The objective of this study was to improved the limited functional characteristics of mungbean whole´ globulin.
The mungbean whole globulin was acylated with succinic and acetic anhydride, and the functional properties of acylated protein were investigated. The results obtained were as follows :
1. The UV-absorption spectra of acylated whole globulins with that of the succinylated 74% whole globulin as large blue shift of the absorption maximum and minimum wavelength from 275㎚ to 269㎚, respectively.
2. The mobility of acylated whole globulin were increased on PAGE pattern, and degree of mobility was particulary remarkable in case of succinylation.
3. The water absorption capacity of whole globulin was increased by acylation. The most increased rate of whole globulin was 174.02% from succinylated 74%. The oil absorption capacity of whole globulin was increased by acylation. The most increased rate of whole globulin was 165.41% from acetylated 81.77%.
4. The bulk density of whole globulin was decreased by acylation, and the greater the extent of acylation, the smaller the bulk density.
5. The foaming capacity and stability of whole globulin was increased by acylation, and remarkably high in 74% succinylated whole globulin, in contrast, however, the foaming capacity and stability of native and acylated whole globulin were decreased by heat treatment.
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