NEW METHODS FOR DETOXIFYING OF TOXIC GLUTEN PEPTIDES AND DETERMINATION OF GLUTEN TOXICITY

摘要

Celiac disease (CD), which is a gastrointestinal disorder, is an auto-immune intolerance against prolamine proteins, like gliadin, hordein, secalin and avenin, of wheat, barley, rye and in some varieties of oats, respectively. Prolamins of wheat, barley and rye, which are toxic to celiac patients, are generally recognised as ‘gluten’ terminologically. Toxic gluten peptides, which are formed through partial hydrolysis of prolamin proteins, cause characteristic inflammation and villous atrophy in upper small intestine of celiac patients. Gluten-free diet is the only safety treatment for celiac patients. Codex Alimentarius Commission (CAC) determined that the threshold values of gluten content in gluten-free foods and foods containing low levels of gluten are <20 mg/kg and <100 mg/kg, respectively. For the production of gluten-free products, the novel gluten detoxifying methods have recently been investigated. These are alternative methods, such as enzymatic approaches like using gluten-specific peptidases obtained from fungi or bacteria, sourdough practices, autolysis of gluten with activated gluten-spesific peptidases during germination of cereals, using microbial transglutaminase fulfilling transamidation reactions. Immunologic technics play an important role in the quantification of gluten. The official standart method issued by CAC is the competitive ELISA method using R5 antibody.