Abstract
The enzymes involved in the hydrolysis of the rhamnose moieties fromα-chaconine were 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 precipitate. Enzyme activity was increased by the use of non-ionic detergents with a mixture of Triton X-100:Triton CF-54 providing the greatest increase in activity. The pH and temperature optimums for the enzymes from both varieties were found to be 6.0 and 42 C, respectively. The route ofα-chaconine metabolism (either through B1-or B2-chaconine) was dependent upon incubation temperature. The effect of substrate concentration on enzyme activity was determined for both varieties and the Kms calculated from Lineweaver-Burke double reciprocal plots. The Km values for the Kennebec and Wauseon rhamnosidases were found to be 9.2×10−4 and 1.7×10−5M, respectively.
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