Immobilization and interfacial activation of lipase at liquid and solid interfaces.

This study investigates the adsorption behaviour of lipase at silica/water and oil/water interfaces by means of molecular dynamics simulations. The findings reveal distinct adsorption orientations and structural differences that can be related to different enzymatic activities and selectivities. At the silica/water interface, lipase adsorbs with the LID region facing the solvent, in a configuration that is not fully open, but still grants access to its catalytic triad, as shown by tunnel calculations.

Cysteines in β-lactoglobulin affects its interfacial adsorption and protein film stabilization.

Hypothesis: Disulfide bonds in proteins are strong chemical bonds forming the secondary and tertiary structure like in the dairy protein β-lactoglobulin. We hypothesize that the partial or complete removal of disulfide bonds affects the structural rearrangement of proteins caused by intra- and intermolecular interactions that in turn define the interfacial activity of proteins at oil/water interfaces. The experimental and numerical investigations contribute to the mechanistic understanding of the structure-function relationship, especially for the interfacial adsorption behavior of proteins.

Characterization of β-lactoglobulin adsorption on silica membrane pore surfaces and its impact on membrane emulsification processes.

Protein adsorption plays a key role in membrane fouling in liquid processing, but the specific underlying molecular mechanisms of β-lactoglobulin adsorption on ceramic silica surfaces in premix membrane emulsification have not been investigated yet. In this study, we aimed to elucidate the β-lactoglobulin adsorption and its effect on the premix membrane emulsification of β-lactoglobulin-stabilized oil-in-water emulsions. In particular, the conformation, molecular interactions, layer thickness, surface energy of the adsorbed β-lactoglobulin and resulting droplet size distribution are investigated in relation to the solvent properties (aggregation state of β-lactoglobulin) and the treatment of the silica surface (hydrophilization).

Structure and adsorption behavior of high hydrostatic pressure-treated β-lactoglobulin.

Hypothesis: High hydrostatic pressure treatment causes structural changes in interfacial-active β-lactoglobulin (β-lg). We hypothesized that the pressure-induced structural changes affect the intra- and intermolecular interactions which determine the interfacial activity of β-lg. The conducted experimental and numerical investigations could contribute to the mechanistic understanding of the adsorption behavior of proteins in food-related emulsions.