Exploring the relationship between protein secondary structures, temperature-dependent viscosities, and technological treatments in egg yolk and LDL by FTIR and rheology

Egg yolk and its main component, low-density lipoproteins (LDL), were consecutively pasteurised, optimally freeze-dried, and dispersed in various NaCl solutions (0–10%). Heat-induced changes in the protein secondary structures which accompanied viscosity-increasing aggregation processes were monitored using Fourier transform infrared spectroscopy (FTIR) to determine the intensities of intermolecular β-sheets (1622 cm−1) and results were compared with the temperature-dependent viscosities. Considerable changes in secondary structures observed after reconstitution of freeze-dried LDL had no detectable effect on the characteristic heat-induced viscosity curves but suggest that LDL plays a particular role in the unwanted gel formation of egg yolk after conventional freezing. For all egg yolk samples and all NaCl-containing LDL samples, the sigmoidal changes in the absorbance units vs. temperature curves corresponded with the first increase in heat-induced viscosity. Both analytical methods showed that the presence of ionic strength caused a shift in curve progressions towards higher temperatures, indicating increased thermal stability.