Abstract
A 108-fold purification of the sucrose synthetase from the extract of the shoot of bamboo Lelaba oldhami was achieved by ammonium sulfate fractionation, calcium phosphate gel adsorption, and chromatographic separations on Sephadex G-100 and diethylaminoethyl-cellulose columns. Some properties of this enzyme, namely thermal and pH stabilities, stabilization by aqueous glycerol, pH optimum, substrate specificities, effects of metallic ions, effects of sulfhydryl reagents, molecular weight, sedimentation constants, isoelectric point, and substrate saturation kinetics had been investigated.
The substrate saturation kinetics indicated that the enzyme could be an allosteric enzyme with the saccharide substrates (sucrose and fructose) serving as the homotropic allosteric effectors in regulating the biosynthesis and degradation of sucrose.
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