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The role of reaction sequence in governing the structure and emulsification performance of ternary protein-polyphenol-polysaccharide covalent complexes
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DOI：10.1016/j.lwt.2026.119411.png)
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Abstract
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Binary and ternary covalent complexes were prepared from soy protein isolate (SPI), epigallocatechin-3-gallate (EGCG), and polydextrose (PD) by varying the reaction sequence. The covalent bonding order was a critical determinant of the complexes' structural and functional properties. Formation of covalent linkages was confirmed by SDS-PAGE, polyphenol binding, and grafting degree. Circular dichroism spectra revealed a significant conformational transition in the secondary structure of SPI after covalent modification, with a decrease in alpha-helix and beta-sheet content and an increase in beta-turn and random coil structures. This structural shift suggests enhanced protein flexibility. In emulsion systems, the ternary complexes, particularly SPE, exhibited excellent stabilization performance, as demonstrated by a minimal droplet size (427.7 +/- 6.84 nm), a high absolute zeta-potential (-33.2 +/- 0.31 mV), reduced interfacial tension, and a high interfacial protein adsorption rate (82.8 +/- 0.53%). These results broaden the potential application of protein, polyphenol, polysaccharide covalent conjugation technology in functional foods and establish a theoretical foundation for developing more efficient emulsion-based delivery systems.
Keywords:
Soybean isolate protein
Polydextrose
Ternary covalent complex
Reaction sequence
Emulsion stability
(-)-Epigallocatechin-3-gallate
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