Abstract: Effects of different neutral salts, urea and propylene glycol on texture properties of soy protein isolate gels were studied. The results were as follows: When the concentrations of neutral salts were low(≤0.1mol/L), the electrostatic charge neutralization of these salts significantly affected the texture properties of protein gels. When the salt concentrations were increasing, the effects of anions of these salts on molecule conformation stability and hydrophobic interaction of proteins would mainly affect the gel texture properties. Hydrogen bonding was also a major physical force affecting gel texture as testified by urea and propylene glycol.

Key words: gels of soy protein isolates, texture properties, electrostatic interaction, hydrophobic interaction, hydrogen bonding