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

Abstract

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. Changes in the immunoreactivity of celiac IgA anti-gliadin antibodies (AGAs) to modified gluten proteins were detected by using a competitive indirect enzyme-linked immunosorbent assay method. Chemical deamidation by acid-heating treatment of gluten lowered IgA-AGA immunoreactivity. IgA-AGA immunoreactivity to gliadins was increased when they were submitted to TGase-catalyzed deamidation. The acid-heating treatment of gluten reduced its cytotoxic activity on human colon adenocarcinoma LoVo cell line. These results showed that chemical deamidation of gluten may be envisaged as a way to lower the potential risk for celiac people due to widespread use of gluten as a food additive.

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@article{Berti2007CeliacrelatedPO, title={Celiac-related properties of chemically and enzymatically modified gluten proteins.}, author={Cristiana Berti and Leda Roncoroni and Maria Letizia Falini and Rosita Caramanico and Ersilia Dolfini and Maria Teresa Bardella and Luca Elli and Claudia Terrani and Fabio Forlani}, journal={Journal of agricultural and food chemistry}, year={2007}, volume={55 6}, pages={2482-8} }