Abstract
The structure of casein micelles has been studied by small-angle neutron scattering and static light scattering. Alterations in structure upon variation of pH and scattering contrast, as well as after addition of chymosin, were investigated. The experimental data were analyzed by a model in which the casein micelle consists of spherical submicelles. This model gave good agreement with the data and gave an average micellar radius of about 100–120 nm and a submicellar radius of about 7 nm both with a polydispersity of about 40–50%. The contrast variation indicated that the scattering length density of the submicelles was largest at the center of the submicelles. The submicelles were found to be closely packed, the volume fraction varying slightly with pH. Upon addition of chymosin the submicellar structure remained unchanged within the experimental accuracy.
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Correspondence to: S. Hansen
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Hansen, S., Bauer, R., Bredsted Lomholt, S. et al. Structure of casein micelles studied by small-angle neutron scattering. Eur Biophys J 24, 143–147 (1996). https://doi.org/10.1007/BF00180271
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DOI: https://doi.org/10.1007/BF00180271