The characterization and stability of the soy protein isolate/1-Octacosanol nanocomplex

The complexation of nanoparticles in extreme alkali treated (pH 10.0, 11.0 and 12.0) soy protein isolate (SPI) with 1-Octacosanol (1-Octa) was investigated. The nanoparticles were compared in complexing with the 1-Octa concerning their characteristics, along with the changes in secondary structure and stability of 1-Octa upon complexation. The nanoparticles did not display obvious changes in size and morphology upon complexation with 1-Octa, except the surface hydrophobicity. The encapsulation efficiency (EE) and loading amount (LA) of the SPI-Octa were first increased and then decreased with an enhanced pH value. The treatment conditions modified some secondary structures, causing greater protein unfolding to expose more hydrophobic clusters. Additionally, the nanocomplex had higher thermal and saline ion stability, the majority of the nanocomplexes were evenly dispersed in the aqueous phase.