Abstract
The α-D-galactosidases of six Streptomyces strains were examined on their inducer susceptibility, substate specificity, and inhibitor susceptibility. In all strains examined, α-D-galactosidase was induced by D-galactose, but neither by D-fucose nor by L-arabinose. α-D-Fucosidase activity was always induced accompanying with α-D-galactosidase activity. β-L-Arabinosidase activity, however, was never observed. These α-D-galactosidases were purified to electro-phoretically pure degree by successive ammonium sulfate and ethanol precipitation, and ion exchange and gel filtration chromatography. The purified preparations from six strains were different from each other in their chromatographic behaviors and in some physical properties, but they all showed strong α-D-fucosidase activity as well. The α-D-galactosidase activities were strongly inhibited by D-galactose and L-arabinose, but scarcely by D-fucose. On the other hand, their α-D-fucosidase activities were inhibited by D-fucose as well as by D-galactose and L-arabinose.
