chicken meat. Differential spectral analysis revealed significant
differences between R and FT samples within the protein region
(1800e1500 cm1) at 1660e1628 cm1 (Fig. 1). Spectral alterations
in this frequency area are primarily determined by the confirmation
sensitive amide I band (1670e1625 cm1) principally based on
symmetric stretching vibrations of the carbonyl (C]O) functional
group. The amide I band is indicative for changes in the protein
secondary structure including alterations in the backbone conformation
and the hydrogen bonding pattern. Subtractive FTIR spectral
analysis revealed changes between R and FT samples associated
to a-helical (1651 cm1) and b-plated sheet (1639 cm1,1633 cm1)
protein secondary structures.