Celiac-related properties of chemically and enzymatically modified gluten proteins.

The effects of chemical (acid-heating treatment) and enzymatic (microbial transglutaminase, TGase) modification (deamidation) of gluten proteins on their physicochemical and celiac disease-related properties were studied. Ammonia release, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and sample solubility analyses were employed to check the extent of gluten modification. Among different treatments achieved, the acid-heating treatment performed at 90 degrees C for 3 h induced gluten deamidation, paralleling an increase of gluten solubility without relevant proteolysis.