Oil in water emulsion stabilized by glycated rice bran protein aggregates: Effect on interfacial behavior and in vitro digestion of emulsion

To investigate the effect of molecular weight of saccharides and heating time on interfacial behavior of protein, glycated rice bran protein aggregates (gRBPAs) were obtained by incubating rice bran protein (RBP) with glucose (Glu), maltose (Mal) and dextran (Dex) via acid-heat treatment (pH 2.0, 90 degrees C). Subsequently, the stability and in vitro simulated digestion properties of oil in water (O/W) emulsion stabilized by gRBPAs were analyzed. Structural analysis (circular dichroism and fluorescence spectra) proved that the tertiary structure and secondary structure of RBP changed after glycation, and the contents of beta-sheet structure of gRBPAs increased significantly. Besides, the glycation improved the interfacial activity and emulsification of protein obviously. Compared with Glu or Mal, the grafting of Dex could produce larger steric hindrance, which better inhibited the aggregation of emulsion droplets. Furthermore, glycation enhanced the pancreatic lipase (PL) inhibitory activity of gRBPAs obviously, and the emulsions stabilized by gRBPAs exhibited higher anti-digestion ability (62.12-75.00%) compared with RBP (95.27%). Moreover, the free fatty acid (FFA) rate of O/W emulsion was closely related to the surface hydrophobicity, degree of glycation, PL inhibitory activity and interfacial behavior of gRBPAs. Therefore, these findings would be enlightening to intuitively tailor the physicochemical stability and digestibility of O/W emulsion system according to heating time and molecular weight of saccharides. Meanwhile, this work would facilitate the application of O/W emulsion stabilized by glycated protein aggregates in functional foods.