Isolating the interface of an emulsion using X-ray scattering and tensiometry to understand protein-modulated alkylglyceride crystallisation

Abstract

HypothesisDairy proteins and mono- and diglycerides (MDG) are often used in unison to tailor the properties of dairy-based emulsions. However, there are significant gaps in our understanding of how proteins affect lipid crystallisation at the oil–water interface. We have used a unique combination of interfacially-sensitive techniques to elucidate the impact of dairy proteins on interfacial MDG crystal formation. ExperimentsThe formation temperature of interfacial MDG crystals was assessed through interfacial tension studies via drop shape analysis. Small and Wide-Angle X-ray Scattering measurements were performed on isolated oil–water interfaces, allowing for in-situ interrogation of MDG crystal structure and concentration at and near the interface. FindingsDairy proteins are seen to reduce the temperature at which MDG crystals form at the oil–water interface. The displacement of proteins upon interfacial crystal formation was also clearly observed in interfacial tension measurements. For the first time, lipid crystals formed at the oil–water interface have been characterised using X-ray scattering. All scattering studies showed no change to the MDG crystal structures at the oil–water interface in the presence of adsorbed proteins. The results demonstrate that informed selection of emulsifier components is critical to controlling interfacial crystallisation with concomitant impact on emulsion stability.