Abstract
The structural changes of skim milk caused by sonication were evaluated by particle size, zeta-potential, turbidity, scanning electron microscopy, Fourier transform infrared spectroscopy, and intrinsic and 8-anilino-1-naphthalenesulfonic acid sodium salt fluorescence properties. The results showed that the particle size and zeta-potential of skim milk remained constant with 1 min ultrasonication, and increased significantly when the duration of sonication was extended to 3 min. With 3-10 min ultrasonic treatment, the diameter and net charge of particles in skim milk changed scarcely. According to the topography, the integrity of casein micelles was not damaged by 30 min sonication, but the turbidity decreased sharply with sonication above 5 min. The secondary structure of protein in skim milk changed after 1 min sonication, shown by a significant increase of α-helix content and decrease in the irregularity of β-sheet. The intrinsic fluorescence intensity of skim milk with 1 min sonication increased dramatically with a shift in the maximum emission wavelength. The fluorescence properties revealed that the spatial structure of protein in skim milk changed by sonication.
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