Impact of Phenolic Acid Derivatives on ?-Lactoglobulin Stabilized Oil-Water-Interfaces

Abstract The physical stability of protein-based emulsions depends on intra- and intermolecular interactions the interfacial protein-film. As studied in aqueous systems before, phenolic acid derivatives (PADs) non-covalently or covalently crosslink proteins depending pH-value thus, may impact protein-films. Whether these occur same manner at interface as water how they vary properties protein-film has not been clarified. present study aimed to investigate viscoelasticity emulsion-stability after (pH 6.0) 9.0) crosslinking PAD-structure. For this purpose, we an ?-lactoglobulin film with dilatational rheology PADs, varying number ?-electrons polar substituents. Then, analyzed by visual evaluation particle size distribution. results indicate that PADs a high (rosmarinic chicoric acid) weaken due competing phenol-protein protein-protein interactions. This is reflected decrease elasticity. additional substituent (verbascoside cynarine) seem further protein film, since affinity increases, preferentially adsorb sterically hinder In pH 6.0 thus low electrostatic repulsion, promote bridging-flocculation. Due higher repulsion 9.0, are hindered form bridges, even though polymeric. Hence, our research enables control Graphical abstract