3 research outputs found
Efficacy of Food Proteins as Carriers for Flavonoids
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), β-casein and gelatin hydrolysates, in particular
fish gelatin, were found to be the most promising carriers with an
affinity on the order of 10<sup>4</sup> M<sup>–1</sup>. 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 β-casein were required to complex EGCG on the
basis of their maximal binding capacity. When the absence of turbidity
is taken into account, β-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