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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2013

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Biochemical modifications of gliadins induced by microbial transglutaminase on wheat flour

Anno di pubblicazione: 2013

Formato: Elettronico Cartaceo

Autori: Mazzeo MF, Bonavita R, Maurano F, Bergamo P, Siciliano RA, Rossi M.

Affiliazioni autori: Institute of Food Sciences, CNR, Avellino, Italy.

Autori CNR:

  • PAOLO BERGAMO
  • FRANCESCO MAURANO
  • MARIA FIORELLA MAZZEO
  • MAURO ROSSI
  • ROSA ANNA SICILIANO

Lingua: inglese

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.

Lingua abstract: inglese

Pagine da: 5166

Pagine a: 5174

Pagine totali: 9

Rivista:

Biochimica et biophysica acta. G, General subjects Elsevier Scientific Publ. Co.
Paese di pubblicazione: Paesi Bassi
Lingua: inglese
ISSN: 0304-4165

Numero volume: 1830

Numero fascicolo: 11

DOI: 10.1016/j.bbagen.2013.07.021.

Referee: Sì: Internazionale

Indicizzato da: PubMed [23891939]

Parole chiave:

  • CD
  • Celiac disease
  • GFD
  • Gliadin
  • K-C(2)H(5)
  • K-gliadins
  • Microbial transglutaminase
  • PEPs
  • Transamidation
  • gluten-free diet
  • insoluble transamidated gliadin
  • lysine ethyl ester
  • mTGase
  • microbial transglutaminase
  • nano-HPLC-ESI-MS/MS
  • prolyl endopeptidases
  • spf
  • tTGase
  • tandem mass spectrometry coupled with nano-reverse phase liquid chromatography
  • tissue transglutaminase
  • water-soluble protein fraction

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