The effect of CaCl2 on water migration, rheological properties, aggregation behavior and protein structure in rapidly salted separated egg yolk plasma and granules.

This research investigated the effects of CaCl2 on the aggregation behavior and protein structure of egg yolk plasma and granules after fast salting. The addition of CaCl2 to the salt solution decreased T23, D [4,3] and the absolute value of the zeta potential by 6.71%, 3.66%, and 3.15%, respectively, while increasing T22 by 15.85% in egg yolk plasma. Moreover, adding CaCl2 also increased the apparent viscosity and G' value of egg yolk plasma. On the other hand, the addition of CaCl2 decreased the T22, T23, D [4,3], and absolute value of the zeta potential of egg yolk granules by 56.53%, 6.71%, 6.02%, and 34.27%, respectively. Furthermore, the addition of CaCl2 increased the number of ß-turns by 51.22%, whereas it decreased the number of ß-sheets by 26.55% in egg yolk plasma protein. The α-helices, ß-turns, and ß-sheets of egg yolk granule protein decreased by 6.58%, 3.58%, and 6.96%, respectively. Additionally, the addition of CaCl2 can increase the degree of λmax redshift in egg yolk plasma and decrease the degree of λmax redshift in egg yolk granules. Overall, the addition of CaCl2 can change the aggregation mode of proteins in egg yolk plasma and granules, improving the quality of salted egg yolk products.

Effects of CaCl2 on the structure of high-density lipoprotein and low-density lipoprotein isolated from rapidly salted separated egg yolk.

According to previous research, adding CaCl2 to the salting solution improves the quality of salted separated egg yolk. To further understand the improvement mechanism of CaCl2, this paper investigated the effect of CaCl2 on the structure of high-density lipoprotein (HDL) and low-density lipoprotein (LDL) during the salting process. The results indicated that the addition of CaCl2 can affect the composition of HDL and LDL apolipoproteins, improving the orderliness of the HDL structure and the looseness of the LDL structure. It was discovered by atomic force microscopy (AFM) that adding CaCl2 to the salting solution can weaken the aggregation behavior of HDL. Simultaneously, the addition of CaCl2 decreased the relative content of intermolecular ß-sheets in the secondary structure of HDL and LDL, influenced their tertiary conformation, and prevented HDL and LDL from participating in the formation of a three-dimensional gel structure by influencing their hydrogen bonds and hydrophobic interactions.

Effects of CaCl2 on the rheology, microstructure and protein structures of rapidly salted separated egg yolk.

Bivalent or trivalent metal salts can enhance the oil output and sandiness of salted eggs. We added CaCl2 to the salting solution to improve the quality of rapidly salted separated egg yolk and investigated its effect on rheological, microstructure, and protein structure. According to the findings, adding CaCl2 to the salting solution can promote the precipitation of egg yolk water, increase its viscosity, induce protein aggregation, and increase the denaturation temperature of the protein. Scanning electron microscopy (SEM) and confocal laser scanning microscopy (CLSM) revealed that the inner boundary of egg yolk salted with CaCl2 was clearer and that the number and size of salted egg yolk lipoprotein aggregates were larger than those of egg yolk salted without CaCl2. Analysis using Fourier transform infrared spectroscopy (FTIR) demonstrated that CaCl2 caused the interconversion of the secondary-level structure. CaCl2 can have an impact on the microenvironment of amino acid residues, according to the results of 3D fluorescence and UV absorption spectra. Therefore, adding CaCl2 can accelerate the loss of water and change the structure of lipoprotein in egg yolk, which improves the sandiness and oil yield of salted separated egg yolk.

Supplemental methionine selenium effects on egg yolk physicochemical, functional, and protein structure during storage.

To clarify the effect of the addition of methionine selenium on the physicochemical, functional, and protein structural properties of egg yolk during storage. We analyzed the changes in the main indicators of egg yolks stored at 4°C and 25°C for 28 days. The results showed that the increase in water content and pH, and the decrease in absolute zeta potential and apparent viscosity of the selenium-rich egg yolks (Se-group) during storage were smaller than those of the control group egg yolks (C-group). In addition, the antioxidant capacity and emulsifying ability of the Se-group during storage were better than those of the C-group. Simultaneously, the hardness and chewiness of the Se-group gel during storage were lower than those of the C-group. The protein structure results showed that selenium rich treatment did not affect the secondary structure of egg yolk protein during storage but could improve the fluorescence intensity of the egg yolk protein. Therefore, the addition of methionine selenium can reduce the degree of deterioration in the physicochemical properties of egg yolk during storage and extend its shelf life.

Effects of CaCl2 on salting kinetics, water migration, aggregation behavior and protein structure in rapidly salted separated egg yolks.

Salted egg yolks are valued by consumers for their delicious taste good processing characteristics. To improve the quality of rapidly salted separated egg yolks, we compared changes in the salting kinetics, textural properties, water migration, protein aggregation and structure of salted egg yolks in the presence or absence of CaCl2 for 24 h. CaCl2 increased the mass transfer driving force and diffusion coefficient during the salting process; as a result, the salted egg yolks exhibited increased hardness and decreased springiness and cohesiveness. Through low field nuclear magnetic resonance (LF NMR), it was confirmed that CaCl2 promoted the precipitation of lipids and the dehydration of egg yolk. Furthermore, CaCl2 promoted the bulk aggregation of proteins. The analyses of protein structures showed that the contents of ß-sheets and irregular curls in CaCl2-salted egg yolk protein increased, while the contents of α-helices and ß-turns decreased. CaCl2 affected the microenvironment of tryptophan residues and embedded these residues, enhancing protein aggregation. Based on the comprehensive information obtained in this study, adding CaCl2 to the salting solution improved the degree of protein polymerization in egg yolk; thus, this method might be used to improve the quality of egg yolks separated by salt.