Abstract

Native casein micelles were treated (incubated) with vitamin D2 at different hydrostatical pressures (0.1, 200, 400, and 600MPa) and temperatures (10-50°C) in order to load the vitamin. Pressure induced the release of αs-, β- and κ-casein and calcium from the micelle into the soluble phase. During the pressure stable reassembled micelles were created due to a structural rearrangement of hydrophobic interactions between the hydrophobic domains of the caseins and vitamin D2. Treatment at 600MPa and 50°C increased the loading of vitamin D2 per casein from 2.2±0.2μg/mg (native sample) to 10.4±0.2μg/mg. The reassembled micelles presented an average hydrodynamic diameter of 272±10nm and contained 8.1, 10.3 and 0.8mg of α-, β- and κ-casein, respectively, per 100mg casein.

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