RESUMEN
Applying hydrocolloids in the structure of protein emulsion gel can improve its properties. Interaction of whey protein concentrate (WPC) (5%) with xanthan gum (XG) and basil seed gum (BSG) at different concentrations (0.2%, 0.4%, and 0.6%) was investigated to improve mechanical and structural properties of emulsion gel. Results illustrated that gums created a stronger structure around the oil droplets, which confocal images approved it. Also, the particle size decreased and uniformed by cooperating 0.6% gum in comparison with WPC (46.87 µm). The lowest and highest hardness values were observed in emulsion gel formed by WPC (1.27 N) and 0.6BSG: WPC (3.03 N), respectively. Also, the increase of gum concentration had a positive on consistency parameter of texture, so the value was 11.48 N s in WPC emulsion gel and it reached 0.6BSG: WPC (25.71 N s) and 0.6XG: WPC (19.96 N s). Evaluating the stability of the treatments by centrifugation indicated that 0.6BSG: WPC (89.10%) and 0.6XG: WPC (74%) had the highest level of stability. Increasing gum concentration increased the consistency and viscosity. Also, the viscoelastic properties of emulsion gel improved by 0.6% BSG. The elastic modulus of the WPC, 0.6XG: WPC, and 0.6BSG: WPC emulsion gels at the same frequency (1 Hz) was 240.90, 894.59, and 1185.61 Pa, respectively. In general, the interaction of WPC solution with hydrocolloids, especially BSG, is suggested to prepare more stable and elastic emulsion gels.
RESUMEN
The solution properties of amino acids determine the folding, aggregation, and liquid-liquid phase separation (LLPS) behaviors of proteins. Various indices of amino acids, such as solubility, hydropathy, and conformational parameter, describe the behaviors of protein folding and solubility both in vitro and in vivo. However, understanding the propensity of LLPS and aggregation is difficult due to the multiple interactions among different amino acids. Here, the solubilities of aromatic amino acids (SAs) were investigated in solution containing 20 types of amino acids as amino acid solvents. The parameters of SAs in amino acid solvents (PSASs) were varied and dependent on the type of the solvent. Specifically, Tyr and Trp had the highest positive values while Glu and Asp had the lowest. The PSAS values represent soluble and insoluble interactions, which collectively are the driving force underlying the formation of droplets and aggregates. Interestingly, the PSAS of a soluble solvent reflected the affinity between amino acids and aromatic rings, while that of an insoluble solvent reflected the affinity between amino acids and water. These findings suggest that the PSAS can distinguish amino acids that contribute to droplet and aggregate formation, and provide a deeper understanding of LLPS and aggregation of proteins.
