Celiac-related properties of chemically and enzymatically modified gluten proteins

Cristiana Berti, Leda Roncoroni, Maria Letizia Falini, Rosita Caramanico, Ersilia Dolfini, Maria Teresa Bardella, Luca Elli, Claudia Terrani, Fabio Forlani

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)2482-2488
Number of pages7
JournalJournal of Agricultural and Food Chemistry
Issue number6
Publication statusPublished - Mar 21 2007


  • Celiac disease
  • Cytotoxicity
  • Deamidation
  • Gluten
  • IgA anti-gliadin antibody
  • Immunoreactivity
  • LoVo cell line

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Food Science
  • Chemistry (miscellaneous)


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