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
Anti-gliadin antibodies in food products. Some of these antibodies can recognize only wheat prolamins or very closely related grass seeds; others can detect antigens over broad taxa. The G12 antibody is the newest example which detects the most immunotoxic fragment, a 33-mer peptide from �-2 gliadin; available from Romer Laboratories and the Spanish company Biomedal. It recognizes the toxic fraction of wheat, barley, rye and also of oat. The R5 sandwich assay is another such assay. This assay can recognize wheat, barley and rye, which makes it ideal for evaluating the presence of contaminants in gluten-free foods that do not contain oat.