Changes of aggregation and structural properties of heat-denatured gluten proteins in fast-frozen steamed bread during frozen storage. (15th December 2021)

• Record Type: Journal Article
• Authors: Qian, Xiaojie; Gu, Yujuan; Sun, Binghua; Wang, Xiaoxi
• Is Part Of: Food chemistry. Volume 365(2021)
• Publication Date: 2021-12-15
• Subjects: Fast-frozen steamed bread -- Heat-denatured gluten -- Frozen storage -- Aggregation properties -- Secondary structure; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2021.130492
• Languages: English
• ISSNs: 0308-8146

Abstract

Graphical abstract: Highlights: Frozen storage induced protein depolymerization for leading to a loose structure. The heat-induced glutenin-gliadin disulfide cross-linking were destroyed. Frozen storage induced the conversion of random coil structure to β-sheet structure. Protein was easier to depolymerize in system of steamed bread than steamed gluten. 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.