Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region
Top Cited Papers
- 7 April 2009
- journal article
- review article
- Published by Springer Science and Business Media LLC in Amino Acids
- Vol. 38 (3), 679-690
- https://doi.org/10.1007/s00726-009-0274-3
Abstract
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 α-helical, β-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.Keywords
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