, Volume 67, Issue 4, pp 233-238

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

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Abstract

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.

Compendio

Se aisló de la cáscara de papas Kennebec y Wauseon una enzima que hidroliza la ramnosa de laα-solanina y se le purificó parcialmente por precipitación con sulfato de amonio. Se encontró acrividad enzimática en la porción de 60 a 80% de sulfato de amonio. La actividad de la enzima se incrementó utilizando detergentes no iónicos; con una mezcla de Triton X-100: Triton CF-54 (2:1, w/w) se obtuvo el mayor incremento en la actividad. El pH óptimo para la ramnosidasa, para ambas variedades, fue 6.0, mientras que 42°C fue la temperatura óptima de todas las temperatures evaluadas. El efecto de la concentratión del sustrato en la actividad de la enzima fue determinado para ambas variedades y la Vmax y Km fueron calculadas de las parcelas Lineweaver-Burke de doble reciprocidad. La Vmax y Km para las ramnosidasas de Kennebec y Wauseon fueron 0.27 mg/cm3 y 5.4 x 10-4M, y 0.48 mg/cm3 y 8.2 x 10-4M, respectivamente.