In this study, aggregation of fucoxanthin (FX) and its effects on binding and delivery properties of whey proteins were explored. Initially, the H- and J-aggregates of FX were successfully prepared by adjusting the water/ethanol ratio and water-dripping rate. The transition from J- to H-aggregates was observed over the standing time. Then, the molecular arrangement of FX H-aggregates was analyzed using the point-dipole approximation model and molecular dynamics, showing that their intermolecular distance and angle were about 5.0-6.7 Å and -35° to 35°, respectively. The transformation of J- to H-aggregates was also observed during molecular dynamics, with a shortened intermolecular distance, a reduced solvent accessible surface area, an enhanced interaction force, and a narrowed dihedral angle. Further, the interactions of whey proteins with different forms of FX were investigated, indicating that both β-lactoglobulin and whey protein isolates could form complexes with the monomers, H-aggregates, and J-aggregates of FX. In terms of affinity, whey proteins bound FX monomers more strongly than aggregates. Furthermore, the complexes comprising whey proteins and monomeric FX had better delivery capabilities than aggregated FX, manifested in encapsulation efficiency, physical stability, and bioaccessibility.
Keywords: aggregates; fucoxanthin; interaction; molecular dynamics; whey proteins.