Speakers
Invited Speaker
First results in heat induced liquid-liquid phase separation studied by x-ray scattering
Proteins in general and egg yolk specifically form complex 3D network structures during gelation. These protein gels are generally composed of a protein-enriched network structure embedded in a solvent rich phase, which gives rise to the coexistence of
elasticity and fluidity. The elastic modulus of the resultant gel depends sensitively on both the strength and nature of the inter-particle interaction and on the topology and connectedness of the gel. The mechanical, interfacial, and transport properties are crucial for various applications in bio-nanotechnology and the food industry. Typically gelation is studied by synchrotron radiation techniques such as small-angle x-ray scattering or in-line holography. Using the latter we have found evidence for the formation of polyeder-shaped lipid globule interfaces as well as effects of non-linear viscoelasticity. More crucially, we have studied the evolution of protein network sizes during heat treatment, where we will present first evidence that this effect can also be studied with laboratory-based x-ray scattering.
