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The Cereal Processing and Quality Control Innovation Team Unveils the Key Role of Gluten Proteins in Maintaining Structural and Quality Stability of Frozen Dough

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The Cereal Processing and Quality Control Innovation Team of IFST-CAAS, has recently made significant progress in the field of frozen dough quality research. The related findings have been published in the internationally renowned journal International Journal of Biological Macromolecules (JCR Q1, IF = 8.5). The paper was authored by PhD candidate Mohsin Rasheed as the first author, with Professor Boli Guo as the corresponding author. This work was supported by the Innovation Program of IFST-CAAS (CAAS-ASTIP-2024-IFST), and the Hebei Modern Agricultural Industry Technology System Project on Alkali-Saline Wheat Processing and Brand Development (HBCT2024030205).

With the accelerating pace of modern life, frozen dough products have become increasingly popular in the food industry due to their convenience. However, quality deterioration during frozen storage, including increased hardness and reduced elasticity, remains a major concern as it adversely affects the sensory properties of the final product. These issues are closely linked to the structural changes in gluten proteins during freezing. Therefore, understanding the impact of wheat flour with varying gluten content on the stability of frozen dough is essential for optimizing formulations and improving storage quality.

This study systematically investigated the effects of wheat flour with different gluten contents on the quality of frozen dough over a 90-day storage period, integrating both macro-scale rheological characteristics and microstructural analyses. The results demonstrated that high-gluten dough exhibited superior freeze-thaw stability, characterized by a smaller increase in hardness and a lesser decline in elasticity, cohesiveness, and adhesiveness. The variations in storage and loss moduli were also minimal. Protein structure analysis revealed that the increase in sulfhydryl (-SH) content in high-gluten dough was limited (10.38 to 15.84 µmol/g), indicating less disulfide bond cleavage. In contrast, low-gluten dough showed a significant rise in -SH content (from 8.34 µmol/g to 18.87 µmol/g), suggesting more severe protein structure disruption. Additionally, the content of glutenin macropolymer (GMP) in low-gluten dough decreased dramatically by 86.72%, much higher than the 21.82% reduction observed in high-gluten dough, confirming the extensive depolymerization of its protein network. Scanning electron microscopy further revealed pronounced structural degradation in low-gluten dough after freezing. Secondary structure analysis indicated a conformational shift of gluten proteins from α-helix to β-sheet, β-turn, and random coil during freezing. Correlation analysis showed that α-helix content was positively associated with dough cohesiveness, adhesiveness, and elasticity, whereas β-sheet content was negatively correlated with these properties.

This study elucidate the mechanistic influence of gluten content on the freeze-thaw stability of dough from a multi-scale perspective for the first time, providing a scientific foundation for the rational formulation of frozen dough products.

https://doi.org/10.1016/j.ijbiomac.2025.145621

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