An in-depth, critical review of model-dependent fitting of small-angle X-ray scattering (SAXS) data of bovine skim milk has led us to develop a new mathematical model for interpreting these data. Calcium-edge resonant soft X-ray scattering data provides unequivocal evidence as to the shape and location of the scattering due to colloidal calcium phosphate, which is manifested as a correlation peak centred at q = 0.035 Å(-1). In SAXS data this feature is seldom seen, although most literature studies attribute another feature centred at q = 0.08-0.1 Å(-1) to CCP. This work shows that the major SAXS features are due to protein arrangements: the casein micelle itself; internal regions approximately 20 nm in size, separated by water channels; and protein structures which are inhomogeneous on a 1-3 nm length scale. The assignment of these features is consistent with their behaviour under various conditions, including hydration time after reconstitution, addition of EDTA (a Ca-chelating agent), addition of urea, and reduction of pH.
The interpretation of milk X-ray and neutron scattering data in relation to the internal structure of the casein micelle is an ongoing debate. We performed resonant X-ray scattering measurements on liquid milk and conclusively identified key scattering features, namely those corresponding to the size of and the distance between colloidal calcium phosphate particles. An X-ray scattering feature commonly assigned to the particle size is instead due to protein inhomogeneities.
The casein micelle is a flexible construct, with its key structural components being casein proteins and colloidal calcium phosphate nanoclusters. According to literature, milk from different species exhibits differences in composition and physicochemical properties. X-ray scattering techniques were used to investigate and compare the nanoscale structure of casein micelles present in cow, goat and sheep milk. Although there were differences in the size and density of larger scale protein structures, at an atomic level the protein structures were similar. There were also strong similarities in the structure of the calcium-containing nanoclusters, namely that they had similar sizes and separations within the casein micelle for all three species.
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