Effects of enzymatic hydrolysis combined with glycation on the emulsification characteristics and emulsion stability of peanut protein isolate.

Peanut protein isolate (PPI) has high nutritional value, but its poor function limits its application in the food industry. In this study, peanut protein isolate was modified by enzymatic hydrolysis combined with glycation. The structure, emulsification and interface properties of peanut protein isolate hydrolysate (HPPI) and dextran (Dex) conjugate (HPPI-Dex) were studied. In addition, the physicochemical properties, rheological properties, and stability of the emulsion were also investigated. The results showed that the graft degree increased with the increase of Dex ratio. Fourier transform infrared spectroscopy (FTIR) confirmed that the glycation of HPPI and Dex occurred. The microstructure showed that the structure of HPPI-Dex was expanded, and the molecular flexibility was enhanced. When the ratio of HPPI to Dex was 1:3, the emulsifying activity and the interface pressure of glycated HPPI reached the highest value, and the emulsifying activity (61.08 m/g) of HPPI-Dex was 5.28 times that of PPI. The HPPI-Dex stabilized emulsions had good physicochemical properties and rheological properties. In addition, HPPI-Dex stabilized emulsions had high stability under heat treatment, salt ion treatment and freeze-thaw cycle. According to confocal laser scanning microscopy (CLSM), the dispersion of HPPI-Dex stabilized emulsions was better after 28 days of storage. This study provides a theoretical basis for developing peanut protein emulsifier and further expanding the application of peanut protein in food industry.