Time-dependent aggregation of casein micelle concentrates

This research focused on understanding physical and chemical changes occurring to concentrated milk protein suspensions as a function of time. Skim (untreated heat treated at 90°C for 10 min) was 6 times the original volume using osmotic stressing, noninvasive concentration method, maintaining serum composition close possible that native milk. A protease inhibitor cocktail, with broad specificity inhibition serine, cysteine, aspartic proteases, aminopeptidases, added in selected samples. Within 9 d storage 4°C, apparent viscosity increased markedly both unheated heated milk, but not those presence inhibitors. However, only showed significant increase diameter casein micelles. Matrix-assisted laser desorption-ionization time-of-flight mass spectrometry measurements indicated significantly lower extent proteolysis than The microstructure aggregates observed field emission scanning electron microscopy, samples clearly aggregation micelles In samples, instead triggered by heat-induced protein-protein interactions.