Soy protein isolate-catechin complexes conjugated by pre-heating treatment for enhancing emulsifying properties: Molecular structures and binding mechanisms.

This study aimed to investigate the impact of different pre-heating temperatures (ranging from 40 °C to 80 °C) on the interactions between soy protein isolate (SPI) and catechin to effectively control catechin encapsulation efficiency and optimize the emulsifying properties of soy protein isolate. Results showed that optimal heat treatment at 70 °C improved catechin encapsulation efficiency up to 93.71 ±â€¯0.14 %, along with the highest solubility, enhanced emulsification activity index and improved thermal stability of the protein. Multiple spectroscopic techniques revealed that increasing pretreatment temperature (from 40 °C to 70 °C) altered the secondary structures of SPI, resulting in a more stable unfolded structure for the composite system with a significant increase in α-helical structures and a decrease in random coil and ß-sheet structures. Moreover, optimal heat treatment also leads to an augmentation of free sulfhydryl groups within complex as well as exposure of more internal chromophore amino acids on molecular surface. Size-exclusion high-performance liquid chromatography and SDS-PAGE analysis indicated that the band intensity of newly formed high-molecular-weight soluble macromolecules (>180 kDa) increased as the pre-heating temperature rose. Furthermore, fluorescence spectroscopy and molecular docking analysis suggest that hydrophobic and covalent interactions were involved in complex formation, which intensified with increasing temperature.