Reformation of casein particles from alkaline-disrupted casein micelles.

In this study, the properties of casein particles reformed from alkaline disrupted casein micelles were studied. For this purpose, micelles were disrupted completely by increasing milk pH to 10.0, and subsequently reformed by decreasing milk pH to 6.

Biocompatible micro-gel particles from cross-linked casein micelles.

The stability of internally cross-linked casein micelles against disruption by urea (which disrupts hydrogen bonds and hydrophobic interactions) and trisodium citrate (which sequesters micellar calcium phosphate) was investigated. Addition of urea (0-6 mol L-1) and/or citrate (0-50 mmol L-1) progressively reduced the turbidity of a suspension of casein micelles cross-linked by transglutaminase and increased particle size (determined by dynamic and static light scattering and small-angle neutron scattering), which was attributed to swelling of the micelles. Furthermore, model calculations, assuming a completely stable casein network, were performed to describe the decreases in turbidity on addition of urea and citrate.

Solvent-mediated disruption of bovine casein micelles at alkaline pH.

The disruption of casein micelles at alkaline pH was investigated using turbidity measurements. The rate and extent of disruption of casein micelles at alkaline pH (8.0-11.