Abstract
High protein milk ingredients, such as micellar casein powder (MCP), exhibit poor solubility upon reconstitution in water, particularly after long-time storage. In this study, ultrasonication (20 kHz, power density of 0.75 W/ml) was used to improve the solubility of aged MCP powders. For all the MCP powders (concentration varying from 0.5 to 5%, and storage of MCP at 50 °C for up to 10 days) it was found that short time ultrasonication (2.5 min) reduced the size of the protein particles from >30 μm to ∼0.1 μm, as measured by light scattering. This resulted in an improvement of solubility (>95%) for all the MCP powders. Cryo-electron microscopy and small x-ray angle scattering showed that the MCP powders dissolved into particles with morphologies and internal structure similar to native casein micelles in bovine milk. SDS-PAGE and RP-HLPC showed that ultrasonication did not affect the molecular weight of the individual casein molecules. Compared to overhead stirring using a 4-blade stirrer, ultrasonication required less than 10 times the drawn electrical energy density to achieve a particle size 10 times smaller.
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