Novel a-linolenic acid emulsions stabilized by octenyl succinylated starch -soy protein-epigallocatechin-3-gallate complexes: Characterization and antioxidant analysis.

In this study, octenyl succinylated starch (OSAS)-soy protein (SP)-epigallocatechin-3-gallate (EGCG) complexes were designed to enhance the physical and oxidative stability of α-linolenic acid emulsions. Formations of OSAS-SP-EGCG complexes were confirmed via particle size, ξ-potential, together with fourier transform infrared (FTIR). A mixing ratio of 1:2 for OSAS to SP-EGCG resulted in ternary complexes with the highest contact angle (59.69°), indicating the hydrophobicity. Furthermore, the characteristics of α-linolenic acid emulsions (oil phase volume fractions (φ) of 10% and 20%) stabilized by OSAS-SP-EGCG complexes were investigated, including particle size, ξ-potential, emulsion stability, oxidative stability, and microstructure. These results revealed exceptional physical stability together with enhanced oxidative stability for these emulsions. Particularly, emulsions utilizing complexes having a 1:2 OSAS to SP-EGCG ratio exhibited superior emulsion stability. These findings provide theoretical support to the development of emulsions containing high levels of α-linolenic acid and for the broader application of α-linolenic acid in food products.

Effect of octenyl succinic anhydride modified starch on soy protein-polyphenol binary covalently linked complexes.

The present study aimed to investigate the effects of octenyl succinic anhydride modified starch (OSAS) on soy protein (SP)-(-)-epigallocatechin-3-gallate (EGCG) binary covalently linked complexes. Mean diameters of OSAS-SP-EGCG complexes decreased from 379.6 ± 54.9 nm to 272.7 ± 47.7 nm as the OSAS-to-SP-EGCG ratio changed from 1:2 to 4:1, while ζ-potential decreased from -19.1 ± 0.8 mV to -13.7 ± 1.2 mV. Fourier transform infrared spectroscopy results revealed that the characteristic peaks at 1725 cm-1 and 1569 cm-1 for OSAS disappeared in the OSAS-SP-EGCG complexes, indicating an interaction between OSAS and SP-EGCG complexes. X-ray diffraction analysis showed that with the increase of OSAS content, the diffraction peak at approximately 8.0° decreased from 8.22° to 7.74°, implying that the structures of OSAS and SP-EGCG complexes were rearranged after forming into OSAS-SP-EGCG complexes. The contact angle of the OSAS-SP-EGCG complexes significantly increased from 59.1° to 72.1° with the addition of OSAS increased, revealing that the addition of OSAS improved hydrophobicity of the SP-EGCG complexes. Transmission electron microscopy images revealed that the individual OSAS-SP-EGCG complexes became smaller but stuck together to form large fragments, which was different from the morphology of OSAS and SP-EGCG complexes. Thus, the OSAS-SP-EGCG complexes developed in this study may be effective emulsifiers for improving the stability of emulsion systems in the food industry.