Computational modeling of an egg yolk protein behavior at oil/water interface via atomistic and mesoscopic approaches.

Many food emulsions are stabilized by functional egg yolk biomolecules, which act as surfactants at the oil/water interface. Experimental studies on egg yolk emulsifying properties have been hindered due to the difficulty in isolating individual chemical species. Our work focuses on the molecular modeling of one of the most surface-active proteins from the egg yolk low-density lipoproteins, the so-called Apovitellenin I. We used two approaches to study several aspects of protein adsorption at the oil/water interface: Dissipative Particle Dynamics [1] and atomistic metadynamics simulations [2]. The goal is to outline the protein behavior as a surfactant, extracting the interfacial tension at increasing surface concentration. Results from both methods are in agreement with those of a similar well-known protein, the β-casein. A thermodynamic model of protein adsorption is used together with simulations to predict the surface state equation and adsorption isotherm of Apovitellenin I that are not experimentally measurable. The main finding is to show how different computational methods can be linked together to obtain a deeper understanding of this egg yolk protein behavior.