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°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.
Celiac-related properties of chemically and enzymatically modified gluten proteins / C. Berti, L. Roncoroni, M.L. Falini, R. Caramanico, E. Dolfini, M.T. Bardella, L. Elli, C. Terrani, F. Forlani. - In: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. - ISSN 0021-8561. - 55:6(2007 Mar 21), pp. 2482-2488.
Celiac-related properties of chemically and enzymatically modified gluten proteins
C. BertiPrimo
;L. RoncoroniSecondo
;M.L. Falini;R. Caramanico;E. Dolfini;M.T. Bardella;L. Elli;C. TerraniPenultimo
;F. Forlani
2007
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°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.File | Dimensione | Formato | |
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