Isolation,partial purification and characterization of a potato peel ∞-solanine cleaving glycosidase

An enzyme which hydrolyzes the rhamnose from ∞-solanine was isolated and partially purified by ammonium sulfate precipitation from the peels of Kennebec and Wauseon potatoes. Enzyme activity was found to be present in the 60 to 80% ammonium sulfate fraction. Enzyme activity was increased by the use of non-ionic detergents with a mixture of Triton X-100:Triton CF-54 (2:1, w/w) providing the greatest increase in activity. The pH optimum for the rhamnosidase for both varieties was found to be 6.0 while of the temperatures evaluated 42 °C was the optimum temperature. The effect of substrate concentration on enzyme activity was determined for both varieties and the Vmax and Km were calculated from Lineweaver-Burke double reciprocal plots. The Vmax and Km for the Kennebec and Wauseon rhamnosidases were found to be 0.27 mg/ml and 5.4 x 10^-4 M and 0.48 mg/ml and 8.2 x 10^-4 M, respectively.