Effects of metal phenolic networks (MPNs) on the structural, IgE binding capacity and functional properties of whey protein isolates: Insights gained from polyphenols constructing MPN

s The development of the food industry has led to an increasing demand for whey protein raw materials with hypoallergenic and excellent functional properties. In this study, five polyphenols, chlorogenic acid (CHA), epigallocatechin gallate (EGCG), caffeic acid (CA), gallic acid (GA) and quercetin (QE), were selected to investigate the effect of metal phenolic networks (MPNs) on whey protein isolate (WPI) on the structure, immunoglobulin E (IgE) binding capacity and functional properties. The results show that polyphenols containing more phenolic hydroxyl groups to construct catechol MPNs (EGCG-Fe 3+ ) and multimodal MPNs (QE-Fe 3+ ) lead to a more de-folded and flexible structure of WPIs. This resulted in their modified WPIs exhibiting lower IgE binding capacity (80.08% and 86.90%) and excellent solubility, antioxidant activity, emulsification properties and foaming properties. This study provides a novel and effective potential strategy for WPI modification. Furthermore, this approach shows potential in reducing the allergenicity of WPI while improving the functional properties.