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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.

Cereal Chem. 80(3):333-338Relaxation behavior was measured for dough, gluten and gluten protein fractions obtained from the U.K. biscuitmaking flour, Riband, and the U.K. breadmaking flour, Hereward. The relaxation spectrum, in which relaxation times (t) are related to polymer molecular size, for dough showed a broad molecular size distribution, with two relaxation processes: a major peak at short times and a second peak at times longer than 10 sec, which is thought to correspond to network structure, and which may be attributed to entanglements and physical cross-links of polymers. Relaxation spectra of glutens were similar to those for the corresponding doughs from both flours. Hereward gluten clearly showed a much more pronounced second peak in relaxation spectrum and higher relaxation modulus than Riband gluten at the same water content. In the gluten protein fractions, gliadin and acetic acid soluble glutenin only showed the first relaxation process, but gel protein clearly showed both the first and second relaxation processes. The results show that the relaxation properties of dough depend on its gluten protein and that gel protein is responsible for the network structure for dough and gluten.

Stickiness in wheat flour doughs was studied as a function of rheological and surface properties. Adhesion was measured using a modified peel test at various water additions, peel rates and peel layer thicknesses. Peeling energy gave a strong positive correlation with subjective bakery stickiness ratings. Peeling forces were highly rate dependent and showed transitions from sticky to nonsticky behvaiour with increasing rate of peeling. Dynamic storage modulus showed a negative correlation with stickiness ratings, suggesting stickiness is primarily a rheologically controlled process. Stress relaxation gradients were greater for sticky doughs and were very similar to peeling force vs. rate slopes, again indicating that adhesion is principally a function of the rheological properties of the dough. Surface tension measurements of sticky and nonsticky dough/liquor interfaces showed no significant differences and are typical of protein solutions. Calculated values of the interfacial surface energy between dough and interface were about 100 mJ/m2, typical of secondary bonding interactions such as polar or van der Waals bonding.