to be removed. This can be done by isoelectric precipitation, that is, adjustment of the pH to the isoelectric point at which proteins are least soluble as they have no net charge. A procedure that uses acidic or basic proteins to neutralize the alkali or acid, respectively, has been reported. No inorganic salt is formed in this process, but the overall proportion of gluten in the final product is very much reduced. Deamidated gluten is easily dispersible, which makes it suitable for use in foods for emulsification or foam stabilization. Ithas been used in meat products, nondairy coffee whiteners, beverages, and milk puddings. No benefits have been reported for the use of deamidated gluten in bread doughs.

Figure 3 Structures of glutamine, glutamic acid, and lysinoalanine.

Gluten may be treated with sulfuric acid, phosphoric acid, or chlorosulfonic acid to prepare products, which bind greatly increased amounts of water. There have been reports that some of these products bind an amount of water equivalent to up to 200 times their own weight. Other chemical modifications include acylation with carboxylic acid anhydrides. In particular, treatment of gluten with succinic anhydride increases its solubility at pH 7 (close to the point of minimum solubility of native gluten) but decreases its solubility at pH 3 where it is normally quite soluble.

Enzymic Modification

Hydrolysis of the peptide bonds by enzymes also increases the solubility of gluten. This is achieved by reducing the molecular weight of the polypeptide chains. A number of commercially available enzymes have been used for this purpose, including papain, bromelain, subtilisin, trypsin, and pronase. The enzyme-solubilized gluten has many of the properties of chemically deamidated gluten, such as foam stability and emulsion formation. Unlike deamidated gluten, enzyme-solubilized gluten does have beneficial effects on dough properties. Addition at levels of 1–2% reduced dough mixing times by amounts similar to those achieved by chemicals, such as cysteine and ascorbic acid, which are often added commercially to give improved loaf volumes. Many of the reports of enzyme-solubilized gluten refer to ithaving a bitter taste. This is believed to arise from the formation of small peptides thathave been identified with bitter flavors in other proteins. Thus, treatment with enzymes needs to be carefully controlled to minimize the formation of these small peptides.

There is a potential for modified glutens to be used in products, which traditionally do not contain wheat or other cereals. This has raised concerns about whether the toxicity of gluten for people with a gluten sensitivity will have been removed. At this point in time, there is insufficient evidence to categorically say whether or not these foods would be safe for people with gluten sensitivity.

The Future for Gluten

Production of gluten is still driven by the need for starch. Thus, it will always be produced, while wheat is a major source of starch. There is the risk that demand for starch will grow faster than the demand for gluten, but to date, this has nothappened despite dire predictions on many occasions. Although its absolute price has not changed significantly over many years, by becoming relatively cheaper than alternative food proteins, gluten has found its way into more applications for which it was formerly too expensive. This has served to maintain its value, while outputhas greatly increased. The demand generated by increased affluence in developing countries will also help to maintain its price and will probably result in higher prices in the longer term.

Consumer concerns about gluten-free foods may limit its application in some areas, but the ubiquity of wheat in many foods ensures that gluten will remain an acceptable additive. The greatest threat to the gluten industry has been and will remain the lower cost of preparing starch from sources other than wheat. Gluten has played a major role in keeping the production of wheat starch economically viable in face of cheaper starch from other sources. This situation is expected to be unchanged in the future.

Exercises for Revision

  • What are the principal protein components of gluten and how do they differ from one another?

  • Which amino acid is predominant in gluten and in what form is it present? What is the second most common amino acid in gluten?

  • Why is gluten added to flour to improve the quality of products?

  • Why is dry, vital gluten difficult to prepare and what technique is used to produce it?

  • What modifications may be applied to gluten to prepare a soluble product?

  • What are two factors driving increased gluten use?

  • What groups of proteins are the storage proteins of cereals?

  • What is protein denaturation and how does it affect the use of gluten in food products?

Exercises for Readers to Explore the Topic Further

  • What are the rheological properties that make gluten so useful, and how are they measured?

  • The quality of what traditional foods may benefit from the addition of gluten to low-protein flours?

  • For sufferers of celiac disease, what are the implications of using solubilized or other modified glutens in foods that normally do not contain wheat?

  • What are the nutritional limitations of gluten as a food protein? Are there any essential amino acids, which are present in greater abundance than would be required in a balanced protein? How could the nutritional limitations of gluten be overcome in a mixed protein food?

  • What bonds are responsible for the primary, secondary, and tertiary structures of proteins?

  • In what two ways is gluten a polymer?

  • What makes up the backbone structure of protein?

See also

Appendix 3: Grains, Foods, and Ingredients Suiting Gluten-Free Diets for Celiac Disease; Food Grains: Intolerance, Allergy and Diseases: Celiac Disease; The Gluten-Free Diet; Non-food Products from Grains: Cereal Grains as Animal Feed; Pet Foods; Proteins: The Protein Chemistry of Cereal Grains; Wheat-Based Foods: Breads; Wheat Processing: Cereal Food Production with Low Salt; The Gluten Proteins of the Wheat Grain in Relation to Flour Quality; Wet Milling of Wheat.

Further Reading

  • K. Khan; P.R. Shewry Wheat Chemistry and Technology 2009 American Association of Cereal Chemists International St. Paul MN 4th edn.
  • G.L. Lookhart; P.K.W. Ng Gluten Proteins 2006 2006 American Association of Cereal Chemists International St. Paul MN.
  • P.R. Shewry; G.L. Lookhart Wheat Gluten Protein Analysis 2003 American Association of Cereal Chemists International St. Paul MN.
  • P.R. Shewry; A.S. Tatham Wheat Gluten The Proceedings of the 7th International Workshop Gluten 2000 2000 Royal Society of Chemistry London.
  • C. Wrigley; F. Bekes; W. Bushuk Gliadin and Glutenin: The Unique Balance of Wheat Quality 2006 American Association of Cereal Chemists International St. Paul MN.
  • I.L. Batey
    Sunset Cereal Services, Meadowbank, NSW, Australia
    W. Huang
    Jiangnan University, Wuxi, Jiangsu, China
    Copyright © 2015 Elsevier Ltd. All rights reserved.

    Related Credo Articles

    Full text Article Gluten
    The Encyclopedia of Seeds: Science, Technology and Uses

    Gluten is a mixture of prolamin storage proteins present in the wheat grain, and also in those of rye, triticale, barley and oats. (See: ...

    Full text Article coeliac disease
    The Macmillan Encyclopedia

    A disease in which the small intestine is abnormally sensitive to gliadin (a component of the protein gluten , found in wheat). It results in...

    Full text Article Preface
    Clinical Guide to Gluten-Related Disorders

    Wheat, the most widely grown crop, is immensely diverse, with over 25,000 different cultivars having been produced by plant breeders worldwide. Much

    See more from Credo