Effects of pH on the Structure of beta-Lactoglobulin at Air/Water and Oil/Water Interfaces
The whey protein β-Lactoglobulin (BLG) is one of the most frequently studied biomacromolecules. The strong effects of pH on the interfacial behavior of BLG (and proteins in general) and on the stability of foams and emulsions are well-recognized issues in the literature but still remain not fully understood. Our preliminary work show that variations of the solution pH lead to non-monotonic changes in the dynamical, mechanical and electrical properties of the interfacial layer, which in turn affect foam stability. To deeper understand the unique pH dependent interfacial behavior of proteins, we plan to study the structure of BLG interfacial layers on the molecular scale. This issue can be resolved by using a range of non-invasive techniques among which is the neutron reflectometry (NR). Hence, we propose comparative NR studies of BLG adsorption layers at the water/air interface as related to foam stability. As a second goal in the project, we plan to investigate this effect also at the water/tetradecane interface (as related to emulsion stability) and to make a comparison between the two types of interfaces. Such information is not accessible by any other experimental methods.
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Georgi Gochev; Richard A. Campbell; KAIRALIYEVA Talmira; MILLER Reinhard; SCHNECK Emanuel and Ernesto Scoppola. (2016). Effects of pH on the Structure of beta-Lactoglobulin at Air/Water and Oil/Water Interfaces. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-640
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