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

Abstract

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.

In situ study of water uptake by the seeds, endosperm and husk of barley using infrared spectroscopy

“…Eigenvectors of the first three principal components that explain most of the variability in whole seed samples analyzed using attenuated total reflectance. spectral range associated with amylose and amylopectin (1100-900 cm À1 ), amide I (1600-1690 cm À1 ) and lipids (1750 cm À1 ) [13,21,33,34]. The MIR band region between 1100 and 900 cm À1 might be also associated with the crystalline structure of the starch as reported by other authors [13,21,33,34].…”

“…The frequency at 1635 cm À1 is associated with OH bond stretching and bending modes of water [8]. Frequencies at 1155 and 1036 cm À1 were associated with carbohydrates while bands related to CÀC, CÀO stretching and CAOAH bending modes can be found between 1400 and 1200 cm À1 [13,21,33,34]. The frequency at 1250 cm À1 was related with cellulosic or structural carbohydrates compounds while the frequency at 1400 cm À1 was related with the presence of phenolic compounds (CACAC aromatic ring stretch) as well as with the phenol OH bending (1410-1310 cm À1 ) [8].…”

Viscoelastic properties of tablets from Osborne fractions, pentosans, flour and bread evaluated by creep tests

“…The same trend was observed for the viscosity coefficients, since that fraction contributed with 72.2% of the total viscosity, almost 10 times the viscosity of the glutenins fraction. Li et al (2006) studied the polymer conformation of structure of wheat proteins and noted that the presence of β-sheet structure and content in gliadins and glutenins are quite different, the glutenins being those of lower content. Those authors proposed that gliadin and soluble glutenin molecules mainly form β-turn structures, and insoluble glutenins in gel proteins form a β-sheet structure, which seem to be an important contributor to the formation of a network structure and, subsequently, affected the elastic and long-time relaxation properties of gluten proteins.…”

Conformational changes of polymers in model batter systems

“…Moreover in combination with new methods of sample presentation such as Attenuated Total Reflectance (ATR) e which enables analysis of food matrix directly in the solid or liquid state without further preparation e FTIR allows the acquisition of high-quality spectra with high reproducibility from previously quite intractable materials ( Van de Voort, Sedman, Emo, & Ismail, 1992;Wilson, Goodfellow, & Belton, 1988). ATR-FTIR spectroscopy has been used to probe gluten secondary structure in dough under various conditions and formulations Bock, Connelly, & Damodaran, 2013;Jazaeri et al, 2015;Kaddour et al, 2008;Li, Dobraszczyk, Dias, & Gil, 2006;Meziani et al, 2011;Sivam et al, 2012;Wang et al, 2014;Wellner et al, 2005). More recently, the poor quality of bran-enriched bread was explained by the conversion of b-turn structure into b-sheet and random structures when bran is added to the gluten or to wheat .…”