Abstract: Dispersions of casein micelles (CM) were studied at a
constant protein concentration of 5 wt % in high NaCl environment
ranging from 0% to 12% by Dynamic light scattering (DLS) and
Fourier Transform Infrared (FTIR). The rehydration profiles obtained
were interpreted in term of wetting, swelling and dispersion stages by
using a turbidity method. Two behaviours were observed depending
on the salt concentration. The first behaviour (low salt concentration)
presents a typical rehydration profile with a significant change
between 3 and 6% NaCl indicating quick wetting, swelling and long
dispersion stage. On the opposite, the dispersion stage of the second
behaviour (high salt concentration) was significantly shortened
indicating a strong modification of the protein backbone. A salt
increase result to a destabilization of the micelle and the formation of
mini-micelles more or less aggregated indicating an average micelles
size ranging from 100 to 200 nm. For the first time, the estimations
of secondary structural elements (irregular, ß-sheet, α-helix and turn)
by the Amide III assignments were correlated with results from
Amide I.