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Polymer Conformation Structure of Wheat Proteins and Gluten Subfractions Revealed by ATR-FTIR

¹The University of Reading, School of Food Biosciences, UK. ²University of Aveiro, CICECO, Dept. of Chemistry, 3810-193 Aveiro, Portugal. ³Corresponding author. E-mail: w.li@reading.ac.uk

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 β-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, β-sheet structure increased progressively from soluble gliadin and glutenin to gluten and gel protein; β-sheet content was also greater in the gel protein from the breadmaking flour Hereward than the biscuit flour Riband.