期刊
AMINO ACIDS
卷 38, 期 3, 页码 679-690出版社
SPRINGER WIEN
DOI: 10.1007/s00726-009-0274-3
关键词
FT-IR; Infrared spectroscopy; Food proteins; Secondary structure
资金
- Ministry of Agricultural Alimentary and Forest Politics [17/2003]
Fourier transform spectroscopy in the mid-infrared (400-5,000 cm(-1)) (FT-IR) is being recognized as a powerful tool for analyzing chemical composition of food, with special concern to molecular architecture of food proteins. Unlike other spectroscopic techniques, it provides high-quality spectra with very small amount of protein, in various environments irrespective of the molecular mass. The fraction of peptide bonds in alpha-helical, beta-pleated sheet, turns and aperiodic conformations can be accurately estimated by analysis of the amide I band (1,600-1,700 cm(-1)) in the mid-IR region. In addition, FT-IR measurement of secondary structure highlights the mechanism of protein aggregation and stability, making this technique of strategic importance in the food proteomic field. Examples of applications of FT-IR spectroscopy in the study of structural features of food proteins critical of nutritional and technological performance are discussed.
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