Lutein bioaccessibility in casein-stabilized emulsions is influenced by the free to acylated carotenoid ratio, but not by the casein aggregation state.

Considering that carotenoids are found acylated to fatty acids in most edible fruits, the influence of the ratio of free to acylated lutein on the hydrolysis extent and bioaccessibility was evaluated by in vitro digestion. For this purpose, for the first time, esterified, free, or a mixture of both carotenoid forms was used in the lipid phase of emulsions stabilized by sodium caseinate (NaCas) and native phosphocaseinate (PPCN). Marigold petals was used as a source of lutein-rich extracts. The emulsions were characterized and the extent of ester hydrolysis, carotenoid recovery, and bioaccessibility were evaluated by LC-DAD-MS/MS. Besides low polydispersity, NaCas and PPCN stabilized emulsions exhibited a constant mean droplet diameter of about 260 and 330 nm, respectively, after 7 days. Caseins were completely digested after the gastric digestion step. Moreover, casein supramolecular structure did not significantly affect carotenoid bioaccessibility. Lutein was majorly found in its free form in all bioaccessible fractions. The carotenoid bioaccessibility increased from 3% to 40% by increasing the percentage of free carotenoids from 0.5 to 100% in the emulsions; but the carotenoid recovery and hydrolysis extent of lutein esters were not affected. In conclusion, emulsion-based systems for carotenoid delivery stabilized either by NaCas or PPCN provided similar carotenoid bioaccessibility. Furthermore, bioaccessibility was inversely dependent on the overall hydrophobicity of the carotenoid extract. Our results suggest that the low bioaccessibility of esterified carotenoids was a consequence of their limited hydrolysis extent. This study provides information that may help design emulsion-based systems stabilized by food protein as a vehicle for carotenoids.

Unraveling the molecular mechanisms underlying interactions between caseins and lutein.

Understanding the food protein binding to bioactive compounds is of utmost importance for the development of efficient protein-based delivery systems. The binding of lutein to sodium caseinate (NaCas) or native casein micelle (PPCN) was investigated at pH 7 to evaluate the effect of casein supramolecular structures on the interaction. Fluorescence quenching, UV-vis spectroscopy, and dynamic light scattering were carried out. Under the medium conditions of interaction analysis (DMSO-water and ethanol-water), lutein exists as H-type aggregates. The investigation of lutein/casein interaction showed a predominantly static mechanism of fluorescence quenching and the presence of two fluorophore populations on NaCas and PPCN, but only one accessible to lutein. Moreover, the Scatchard plot indicated that lutein interacted with both caseins in one binding site. The interaction of lutein with caseins occurred with binding constant Kb of 105 M-1, regardless of casein supramolecular structure.