Purification and Characterization of Dioscin-α-L-rhamnosidase from Pig Liver

Abstract

Dioscin-α-L-rhamnosidase was isolated, purified and partially characterized from pig liver. The maximum activity was reached at pH 7, 42 °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-α-L-rhamnosidase was about 47 kDa as determined by the method of SDS–polyacrylamide gel electrophoresis.