The structure and dynamic properties of mixed adsorption and penetration layers of α-dipalmitoylphosphatidylcholine/β-lactoglobulin at water/fluid interfaces

Abstract

The interfacial tensions of mixed α-dipalmitoylphosphatidylcholine (DPPC)/β-lactoglobulin layers at the chloroform/water interface have been measured by the pendent drop and drop volume techniques. In certain intervals, the adsorption kinetics of these mixed layers was strongly influenced by the concentrations of both protein and DPPC. However, at low protein concentration, C β-lactoglobulin=0.1 mg l −1, the adsorption rate of mixed interfacial layers was mainly controlled by the variation of the DPPC concentration. As C β-lactoglobulin was increased to 0.8 mg l −1, the interfacial activity was abruptly increased, and within the concentration range of C DPPC=10 −4–10 −5 mol l −1, the DPPC has very little effect on the whole adsorption process. In this case, the adsorption rate of mixed layers was mainly dominated by the protein adsorption. This phenomenon also happened as the protein concentration was further increased to 3.6 mg l −1. When C DPPC>3 · 10 –5 mol l −1, the adsorption behaviour was very similar to that of the pure DPPC although the protein concentration was changed. The equilibrium interfacial tensions of the mixed layers are dramatically effected by the lipid as compared to the pure protein adsorption at the same concentration. It reveals the estimation of which composition of lipid and protein decreases the interfacial tension. The combination of Brewster angle microscopy (BAM) with a conventional LB trough was applied to investigate the morphology of the mixed DPPC/β-lactoglobulin layers at the air/water interface. The mixed insoluble monolayers were produced by spreading the lipid at the water surface and the protein adsorbed from the aqueous buffer subphase. The BAM images allow to visualise the protein penetration and distribution into the DPPC monolayer on compression of the complex film. It is shown that a homogeneous distribution of β-lactoglobulin in lipid layers preferentially happens in the liquid fluid state of the monolayer while the protein can be squeezed out at higher surface pressures.