SDS and native PAGE profiles of the prepared SPIs
The SPI prepared by both alternative defatting and modified protein
extraction procedures displayed similar denaturing and native
electrophoretic profiles, with , , and subunits present for -conglycinin,
and acid and basic subunits present for glycinin (Figure 2).
The native PAGE profiles (Figure 2b, 2d) revealed that the SPI
prepared from methanol defatted meal, soaked bean and the SPI
resolubilized at pH 5.0, contained higher amounts of aggregated
proteins (that is, proteins with MW between 440 and 669 KDa). The
absence of a protein band with MW between 80 and 90 kDa was also
observed in the SDS-PAGE profile of the SPI resolubilized at pH 5.0.