Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region |
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Authors: | M Carbonaro A Nucara |
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Institution: | 1. Istituto Nazionale di Ricerca per gli Alimenti e la Nutrizione, Via Ardeatina, 546, 00178, Rome, Italy 2. Dipartimento di Fisica, Università di Roma “La Sapienza”, Rome, Italy
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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. |
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Keywords: | |
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