Spontaneous aggregation of bovine milk casein micelles: Ultra-small angle x-ray scattering and mathematical modeling

Abstract

We have used Ultra Small Angle X-ray Scattering (USAXS) and mathematical models to study seemingly-spontaneous aggregation structures in two pasteurized bovine milks. Although extensive studies of casein micelles and their aggregation have been carried out, few have been done to numerically characterize submicron structures to micron-scale structures. We measured the USAXS intensity, I(q), as a function of the scattering vector magnitude, q, for commercial pasteurized skim milk and nonhomogenized whole milk at two temperatures, 7 °C and 45 °C. We observed broad peaks, reported previously to be related to casein micelles, centered at q ≈ 2 × 10−2 Å−1 and at q ≈ 9 × 10−2 Å−1. At lower q values, log I(q) displayed a behavior characteristic of aggregation manifested for a slope in the region 3–7 × 10−4 Å−1 < q < 4 × 10−3 Å−1. This behavior appeared in the absence of (a) chymosin, (b) any change in pH or CaCl2 concentration, and (c) temperature changes. We introduced a model of milk and used computer simulations to investigate consequences of casein micelles possessing surface areas lacking the water-soluble components of κ-casein proteins. These components exist to provide stability against aggregation to the casein micelles. We propose that bovine casein micelles spontaneously formed 1-dimensional aggregates.