Self-assembly of β-lactoglobulin and egg white lysozyme as a potential carrier for nutraceuticals

Abstract

Self-assembly structures of β-lactoglobulin (βlg) and egg protein lysozyme (Lyso) were developed, using electrostatic interactions between the two oppositely charged proteins. Different βlg/Lyso concentration ratios were essayed at pH 6.8 to select the optimal ratio for the proteins co-precipitation, which behaviour was then studied at varying pH values. Optimal βlg/Lyso concentration ratio, prepared at pH 7.5, was selected for protein co-precipitation. As a result, a structure with a mean diameter of 7.1±2.5 μm was formed, as indicated by static light scattering. Furthermore, the SEM images showed that βlg and Lyso self-assembled to form a microsphere. Vitamin D3, used as a model nutraceutical, was successfully entrapped in the βlg/Lyso microspheres with an encapsulation efficiency of 90.8±4.8%. Therefore, the βlg/Lyso microspheres can serve as a potential food-grade vehicle for bioactives in the formulation of food products and pharmaceuticals.

Keywords: Bioactives; Delivery vehicle; Lysozyme; Proteins; Self-assembly; β-Lactoglobulin.