Study on the binding behavior and functional properties of soybean protein isolate and β-carotene.

ABSTRACT: This study focused on the non-covalent interaction between soybean protein isolate (SPI) and β-carotene (BC). The conformational changes of SPI with β-carotene in varying proportions (BC/SPI: 2%, 4%, 6%, 8%, and 10%) were investigated by multi-spectroscopy and molecular docking. Results showed that the quenching mode is static quenching and binding affinity increased with temperature. The stoichiometry was 1:1, indicating there was only one binding site in SPI. The binding was based on entropy and primarily driven by hydrophobic interactions and its binding constant was in the order of 10⁴ L⋅mol^-1. The addition of the β-carotene affected the secondary structure of SPI resulting in an increase in α-Helix and a decrease in random coil and β-turn content, indicating prot

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC9493324 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature