数字农科院2.0

Unraveling the mechanism of frozen dough moisture-protein structure-ice crystal growth interactions at different glutenin/ gliadin ratios

文献类型： 外文期刊

作者： Jiang, Jikai;Yang, Jingjie;Fan, Xiangqi;Zhang, Yingquan;Li, Ming;Zhao, Bo;Zhang, Bo;Guo, Boli;Zhong, Geng

作者机构：

关键词： Frozen dough;Glutenin/gliadin ratio;Gluten network structure;Moisture-distribution;Ice crystal growth

期刊名称： INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

ISSN： 0141-8130

年卷期： 2025 年 335 卷

页码：

收录情况： SCIE（2025版） ; ; EI（2025版）

摘要： Ice crystallization critically affects frozen dough quality, yet the molecular role of gluten composition in ice-crystallization remains unclear. This study investigates how glutenin/gliadin ratios regulate ice formation through structural interactions and water immobilization. At the optimal 1.5:1 ratio (S2 group), covalent crosslinking (beta-sheet-mediated) and hydrogen bonding (alpha-helix-dependent) synergistically stabilize the dough, with hydrophobic interactions further enhancing network stability, resulting in superior cryoprotection. Compared to fresh dough, the S2 sample exhibited the smallest increase in ice porosity at 1.39 %. Excess glutenin (>1.5:1) disrupted glutenin-starch interfaces, resulting in a 2.99 % increase in ice porosity. Predominant gliadin (1:2) weakened gluten structure, elevating water mobility and increasing ice porosity by 1.73 %. Both imbalances exacerbated ice-related structural damage. This is the first molecular-level evidence that glutenin-gliadin equilibrium intrinsically regulates cryoprotection in frozen dough.

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