Magnetic field improves the functional properties of frozen gluten by inhibiting structural deteriorations of glutenin and gliadin

The structural and functional properties of glutenin and gliadin after magnetic field (MF)-assisted freezing-thawing cycles treatment was compared to clarify the protective mechanism of MF on frozen dough. Compared with conventional frozen glutenin and gliadin, MF inhibited the freezing-induced structural unfolding of glutenin and the rearrangement of gliadin, whereby the surface hydrophobicity individually increased and decreased by 23.5% and 47.5%. Raman spectra and atomic force microscope analyses showed that MF-assisted freezing treatment provided both the glutenin and gliadin with a higher aggregation, as manifest with the increased stable disulfide bond conformation (g-g-g), average molecular chain height and width. Small angle X-ray scattering indicated that the conformation and fractal dimensions of MF-assisted frozen glutenin and gliadin were close to those of fresh groups. MF individually enhanced the water retention capacity and emulsifying performances of gliadin and glutenin, which synergistically contributed to an improved foaming performances in a reconstituted gluten model system. This study established a substantial relationship between the individual component structural changes and whole gluten functional properties, which is benefit to the application of MF in frozen market.