title: -Fructofuranosidases from roots of dandelion (Taraxacum officinale Weber).
abstract: 1. Three beta-fructofuranosidases were separated by chromatography on a DEAE-cellulose column from the soluble protein extracted from dandelion (Taraxacum officinale Weber) roots. 2. One enzyme, which acted on sucrose, was characterized as an invertase, with a K(m) of 2.00x10(-2)m and pH optimum of 7.5. 3. The other two enzymes are hydrolases (A and B), which act on the inulin series of oligosaccharides [general formula glucose-fructose-(fructose)(n)]. They both have a pH optimum of 4.0 and K(m) of 1.54x10(-2)m but differ in their chromatographic behaviour on DEAE-cellulose. Neither of the hydrolases is inhibited by sucrose. 4. The physiological role of these three hydrolytic enzymes is discussed.
mesh_terms: D002848:Chromatography, DEAE-Cellulose; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000302:isolation & purification; D010944:Plants / Q000201:enzymology*; D013393:Sucrase / Q000302:isolation & purification*; D013395:Sucrose
chemical_list: D013395:Sucrose; D006867:Hydrolases; D013393:Sucrase