Casein Micelles and Micelles of ϰ- and β-Casein

The influence of milk composition on the growth of Bacillus stearothermophilus

“…However even mild heat treatments (up 60°C) can affect the hydrophobicities of some proteins, such as b-casein and blactoglobulin causing fouling (de Wit & Klarenbeek, 1984;Payens & Vreeman, 1982) and as Brandts (1969) mentioned that hydrophobic effects are important in maintaining protein stability in milk processing. In this study, protein aggregation occurred at 55°C in the samples both with and without the presence of B. stearothermophilus.…”

Contribution of Protein Flexibility to the Foaming Properties of Casein

“…Our study suggests flexibility plays an essential role in the surface properties of food proteins. The p monomer, which is the most flexible monomer (Payens, 1982), is also the most efficient in decreasing surface tension and in yielding foams . Moreover, comparisons between native and denatured globular proteins (Song and Damodaran, 1987) lead to the same conclusion that the higher flexibility of the denatured protein promotes surface properties, except when precipitation occurs.…”

“…Casein presents a strong tendency to associate, leading either to consecutive oligomers (a) or to micelle formation when the protein concentration is higher than the critical micellar concentration (P,K : c = 0.5g. L-l-ionic strength = 0.2-21°C) (Payens, 1982). Colas et al (1988) showed that the voluminosity of casein (calculated from viscosity measurements) increased with the covalent binding of galactose ( Table 2).…”

Casein structures in the context of unfolded proteins

“…In the past, the self-association of individual caseins and the association of casein mixtures in the absence of calcium ions or calcium phosphate have been likened to that of detergent molecules in which the hydrophobic effect (Cramer & Truhlar, 1992;Kauzmann, 1959) is assumed to provide the driving force (Horne, Lucey, & Choi, 2007;Mikheeva, Grinberg, Grinberg, Khokhlov, & de Kruif, 2003;Payens & Vreeman, 1982). Comparison with similar unfolded proteins suggests that an alternative driving force is more likely which involves main-chain-to-main-chain interactions of low sequence specificity rather than the side-chain interactions of the hydrophobic effect.…”