Abstract
In this work, we investigated the interaction of docosahexaenoic acid (DHA) with β-lactoglobulin (β-Lg) using spectroscopic and crystallographic methods. The fluorescence results showed that DHA formed complexes with β-Lg with a binding constant of 4.13×104 M-1. The secondary structure of β-Lg was not significantly (p>0.05) changed after binding with DHA. Dynamic light scattering showed the particle size of β-Lg-DHA complexes was about 5nm, the same as that of β-Lg alone. The turbidity of DHA in aqueous solution decreased after binding with β-Lg. The crystallographic results showed that DHA was bound at one site in the calyx of β-Lg and that the aliphatic chain was hidden inside the hydrophobic β-barrel while the carboxyl group was located at the calyx entrance. These findings indicate that β-Lg can act as an effective nanocarrier for DHA.
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