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Structural, Binding and Functional Properties of Milk Protein-Polyphenol Systems: A Review.

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Název: Structural, Binding and Functional Properties of Milk Protein-Polyphenol Systems: A Review.
Autoři: van de Langerijt, Tessa M, O'Mahony, James A, Crowley, Shane V
Zdroj: Molecules (Basel, Switzerland) ; 28 ; 5 ; Switzerland
Rok vydání: 2023
Sbírka: Lenus - Irish Health Publications Archive (HSE - Health Service Executive)
Témata: aggregates, blood serum albumin aggregates, casein nanoparticles, complex formation, micelles, milk proteins, native casein micelles, polyphenols, protein-polyphenol interaction, re-assembled casein micelles
Popis: 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.
Druh dokumentu: article in journal/newspaper
Jazyk: English
Relation: http://hdl.handle.net/10147/641832; Molecules (Basel, Switzerland)
DOI: 10.3390/molecules28052288
Dostupnost: http://hdl.handle.net/10147/641832
https://doi.org/10.3390/molecules28052288
Rights: Attribution 4.0 International ; http://creativecommons.org/licenses/by/4.0/
Přístupové číslo: edsbas.C4BA29EF
Databáze: BASE
Popis
Abstrakt: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.
DOI:10.3390/molecules28052288