Gliadin Deamidated gliadin is produced by acid or enzymatic treatment of gluten. The enzyme tissue transglutaminase converts some of the abundant glutamines to glutamic acid. This is done because gliadins are soluble in alcohol and cannot be mixed with other foods (like milk) without changing the foods' qualities. Deamidated gliadin is soluble in water. The cellular immunity to deamidated α-/β-gliadin is much greater than α/β-gliadin and can result in symptomatic gluten-sensitive enteropathy. Celiac disease is a chronic, immune-mediated intestinal disorder, in which the body becomes intolerant to gliadin, which is a component of gluten. Individuals with celiac disease exhibit a lifelong
Prolamin disease in genetically predisposed individuals. Prolamin Prolamins are a group of plant storage proteins having a high proline content and found on plant materials mainly like in the seeds of cereal grains: wheat (gliadin), barley (hordein), rye (secalin), corn (zein), sorghum (kafirin) and as a minor protein, avenin in oats. They are characterised by a high glutamine and proline content and are generally soluble only in strong alcohol [70-80%] solutions, light acids, and alkaline solution. They do not coagulate in heat. They hydrolyse into prolin and ammonia. Some prolamins, notably gliadin, and similar proteins found in the tribe Triticeae (see