LAUSR

Due to people's pursuit of healthy and green life, soy protein isolate (SPI) is occupying a larger and larger market share. However, the low solubility of SPI affects its development in the field of food and medicine. This paper aimed to investigate the effects of sodium trimetaphosphate (STMP) on the functional properties and structures of phosphorylated SPI and its lutein-loaded emulsion. After modification by STMP, the phosphorus content of phosphorylated SPI reached 1.2-3.61 mg/g. Infrared spectrum and X-ray photoelectron spectrum analysis confirmed that PO4 3- had phosphorylation with -OH in serine of SPI molecule. X-ray diffraction analysis showed that phosphorylation destroyed the crystal structure of protein molecules. Zeta potential value of phosphorylated SPI decreased significantly. When STMP addition was 100 g/kg, particle size of protein solution decreased to 203 nm, and solubility increased to 73.5%. Furthermore, emulsifying activity and emulsifying stability increased by 0.51 times and 8 times, respectively. At the same protein concentration (1%-3% [w/w]), lutein-loaded emulsion prepared by phosphorylated SPI had higher absolute potential and smaller particle size. The phosphorylated protein emulsion at 2% concentration had the best emulsion stability after storage for 17 days. PRACTICAL APPLICATION: Phosphorylation significantly improved the emulsifying properties and solubility of SPI. Phosphorylated SPI significantly improved the stability of lutein-loaded emulsion. It provides theoretical basis for the application of phosphorylated SPI as emulsifier in delivery system and broadens the development of lutein in food and medicine field.