Improvement of protein emulsion stability through glycosylated black bean protein covalent interaction with (−)-epigallocatechin-3-gallate†

Abstract

This study investigated the effects of covalent conjugates combined by glycosylated black bean protein isolate (BBPI-G) and (−)-epigallocatechin-3-gallate (EGCG) on the emulsion stability. Fourier transform infrared (FTIR) spectroscopy showed that covalent binding of EGCG with BBPI-G made the protein molecule unfolded. Besides, the emulsifying properties of BBPI-G were increased after combined with EGCG. BBPI-G–EGCG emulsion had lower mean particle size and higher content of interfacial protein adsorption (AP), which resulted in thicker and more impact oil–water interface. Therefore, the stability of emulsions was significantly improved. Furthermore, the emulsions prepared by BBPI-G–EGCG compounds exhibited considerable stability in storage, oxidation, thermal treatments, freeze–thaw and freeze-dried powders resolubility. This study demonstrated that the covalent bond of glycosylated protein and polyphenols could advance the emulsifying performance of protein, and BBPI-G–EGCG covalent complex was an effective emulsifier for preparing high stability emulsions.

Abstract

Stability improvement of emulsions stabilized by covalent conjugation with glycosylated black bean protein and EGCG (BBPI-G–EGCG) was studied through structure changes of proteins and emulsion properties.