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Polymer conformation structure of wheat proteins and gluten subfractions revealed by ATR-FTIR
- Li, W., Dobraszczyk, B.J., Dias, A., Gil, A.M.
- Cereal chemistry 2006 v.83 no.4 pp. 407-410
- wheat, gluten, protein composition, protein secondary structure, wheat flour, cultivars, gliadin, glutenins, gels, infrared spectroscopy
- The polymer conformation structure of gluten extracted from a Polish wheat cultivar, Korweta, and gluten subfractions obtained from 2 U.K. breadmaking and biscuit flour cultivars, Hereward and Riband, was investigated using attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR). The results showed the conformation of proteins varied between flour, hydrated flour, and hydrated gluten. The beta-sheet structure increased progressively from flour to hydrated flour and to hydrated gluten. In hydrated gluten protein fractions comprising gliadin, soluble glutenin, and gel protein, beta-sheet structure increased progressively from soluble gliadin and glutenin to gluten and gel protein; beta-sheet content was also greater in the gel protein from the breadmaking flour Hereward than the biscuit flour Riband.