Triticeae glutens

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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 seed proteins fall into four groups:^[1]

• albumins – soluble in hypotonic solutions and are coagulated by heat
• globulins – soluble on 'isotonic' solutions
• prolamins – soluble in aqueous alcohol
• glutelins – are soluble in dilute acids or bases, detergents, chaotropic or reducing agents.

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.