Purification and characterization of dioscin-alpha-L-rhamnosidase from pig liver.

Dioscin-alpha-L-rhamnosidase was isolated, purified and partially characterized from pig liver. The maximum activity was reached at pH 7, 42 degrees C, 24 h, and 2% of substrate concentration. Fe3+ and Cu2+ inhibited the enzyme; the ion Ca2+ activated it. Mg2+ was an inhibitor at 100 mM, but it was an activator at 200 mM. Zn2+ could be a weak activator of the enzyme. The molecular weight of dioscin-alpha-L-rhamnosidase was about 47 kDa as determined by the method of SDS-polyacrylamide gel electrophoresis.