Physicochemical and functional properties of pea globulin (7S, 11S) and pea protein isolate (PPI) were analyzed and compared. The results showed that pea globulin showed excellent functional properties. Its protein solubility (PS), emulsifying ability and stability were much higher than those of PPI. Intrinsic fluorescence spectrum analyses confirmed much loss of tertiary conformation of PPI, which may be attributed to acid and alkaline treatment during PPI preparation resulted in protein denaturation, exposure of hydrophobic groups. DSC showed that thermal stability of 11S was higher than 7 S, and the lower degree of degeneration of the 11S protein. DSC data showed that thermal stability of 11S was higher than 7 S, pea protein isolate and 7S had undergone denaturation.
