Polyphenols (PP) are linked to health benefits (e.g., prevention of cancer, cardiovascular disease and obesity), which are mainly attributed to their antioxidant activity. During digestion, PP are oxidised to a significant degree reducing their bio-functionality. In recent years, the potential of various milk protein systems, including β-casein micelles, β-lactoglobulin aggregates, blood serum albumin aggregates, native casein micelles and re-assembled casein micelles, to bind and protect PP have been investigated. These studies have yet to be systematically reviewed. The functional properties of the milk protein-PP systems depend on the type and concentration of both PP and protein, as well as the structure of the resultant complexes, with environmental and processing factors also having an influence. Milk protein systems protect PP from degradation during digestion, resulting in a higher bioaccessibility and bioavailability, which improve the functional properties of PP upon consumption. This review compares different milk protein systems in terms of physicochemical properties, PP binding performance and ability to enhance the bio-functional properties of PP. The goal is to provide a comprehensive overview on the structural, binding, and functional properties of milk protein-polyphenol systems. It is concluded that milk protein complexes function effectively as delivery systems for PP, protecting PP from oxidation during digestion.

This study aimed to determine whether the fat and protein content in dairy‐fruit blends prepared using full‐fat, semi‐skimmed, skimmed or high‐protein milk in combination with freeze‐dried blackberry puree influenced the bioaccessibility and bioavailability of blackberry polyphenols and organic acids. Samples were subjected to in vitro digestion, after which bioavailability was analysed with a Caco‐2 cell model. The addition of puree to milk resulted in the formation of protein aggregates, which partially protected anthocyanins during digestion. Milk fat may have increased the bioaccessibility of anthocyanins while reducing permeability through the Caco‐2 cells, leading to a lower bioavailability in tested samples.

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