Molecular Structure Evaluation of Wheat Gluten during Frozen Storage

The effects of frozen storage (0–120 day) on the secondary structure and molecular chain conformation of hydrated gluten were investigated using Fourier transform infrared spectroscopy (FTIR) and atomic force microscopy (AFM). After frozen storage, no changes were observed in the secondary structure of the 60% hydrated gluten; spectra were consistent with a tight ordered structure with many interchain hydrogen bond interactions. For the dehydrated gluten, more complex changes took place: during frozen storage for up to 60 days, there were distinctive changes in the low-frequency region of the amide I band (1618–1633 cm^?1) which were attributed to changes in the β-sheet structure. However, with the increase of frozen storage from 60 to 120 days, a band near 1614 cm^?1 replaced that at 1659 cm^?1 illustrate that the formation of protein aggregates during the long-time frozen storage, which along with the establishment of new intermolecular non-covalent bonds within the protein molecule or between two neighboring molecules. AFM images showed that the gluten chain formed a fibril-like branched network, and this network was weakened with increasing frozen storage time.