Effects of alpha-Chymotrypsin Modification on the Functional Properties of Soy Protein Isolates

Abstract

Efects of α-chymotrypsin modification ondegre of hydrolysis (DH), solubility, emulsifying capacitytein isolate (SPI) using a lipoxygenase-defected soybean(Jinpum-kong) and commercial soy protein isolate (Supro500E) were compared. SPIs were hydrolyzed by α-chy-motrypsin at pH 7.8 and 37oC for 30 min. DHs of Supro50E and Jinpum-kong SPI were increased by α-chymot-rypsin modification, and DH of Supro 500E was higherthan that of Jinpum-kong SPI. DH of α-chymotrypsintreated Jinpum-kong SPI was similar with untreatedest. Solubility, emulsifying capacity and thermal aggrega-tion of SPIs were increased by α-chymotrypsin modification,and these changes were highly related to changes in DH.Functional properties of Supro 500E were higher thanJinpum-kong SPI in both of untreated and α-chymot-rypsin treated SPIs.