Tessa Marianne van de Langerijt
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Tessa Marianne van de Langerijt has a total of 13 co-authors. Here are the top co-authors by number of shared publications:
- Shane V. Crowley
School of Food and Nutritional Sciences, University College Cork, T12 TP07 Cork, Ireland
2 shared publications - Alice J. Lucey
Cork Centre for Vitamin D and Nutrition Research, School of Food and Nutritional Sciences, University College Cork, Cork, Ireland
1 shared publication Carine Morgenegg
1 shared publication- Christophe Schmitt
Department of Food Science, Nestlé Research Center, Vers-chez-les-Blanc, CH-1000 Lausanne 26, Switzerland
1 shared publication - Conor C. Carey
Cork Centre for Vitamin D and Nutrition Research, School of Food and Nutritional Sciences, University College Cork, Cork, Ireland
1 shared publication Dilip K. Rai
1 shared publication
Latest Publications
- 22 December 2023
- Published by Elsevier in Food Bioscience
- Vol. 58
Influence of protein and leucine on in vitro accessibility and apparent permeability of phenolic compounds in blackberry-dairy blends
- 22 December 2023
- Published by Elsevier in Food Bioscience
- Vol. 58
Influence of protein and leucine on in vitro accessibility and apparent permeability of phenolic compounds in blackberry-dairy blends
- Open Access
Structural, Binding and Functional Properties of Milk Protein-Polyphenol Systems: A Review
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.
Open AccessStructural, Binding and Functional Properties of Milk Protein-Polyphenol Systems: A Review
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.
- 9 December 2022
- Published by Elsevier in Food Hydrocolloids
- Vol. 137
Influence of charged and non-charged co-solutes on the heat-induced aggregation of soy and pea proteins at pH 7.0
- 9 December 2022
- Published by Elsevier in Food Hydrocolloids
- Vol. 137
Influence of charged and non-charged co-solutes on the heat-induced aggregation of soy and pea proteins at pH 7.0