Isolation and characterization of fructosyltransferase from chicory roots

Abstract

The occurrence of fructosyltransferase was demonstrated in the roots of chicory. The enzyme was purified 14-fold by ammonium sulphate fractionation and sephadex column chromatography. The optimal conditions for activity were pH 5·6, 37° and substrate (sucrose) concentration of 5·84 × 10^-1 M. The K_m of the enzyme was found to be 2·85 × 10^-1 M. The enzyme was completely inactivated at 62·5°. Neither dialysis nor addition of inorganic phosphate affected its activity. The enzyme was capable of synthesizing glucofructosans from sucrose alone with the simultaneous release of glucose until seven oligosaccharides were synthesized, and with progressive enzyme activity small quantities of fructose were also released. Ag⁺ and Hg²⁺ completely inhibited the enzyme action, whereas, Cu²⁺, Zn²⁺, Fe²⁺, Na⁺, K⁺ and Ca²⁺ had almost no effect. The enzyme activity was significantly increased by Mn²⁺, Mg²⁺, Co²⁺ and Ni²⁺.