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Updated: Jun 5, 2026

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
Published on: April 14, 2015
Characterization of high-milk-protein powders upon rehydration under various salt concentrations
R Hussain1, C Gaiani, L Aberkane
1LIBio, Nancy Université, Laboratoire d'Ingénierie des Biomolécules, 54505 Vandoeuvre Les Nancy Cedex, France.
Abstract:
Rehydration of native micellar casein and native whey isolate protein powders was followed in different ionic environments. Solutions of NaCl and CaCl2 in the concentration range of 0 to 12% (wt%) were used as rehydration media. The rehydration profiles obtained were interpreted in terms of wetting, swelling, and dispersion stages by using a turbidity method. Two behaviors were observed depending on the salt concentration. For native micellar casein powder, a significant change was observed between 3 and 6% NaCl and between 0.75 and 1.5% CaCl2. The first behavior (low salt concentration) presents a typical rehydration profile: quick wetting, swelling, and long dispersion stage. The dispersion stage of the second behavior (high salt concentration) was significantly shortened, indicating a strong modification of the protein backbone. The rehydration of whey protein powder was less influenced by salts. At low salt concentrations, a typical profile for whey powders was observed: wetting with lump formation and no swelling followed by a quick dispersion. At high CaCl2 concentrations, no turbidity stabilization was observed, indicating a possible protein unfolding and denaturation. Additionally, the changes in secondary structures of the 2 proteins upon salt increase were followed by Fourier transform infrared spectroscopy and confirmed the different profiles observed.
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