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Polymer conformation structure of wheat proteins and gluten subfractions revealed by ATR-FTIR

Li, W., Dobraszczky, B.J., Dias, A. and Gil, A.M. (2006) Polymer conformation structure of wheat proteins and gluten subfractions revealed by ATR-FTIR. Cereal Chemistry, 83 (4). pp. 407-410. ISSN 0009-0352

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To link to this item DOI: 10.1094/cc-83-0407

Abstract/Summary

The polymer conformation structure of gluten extracted from a Polish wheat cultivar, Korweta, and gluten subtractions 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.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences
ID Code:13211
Uncontrolled Keywords:TRANSFORM INFRARED-SPECTROSCOPY, SUBUNITS, MACROPOLYMER, ELASTICITY, GLIADINS

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