Changes in particle size, calcium and phosphate solubilization, and microstructure of rehydrated milk protein concentrates, prepared from partially acidified milk

The present work studied the rehydration properties of milk protein concentrates (MPCs), prepared using ultrafiltration (UF) and diafiltration (DF). Milk was acidified to pH 6 with glucono-delta-lactone (GDL) prior to UF to alter the mineral composition of the final concentrates. The particle size distribution and the microstructure of the casein micelles in reconstituted MPCs as well as the partitioning of calcium, phosphate, and proteins between the colloidal and soluble phases were investigated. Reconstituted samples analyzed by electron microscopy showed that, even in partially dissolved particles, the particle surface was porous and similar to its inner portion and had no distinct skin layer. Partial acidification of milk did not have any significant effects on the microstructure; however, it significantly increased the average diameter of the casein micelles for both UF and DF samples and decreased the concentration of total calcium and phosphate. Sodium dodecyl sulfate (SDS)-PAGE analysis of the centrifugal supernatants of reconstituted MPC demonstrated that the amount of soluble caseins present in milk concentrates dramatically increased with acidification, and it further increased after restoring the mineral composition of the serum phase through dialysis against milk. This work contributes to a better understanding of how processing conditions, particularly partial acidification of milk prior to concentration, can alter the composition and physical properties of the caseins and the soluble phase of MPC after rehydration. Such alterations can significantly impact the technological properties of the reconstituted MPC.