Development of protein-polyphenol particles to stabilize high internal phase Pickering emulsions by polyphenols' structure

Protein-polyphenol colloidal particles are promising stabilizers for high internal phase Pickering emulsions (HIPPEs). However, the relationship between the structure of the polyphenols and its ability to stabilize HIPPEs has not been studied thus far. In this study, bovine serum albumin (BSA)-polyphenols (B-P) complexes were prepared, and their ability to stabilize HIPPEs was investigated. The polyphenols were bound to BSA via noncovalent interactions. Optically isomeric polyphenols formed similar bonds with BSA, whereas a greater number of trihydroxybenzoyl groups or hydroxyl groups in the dihydroxyphenyl moieties of polyphenols increased the B-P interactions. Polyphenols also reduced the interfacial tension and enhanced the wettability at the oil-water interface. The HIPPE stabilized by BSA-tannic acid complex exhibited the highest stability among the B-P complexes and resisted demixing and aggregation during centrifugation. This study promotes the potential applications of polyphenol-protein colloidal particles-stabilized HIPPEs in the food industry.

Automated summary

In this study, bovine serum albumin (BSA)-polyphenols (B-P) complexes were prepared and their ability to stabilize high internal phase Pickering emulsions (HIPPEs) was investigated. It was found that noncovalent interactions between polyphenols and BSA enhanced the stability of B-P complexes and reduced interfacial tension while improving wettability at the oil-water interface. Among the B-P complexes, the HIPPE stabilized by BSA-tannic acid complex exhibited the highest stability, resisting demixing and aggregation during centrifugation. This study promotes the potential applications of polyphenol-protein colloidal particles-stabilized HIPPEs in the food industry.