Enrichment of flavonoids in food is often limited by their off-tastes, which might be counteracted by the use of food proteins as carriers of flavonoids. Various milk proteins, egg proteins, and gelatin hydrolysates were compared for their binding characteristics to two flavan-3-ols. Among the proteins tested for their affinities toward epigallocatechin gallate (EGCG), ß-casein and gelatin hydrolysates, in particular fish gelatin, were found to be the most promising carriers with an affinity on the order of 104 M-1. A flexible open structure of proteins, as present in random coil proteins, was found to be important. The saturation of binding observed at high flavonoid/protein ratios was used to estimate the maximal binding capacity of each protein. To reach a daily intake of EGCG that has been associated with positive health effects, only 519 mg of gelatin B and 787 mg of ß-casein were required to complex EGCG on the basis of their maximal binding capacity. When the absence of turbidity is taken into account, ß-casein prevails as carrier. Three selected proteins were further investigated for their binding potential of representative flavonoids differing in their C-ring structure. An increase in hydrophobicity of flavonoids was related to a higher affinity for proteins, and the presence of a gallic acid ester on the C-ring showed an overall higher affinity.
- isothermal titration calorimetry
- tea catechins
- bitter taste
- green tea