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Updated: Jun 30, 2025

Author Spotlight: Integrating Biochemical Functions of β-Glucanases and Peroxidase Enzymes in Wheat-RWA Interaction
Published on: July 26, 2024
Insight into the solubilization mechanism of wheat gluten by protease modification from conformational change and
Weixiao Li1, Qianxin Zhou1, Jianxia Xu1
1Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei 230036, China.
Abstract:
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.
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