Some features of the association of β-casein

Rheology and Flocculation of Oil-in-Water Emulsions Made with Mixtures of αs1-Casein + β-Casein

“…So, at room temperature, we can assume that essentially all of the unadsorbed protein present in a ␤-casein-stabilized emulsion is in the form of micelles containing about 40 monomers (25). But, since ␤-casein micelles are apparently completely dissociated below 5°C (26), if their presence is an important factor controlling the state of flocculation of ␤-casein-stabilized emulsions, we might have expected considerable differences in emulsion rheology between 5 and 20°C. However, this is not quite what occurs experimentally (see Fig.…”

The Application of Membrane Separation Technology in the Dairy Industry

“…The temperature in membrane filtration is 45 to 50°C that is beneficial for high flux and growth control of mesophilic bacteria [22]. β-Casein exists in the serum phase that requires low temperature [23,24]. Therefore, new separation techniques are developed such as polyethersulfone (PES) and polyvinylidene fluoride (PVDF) membrane that applied in β-casein enrichment at refrigeration temperatures (<20°C).…”

Rennets: their role in milk coagulation and cheese ripening

“…The strong influence of ionic strength on the hydrolysability of bonds in the C-terminal region of [J-casein presumably reflects the high hydrophobicity of this region. [J-Casein undergoes strong temperature-dependent association (Payens and van Markwijk, 1963). Presumably, the chymosin-susceptible bonds of [J-casein are inaccessible in the associated protein, e.g.…”