LAUSR

This study sought to understand how the features of proteins impact the properties of nanoparticles assembled using the pH-shifting approach and the mechanism behind. Four legume protein isolates from faba bean, mung bean, soy, and pea were fractionated into natural aqueous-soluble (Sup) and aqueous-insoluble (Sed) fractions, which were proved to serve as shell and core, respectively, for the pH-driven-assembled nanoparticles. Using zein instead of Sed fractions as the core improved size uniformity, and particle size can be precisely controlled by adjusting core/shell ratios. Using the proteomic technique and silico characterization, the features of identified proteins indicated that hydrophobicity rather than molecular weight, surface charge, etc., mainly determined particle size. With molecular docking, structural analysis, and dissociation tests, the assembly of zein/Sup-based nanoparticles was dominantly driven by hydrophobic interactions. This study provides constructive information on the correlation between protein features and the properties of pH-driven-assembled nanoparticles, achieving a precise control of particle size.