Effect of pH on the internal structure of protein stabilized foams studied by SANS
Foams stabilized by proteins will be investigated by small angle neutron scattering (SANS) in order to elucidate the internal foam structure. Therefore, foams stabilized by three different proteins Beta Lactoglobulin, Casein and Bovine Serum Albumin at varying pH values will be investigated. From studies at single foam films, it is known that the different types of proteins show different tendencies for aggregation and network formation which is affected by the pH value. We want to know how the aggregation/networks affect the inner foam structure and the foam stability. In addition, structures with different liquid volume fractions in the foam will be studied. In this context the question of thinning of the foam films during foam drainage will be addressed. This experiment will be realized by probing a steady state foam at different heights in our home-built sample environment, which was designed to study macroscopic foams by SANS.
The data is currently only available to download if you are a member of the proposal team.
The recommended format for citing this dataset in a research publication is in the following format:
GRAEFF Kevin; Leonardo Chiappisi; Olaf Soltwedel; VON KLITZING Regine and ZIMMER Joanne. (2023). Effect of pH on the internal structure of protein stabilized foams studied by SANS. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-10-1787
This data is not yet public
This data is not yet public
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