Journal
FOOD CHEMISTRY
Volume 384, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2022.132492
Keywords
Rose anthocyanin extracts; Whey protein isolate; Interaction mechanism; Spectroscopy; Molecular docking
Funding
- Xinjiang Innovation Team Construction Project in Key Areas, National Key Technology R&D Program for the 13th five-year plan [2017 BAD 33B05]
- Jiangsu province Collaborative Innovation Center for Food Safety and Quality Control industry development program
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This study investigated the non-covalent interaction mechanism between rose anthocyanin extract (RAEs) and whey protein isolate (WPI) and compared it with the interaction mechanism between pure anthocyanin (PC) and WPI. The results showed that RAEs and WPI had non-covalent interactions under different pH conditions, with hydrogen bonds and van der Waals forces playing a role. Interestingly, PC and WPI also exhibited non-covalent interactions, with hydrogen bonds and van der Waals forces as the driving forces. Additionally, changes in WPI's secondary structure were observed in both RAEs and PC.
The non-covalent interaction between anthocyanin and dietary protein had an impact on their physicochemical property. The purpose of this study was to study the non-covalent interaction mechanism between rose anthocyanin extract (RAEs) and whey protein isolate (WPI), and further compare the interaction mechanism with pure anthocyanin (PC) and WPI. At pH 3.0 and pH 7.0, RAEs and WPI had non-covalent interactions in the two systems with two types of unequal and mutually influencing binding sites, and the interaction forces were both hydrogen bonds and van der Waals forces. Interestingly, PC and WPI also had non-covalent interactions in both systems, the number of which binding sites was about one type, and the forces were hydrogen bonds and van der Waals forces. In addition, a variety of spectral combination techniques indicated that RAEs and PC caused similar changes in the secondary structure of WPI.
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