Enhancement Of Solubility And Emulsifying Properties Of Soy Protein Isolates By Glucose Conjugation

Soy protein isolate (SPI) was modified with glucose (G-) through the amino-carbonyl reaction (Maillard reaction). Solubility and emulsifying properties of the modified proteins were investigated. G-SPI conjugate was highly soluble at a wide range of pH values, while untreated SPI showed limited solubility especially at pH 4-6. Solubility of modified SPI showed the resistance to heat treatment and high ionic strength. Emulsifying activity and emulsion stability of G-SPI conjugate were much higher than those of native SPI. Comparing with some commercial emulsifiers, G-SPI conjugate showed excellent emulsifying properties in high salt concentration and neutral pH. Sodium dodecylsulfate-polyacrylamide gel electrophoresis was also used to confirm the formation of G-SPI conjugate