Abstract
Gluten samples were obtained from two wheat flours with different levels of total protein in the presence or absence of sodium chloride (2% flour base). The dynamic oscillation rheology, large extensional deformation, confocal laser scanning microscopy (CLSM), transmission electron microscopy (TEM) and chemical analysis of disulfide bond linkages and the ratio of polymeric glutenins and monomeric gliadins were used to investigate the effect of salt on the structure and rheological properties of gluten. CLSM and TEM images showed that NaCl caused the gluten to form fibrous structure. The presence of NaCl increased non-covalent interactions and β-sheet structure, measured by FTIR, in gluten proteins. The gluten matrix formed with salt resulted in higher tan δ values corresponding to a less elastic network when measured using oscillatory rheometry. Large deformation extensional measurements showed that the maximum force to fracture were lower for the gluten samples prepared in the presence of NaCl. The results from this study indicate that changes in the solvent quality due to the presence of NaCl during dough mixing result in different molecular conformation and network structure of gluten proteins which contributed to the differences in the rheological properties.
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