Hydrogen bonding-mediated regulation of protein conformation and starch crystallization in dough: the role of emulsifier hydrophilicity.

This study utilized three emulsifiers with distinct hydrophilic-lipophilic balances (HLB)-monoglycerides (MAG, HLB 3.8), soy phospholipids (PLs, HLB 7.0), and sucrose esters (SE, HLB 11.0)-as structural modifiers to investigate the role of hydrogen bonding in regulating the synchronization of protein aggregation and starch gelatinization. The strong hydrogen bonds formed between SE and proteins significantly promote the aggregation of protein macromolecules and the formation of β-sheet structures, thereby enhancing the viscoelastic properties of fresh dough. The formation of V-type starch complexes with SE and MAG decreased the levels of free amylose, which interfered with the hydrogen bonding between protein and starch. In addition, the changes of hydrogen bonding content in samples were consistent with the amylose content. The crucial role of hydrogen bonding in regulating the conformational changes and interfacial interactions of starch and proteins provides researchers with precise control strategies for the preparation of starch-protein-based products.