Kinetic interactions of nanocomplexes between astaxanthin esters with different molecular structures and β-lactoglobulin.

The influence of different fatty acid carbon chains on the kinetic interactions of nanocomplexes between esterified astaxanthin (E-Asta) and β-lactoglobulin (β-Lg) were investigated by multi-spectroscopy and molecular modeling techniques. We synthesized ten different E-Asta bound to β-Lg and formed nanocomplexes (< 300 nm). Fluorescence spectroscopy showed moderate affinities (binding constants Ka = 103-104 M-1). Docosahexaenoic acid astaxanthin monoester (Asta-C22:6) had the strongest binding affinity towards β-Lg (Ka = 3.77 × 104 M-1). The fluorescence quenching of β-Lg upon binding of E-Asta displayed a static mechanism, with binding sites (n) equal to 1. Fourier transform infrared spectroscopy and ultraviolet-visible absorption spectroscopy revealed that E-Asta might enter the β-Lg hydrophobic cavity, leading to unfolding of the peptide chain skeleton. In summary, β-Lg and E-Asta can form stable nanocomplex emulsions to achieve an effective delivery process for E-Asta.