Surface rheological properties of liquid–liquid interfaces stabilized by protein fibrillar aggregates and protein–polysaccharide complexes

Abstract

In this study we have investigated the surface rheological properties of oil–water interfaces stabilized by fibrils from lysozyme (long and semi-flexible and short and rigid ones), fibrils from ovalbumin (short and semi-flexible), lysozyme–pectin complexes, or ovalbumin–pectin complexes. We have compared these properties with those of interfaces stabilized by the native proteins. The surface dilatational and surface shear moduli were determined using an automated drop tensiometer and a stress controlled rheometer with biconical disk geometry. Results show that interfaces stabilized by complexes of these proteins with high-methoxyl pectin have higher surface shear and dilatational moduli than interfaces stabilized by the native proteins only. The interfaces stabilized by ovalbumin and lysozyme complexes have comparable shear and dilatational moduli though ovalbumin–pectin complexes are twice as large in radius as lysozyme–pectin complexes. Under most of the experimental conditions, interfaces stabilized by fibrils have the highest surface rheological moduli. The difference between long semi-flexible lysozyme fibrils or short rigid lysozyme fibrils is not pronounced in interfacial dilation rheology but significant in interfacial shear rheology. The complex surface shear moduli of interfaces stabilized by long semi-flexible fibrils are about 10 times higher than those of interfaces stabilized by short rigid fibrils, over a range of bulk concentrations. Interfaces stabilized by short and more flexible ovalbumin fibrils have a significantly higher surface shear modulus than those stabilized by longer and more rigid lysozyme fibrils. This study has shown that the use of such supra-molecular structural building blocks creates a wider range of microstructural features of the interface, with higher surface shear and dilatational moduli and a more complex dependence on strain.