Self-assembly Soy Protein Gel Based on Thymol Nanocomplexation and Its Molecular Mechanism
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Abstract:
In order to reveal the approach and mechanism of soy protein self-assembly gel based on thymol nanocomplexation, the effects of protein concentration, thymol addition concentration, as well as initial and final pH value of the reaction on soy protein-thymol interaction and gel formation were investigated in the present study. The results showed that all the factors synergistically regulated the formation of soy protein-thymol nanocomplex gel. A higher thymol loading amount facilitated the formation of soy protein gel with a lower critical protein concentration (75 mg/mL). Additionally, the pH value adjusted to neutral at the end of complexation was necessary for soy protein-thymol nanocomplex gel formation. Considering that the average particle size and light scattering intensity of particles, as well as Th T fluorescence intensity of soy protein were increased by 26.70%, 154.67% and 93.78%, respectively at a pH of 7.0, the soy protein gel formation could have been largely associated with the fibrous aggregation that occurred in the soy protein after thymol nanocomplexation. The solubility of prepared gel in urea and DTT was increased, thus it is assumed that the intermolecular interaction forces that maintain the soy protein gel network were mainly hydrogen bonding, hydrophobic interactions, and disulfide bonding. Thus, the findings are important for developing cold-set soy protein gels and utilizing thymol.
