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

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-FT...

Full description

Saved in:
Bibliographic Details
Published in:Cereal chemistry 2006-07, Vol.83 (4), p.407-410
Main Authors: Li, W, Dobraszczyk, B.J, Dias, A, Gil, A.M
Format: Article
Language:English
Subjects:
beta-sheets
Biological and medical sciences
Cereal and baking product industries
cultivars
Food industries
Fundamental and applied biological sciences. Psychology
gels
gliadin
Gluten
glutenins
hydrated flour
hydrated gluten
infrared spectroscopy
Polymers
protein composition
protein secondary structure
wheat
wheat flour
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0009-0352
1943-3638
DOI:10.1094/CC-83-0407