Amino Acids

, Volume 38, Issue 3, pp 679–690

Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region

Authors

    • Istituto Nazionale di Ricerca per gli Alimenti e la Nutrizione
  • A. Nucara
    • Dipartimento di FisicaUniversità di Roma “La Sapienza”
Review Article

DOI: 10.1007/s00726-009-0274-3

Cite this article as:
Carbonaro, M. & Nucara, A. Amino Acids (2010) 38: 679. doi: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

FT-IRInfrared spectroscopyFood proteinsSecondary structure

Copyright information

© Springer-Verlag 2009