Gliadin in the context of "Coeliac disease"

Gluten is a structural protein complex naturally found in certain cereal grains. The term gluten usually refers to the elastic network of a wheat grain's proteins, gliadin and glutenin primarily, which forms readily with the addition of water and often kneading in the case of bread dough. The types of grains that contain gluten include all species of wheat (common wheat, durum, spelt, khorasan, emmer, and einkorn), and barley, rye, and some cultivars of oat; moreover, cross hybrids of any of these cereal grains also contain gluten, e.g. triticale. Gluten makes up 75–85% of the total protein in bread wheat.

Glutens, especially Triticeae glutens, have unique viscoelastic and adhesive properties, which give dough its elasticity, helping it rise and keep its shape and often leaving the final product with a chewy texture. These properties, and its relatively low cost, make gluten valuable to both food and non-food industries.

In cooking (and more specifically baking), kneading is a process in the making of bread or dough, used to mix the ingredients and add strength and stiffness to the final product. It shortens baking times by forming gluten structural protein complexes more quickly than without kneading.

Kneading's importance lies in the mixing of flour with water; when these two ingredients are combined and kneaded, the gliadin and glutenin proteins in the flour expand and form strands of gluten, which gives bread its texture. (To aid gluten production, many recipes use bread flour, which is higher in protein than all-purpose flour.) The kneading process warms and stretches these gluten strands, eventually creating a springy and elastic dough.

Glutenin (a type of glutelin) is a major protein within wheat flour, making up 47% of the total protein content. The glutenins are protein aggregates of high-molecular-mass (HMW) and low-molecular-mass (LMW) subunits with molar masses from about 200,000 to a few million, which are stabilized by intermolecular disulfide bonds, hydrophobic interactions and other forces. Glutenin is responsible for the strength and elasticity of dough.

Wheat gluten proteins consist of two major fractions: the gliadins and the glutenins. Gliadins are monomeric proteins, which can be separated into four groups: alpha-, beta-, gamma- and omega-gliadins. They are structurally similar to LMW glutenins. Glutenins occur as multimeric aggregates of high-molecular-mass and low-molecular-mass subunits held together by disulfide bonds. The way the glutenins form their disulfide bond network is predicted to be regulated by the hydrophobicity in the peptide sections where their cysteins are located, explaining why the gliadins are monomeric despite sharing similar conserved cysteine motifs as the LMW-glutenins.