Amphiphilic properties enable proteins like beta-lactoglobulin to stabilize oil/water-interfaces and provide stability in food-related emulsions. During emulsification, the protein undergoes three stages: (I) migration through bulk phase, (II) adsorption, and (III) interfacial rearrangement at the oil/water-interface the kinetics of which require further research. Therefore, the aim of our study was the analytical and computational investigation of stage (I) and (II) as a function of the interfacial preoccupation, conformational state and charge of beta-lactoglobulin. For this purpose, the adsorption of beta-lactoglobulin (at pH 7, pH 7 containing 0.1 M NaCl, and pH 9) at increasingly preoccupied oil/water-interfaces has been compared through measuring interfacial tension and zeta-potential and through running molecular dynamics simulations. With increasing interfacial preoccupation, (I) the migration via lag time increased and (II) the adsorption rate decreased. The (II) adsorption rate was highest for beta-lactoglobulin containing NaCl, due to dense packing and electrostatic screening. B-lactoglobulin at pH7 reached a lower adsorption rate than the more negatively charged beta-lactoglobulin at pH 9, due to exposure of hydrophobic regions that had a greater effect on adsorption rates than electrostatic repulsion. Our research contributes to a profound understanding of the interfacial stabilization mechanism of proteins at oil/water-interfaces, necessary to characterise and control emulsification processes. (C) 2018 Elsevier Inc. All rights reserved.