DOI: 10.1094/CC-83-0407 |  VIEW ARTICLE

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

W. Li (1), B. J. Dobraszczyk (1), A. Dias (2), and A. M. Gil (2). (1) The University of Reading, School of Food Biosciences, UK. (2) University of Aveiro, CICECO, Dept. of Chemistry, 3810-193 Aveiro, Portugal. (3) Corresponding author. E-mail: <w.li@reading.ac.uk> Cereal Chem. 83(4):407-410. Accepted April 13, 2006. Copyright 2006 AACC International, Inc.

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.