Abstract
Alpha-galactosidase and invertase were accumulated in a coherent middle phase in a three-phase partitioning system under different conditions (ammonium sulphate, ratio of tert-butanol to crude extract, temperature and pH). Alpha-galactosidase and invertase were purified 15- and 12-fold with 50 and 54% activity recovery, respectively. The fractions of interfacial precipitate arising from the three-phase partitioning were analyzed by SDS-PAGE. Both purified preparations showed electrophoretic homogeneity on SDS-PAGE.
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