Insight into the solubilization mechanism of wheat gluten by protease modification from conformational change and molecular interaction perspective.

The low solubility limits the utilization of other functional characteristics of wheat gluten (WG). This study effectively improved the solubility of WG through protease modification and explored the potential mechanism of protease modification to enhance the solubility of WG, further stimulating the potential application of WG in the food industry. Solubility of WG modified with alkaline protease, complex protease, and neutral protease was enhanced by 98.99%, 54.59%, and 51.68%, respectively. Notably, the content of β-sheet was reduced while the combined effect of hydrogen bond and ionic bond were increased after protease modification. Meanwhile, the reduced molecular size and viscoelasticity as well as the elevated surface hydrophobicity, thermostability, water absorption capacity, and crystallinity were observed in modified WG. Moreover, molecular docking indicated that protease was specifically bound to the amino acid residues of WG through hydrogen bonding, hydrophobic interaction, and salt bridge. [Display omitted] • Solubility of wheat gluten (WG) was improved after treatment by three proteases. • WG bound to proteases mainly through non-covalent interactions at specific sites. • Protease modification induced β-sheet changed into α-helix, β-turn and random coil. • Proteases enhanced the combined effect of hydrogen bond and ionic bond in WG. [ABSTRACT FROM AUTHOR]