Abstract
The aim of this research was to clearly clarify the deterioration mechanism of heat-denatured gluten proteins by exploring the change of aggregation and structural characteristics of heat-denatured gluten proteins in the steamed bread system and the steamed gluten system during frozen storage. An increase in the total SDS-soluble protein content was determined, which mainly attributed to the soluble monomer protein content increased. Combined with the significant increase of free sulfhydryl, from 3.12 μmol/g to 5.06 μmol/g and 2.64 μmol/g to 3.29 μmol/g, respectively, it can be inferred that the proteins depolymerization induced by frozen storage was mainly involved in the breakdown of heat-induced glutenin-gliadin disulfide cross-linking. Frozen storage induced the conversion of random coil structure to β-sheet structure and a ruptured microstructure with small fragment was observed. Moreover, the protein of steamed bread system was easier to depolymerize than that of the steamed gluten system.
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