Journal
AMINO ACIDS
Volume 43, Issue 2, Pages 911-921Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-011-1151-4
Keywords
FT-IR; Diffuse reflectance; Food protein structure; Thermal aggregation; Legumes; Digestibility
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Funding
- Ministry of Agricultural Alimentary and Forest Politics
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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 ( beta-sheets, random coil, alpha-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 beta-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 beta-sheet structures of raw legume proteins and the intermolecular beta-sheet aggregates, arising upon heating, are primary factors in adversely affecting the digestibility.
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