FTIR spectroscopic characterization of soy proteins obtained through AOT reverse micelles

Formation of macromolecules in wheat gluten/starch mixtures during twin‐screw extrusion: effect of different additives

“…To obtain information about the changes occurring at the secondary level of folding in the process of extrusion, FTIR spectra in amide I band were analyzed further. The assignment of secondary structures in amide I region of protein FTIR spectrum as: α ‐helices, 1650–1660 cm −1 ; β ‐sheets, 1610–1640 and 1670–1680 cm −1 ; β ‐turns, 1660–1670 and 1680–1700 cm −1 ; and random coils, 1640–1650 cm −1 , respectively . The percentages of α ‐helices, β ‐sheets, β ‐turns and random coils are shown in Table .…”

The structural properties and antigenicity of soybean glycinin by glycation with xylose

“…The protein secondary structure is reflected in the 1600–1700 cm −1 range, which is the characteristic absorption band for protein amino I. The following parameters were used in the study: β‐sheet, 1600–1640 cm −1 ; disordered structure, 1640–1650 cm −1 ; α‐helix structure, 1650–1660 cm −1 ; and β‐turn structure, 1660–1700 cm −1 . The data were analyzed using PeakFit V4.12 software, which depicted the secondary structure as shown in Table .…”

Effects of saccharide on the structure and antigenicity of β-conglycinin in soybean protein isolate by glycation

“…The characteristic absorption band of protein amino I in the 1,600-1,700 cm −1 range reflects the protein secondary structure. The following parameters were used in the current manuscript based on literature review: β-sheet, 1,600-1,640 cm −1 ; disordered structure, 1,640-1,650 cm −1 ; α-helix structure, 1,650-1,660 cm −1 ; and β-turn structure, 1,660-1,700 cm −1 [32]. The changes in protein secondary structure were analyzed by the Peak Fit version 4.12 software ( Table 2).…”