Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study (Articolo in rivista)

Type
Label
  • Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1007/s00726-011-1151-4 (literal)
Alternative label
  • Carbonaro M1, Maselli P 2, Nucara A 2. (2012)
    Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study
    in Amino acids (Wien, Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Carbonaro M1, Maselli P 2, Nucara A 2. (literal)
Pagina inizio
  • 911 (literal)
Pagina fine
  • 921 (literal)
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  • 43 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 11 (literal)
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  • 2 (literal)
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  • 1 Istituto Nazionale di Ricerca per gli Alimenti e la Nutrizione, Via Ardeatina 546, 00178 Rome, Italy 2 Dipartimento di Fisica, Universita` Sapienza di Roma and CNR-SPIN, P.le Aldo Moro 2, 00185 Rome, Italy (literal)
Titolo
  • Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study (literal)
Abstract
  • The secondary structure of proteins in legumes, cereals, milk products and chicken meat was studied by diffuse reflectance infrared spectroscopy in the region of the amide I band. Major secondary structure components ( ?-sheets, random coil, ?-helix, turns), together with the low- and high-frequency side contributions, were resolved and related to the in vitro digestibility behaviour of the different foods. A strong inverse correlation between the relative spectral weights of the ?-sheet structures and in vitro protein digestibility values was measured. Structural modifications in legume proteins induced by autoclaving were monitored by the changes in the amide I spectra. The results indicate that the ?-sheet structures of raw legume proteins and the intermolecular ?-sheet aggregates, arising upon heating, are primary factors in adversely affecting the digestibility. (literal)
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