Effect of sheeting stress and heating on the molecular chain structure, size, and conformation of gluten proteins during noodle processing

In this paper, the changes in molecular structure, size distribution, and conformation of gluten induced by the mechanical stress during sheeting and the heating effect during cooking of noodles were investigated by atomic force microscopy (AFM), X-ray scattering (SAXS), and size-exclusion chromatography multi-angle laser light scattering (SEC-MALLS). AFM results showed that the height and width of gluten molecular chains were decreased after calendering and increased post-cooking. Calendering reduced the molecular size and compacted the gluten network (increased D_m). The SDS extractable gluten components showed a quasi-spherical chain conformation but gradually changed to a random coil conformation due to heating. According to SEC-MALLS profiles, calendering and appropriate heating (4 min) promoted the homogeneity of molecular mass of glutenin polymer. The mechanical depolymerization and the heat-promoted polymerization of gluten could be due to the breakage and formation of disulfide bonds and the interconversion of sulfhydryl groups.