The emulsifying activity of native and citraconylated globulins in sesame (13S) and soybean (7S and 11S) seeds was examined. Native 13S showed intermediate emulsifying activity between those of native 7S and 1 IS. The emulsifying activity and stability of all the globulins increased with citraconylation, but the emulsifying stability of 13S was lower than those of 1 IS and 7S. The surface hydrophobicities of all the globulins increased with the modification, the value of citraconylated 13S being 4 times that of native globulin. Enzymatic hydrolysis as an in vitro model system of digestibility indicated that citraconylated globulins had the same digestibility as the native globulins.
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