Comparison of soy protein isolate-(–)-epigallocatechin gallate complexes prepared by mixing, chemical polymerization, and ultrasound treatment

Abstract

The effects of the preparation method (mixing, chemical polymerization, or ultrasound treatment) on the structure and functional properties of soy protein isolate-(–)-epigallocatechin-3-gallate (SPI-EGCG) complexes were examined. The mixing treated SPI-EGCG samples (M−SE) were non-covalently linked, while the chemical polymerization and ultrasound treated SPI-EGCG samples (C-SE and U-SE, respectively) were bound covalently. The covalent binding of EGCG with protein improved the molecular weight and changed the structures of the SPI by decreasing the α-helix content. Moreover, U-SE samples had the lowest particle size (188.70 ± 33.40 nm), the highest zeta potential (−27.82 ± 0.53 mV), and the highest polyphenol binding rate (59.84 ± 2.34 %) compared with mixing and chemical polymerization-treated samples. Furthermore, adding EGCG enhanced the antioxidant activity of SPI and U-SE revealed the highest DPPH (84.84 ± 1.34 %) and ABTS (88.89 ± 1.23 %) values. In conclusion, the SPI-EGCG complexes prepared by ultrasound formed a more stable composite system with stronger antioxidant capacity, indicating that ultrasound technology may have potential applications in the preparation of protein-polyphenol complexes.