β-Fructofuranosidases from roots of dandelion (<i>Taraxacum officinale</i> Weber)
Peter Rutherford, A C Deacon
Biochemical Journal
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.
Extracted Claims
4 claims extracted from this paper into the knowledge graph
hydrolases (A and B) not inhibited by sucrose
“Neither of the hydrolases is inhibited by sucrose.”
beta-fructofuranosidases separated dandelion roots
“Three beta-fructofuranosidases were separated by chromatography on a DEAE-cellulose column from the soluble protein extracted from dandelion (Taraxacum officinale Weber) roots.”
hydrolases (A and B) acted on inulin series of oligosaccharides
“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 1.54...”