Deciphering β-Lactoglobulin Interactions at an Oil-Water Interface: A Molecular Dynamics Study

Area of Science:

• Biophysics
• Food Science
• Materials Science

Background:

• Protein adsorption at liquid-liquid interfaces is vital for biological processes and functional foods.
• Understanding the molecular-level adsorption mechanism remains challenging due to experimental limitations.

Purpose of the Study:

• To elucidate the approach and adsorption mechanism of beta-lactoglobulin (β-LG) at a decane-water interface.
• To characterize the molecular dynamics of protein adsorption at oil/water interfaces.

Main Methods:

• Atomistic molecular dynamics simulations were employed.
• Multiple independent simulations were conducted using varied initial orientations of β-LG.

Main Results:

• The rate of β-LG approach to the interface is orientation-independent and stochastic.
• Adsorption is driven by structural rearrangements that maintain secondary structure while exposing hydrophobic residues.
• Final adsorbed orientations and initial contact points are consistent across simulations.

Conclusions:

• The study provides a detailed molecular-level understanding of β-LG adsorption at oil/water interfaces.
• Findings can inform the design of advanced encapsulation and delivery systems in food and pharmaceutical industries.