Abstract
Preheating proteins have the potential to improve anthocyanin stability. Our aim was to investigate the effect of preheated whey protein isolate (WPI) on the color stability and astringency of the beverage model system in the presence of rose anthocyanin extracts (RAEs), and to explore the mechanism of interaction between preheated WPI and RAEs. The secondary structure, particle size and transparency of WPI were obviously changed by preheating. WPI preheated at 100°C (WPI100) could effectively improve the color stability of RAEs in the beverage model system. Importantly, the WPI100-RAEs in the beverage model system exhibited the smallest particle size and the weakest astringency effect. In addition, different preheated WPIs could interact with RAEs non-covalently, and the interaction forces are hydrogen bonding and van der Waals forces, among which WPI100 had the strongest binding ability to RAEs. These results will provide a new insight into the development of protein-anthocyanin beverages.
Published Version
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