Biochemical modifications of gliadins induced by microbial transglutaminase on wheat flour (Articolo in rivista)

Type
Label
  • Biochemical modifications of gliadins induced by microbial transglutaminase on wheat flour (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bbagen.2013.07.021. (literal)
Alternative label
  • Mazzeo MF, Bonavita R, Maurano F, Bergamo P, Siciliano RA, Rossi M. (2013)
    Biochemical modifications of gliadins induced by microbial transglutaminase on wheat flour
    in Biochimica et biophysica acta. G, General subjects (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Mazzeo MF, Bonavita R, Maurano F, Bergamo P, Siciliano RA, Rossi M. (literal)
Pagina inizio
  • 5166 (literal)
Pagina fine
  • 5174 (literal)
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  • 1830 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 9 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 11 (literal)
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  • PubMe (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Food Sciences, CNR, Avellino, Italy. (literal)
Titolo
  • Biochemical modifications of gliadins induced by microbial transglutaminase on wheat flour (literal)
Abstract
  • BACKGROUND: Celiac disease (CD) is an immune-mediated disorder caused by the ingestion of wheat gluten. A lifelong, gluten-free diet is required to normalize the intestinal mucosa. We previously found that transamidation by microbial transglutaminase (mTGase) suppressed the gliadin-specific immune response in intestinal T-cell lines from CD patients and in models of gluten sensitivity. METHODS: SDS-PAGE, Western blot, ELISA, tissue transglutaminase (tTGase) assay and nano-HPLC-ESI-MS/MS experiments were used to analyze prolamins isolated from treated wheat flour. RESULTS: Gliadin and glutenin yields decreased to 7.6±0.5% and 7.5±0.3%, respectively, after a two-step transamidation reaction that produced a water-soluble protein fraction (spf). SDS-PAGE, Western blot and ELISA analyses confirmed the loss of immune cross-reactivity with anti-native gliadin antibodies in residual transamidated gliadins (K-gliadins) and spf as well as the occurrence of neo-epitopes. Nano-HPLC-ESI-MS/MS experiments identified some native and transamidated forms of celiacogenic peptides including p31-49 and confirmed that mTGase had similar stereo-specificity of tTGase. Those peptides resulted to be 100% and 57% modified in spf and K-gliadins, respectively. In particular, following transamidation p31-49 lost its ability to increase tTGase activity in Caco-2 cells. Finally, bread manufactured with transamidated flour had only minor changes in baking characteristics. CONCLUSIONS: The two-step transamidation reaction modified the analyzed gliadin peptides, which are known to trigger CD, without influencing main technological properties. GENERAL SIGNIFICANCE: Our data shed further light on a detoxification strategy alternative to the gluten free diet and may have important implications for the management of CD patients. (literal)
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