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Polymer Conformation Structure of Wheat Proteins and Gluten Subfractions Revealed by ATR‐FTIR
Author(s) -
Li W.,
Dobraszczyk B. J.,
Dias A.,
Gil A. M.
Publication year - 2006
Publication title -
cereal chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.558
H-Index - 100
eISSN - 1943-3638
pISSN - 0009-0352
DOI - 10.1094/cc-83-0407
Subject(s) - glutenin , chemistry , gluten , gliadin , fourier transform infrared spectroscopy , food science , wheat flour , wheat gluten , cultivar , polymer , attenuated total reflection , infrared spectroscopy , chemical engineering , biochemistry , botany , organic chemistry , protein subunit , biology , engineering , gene
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.