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3.2.1.26: beta-fructofuranosidase

This is an abbreviated version!
For detailed information about beta-fructofuranosidase, go to the full flat file.

Word Map on EC 3.2.1.26

Reaction

raffinose
+
H2O
=
beta-D-fructofuranose
+
6-O alpha-D-galactopyranosyl-alpha-D-glucopyranose

Synonyms

A/N-InvG, acid invertase, Acid sucrose-6-phosphate hydrolase, acINV, AFR529Wp, AI, AIV, alkaline invertase, alkaline invertase InvA, alkaline invertase InvB, alkaline/neutral invertase, Atbetafruct4, b-fructofuranosidase, beta-(1-2)-fructofuranosidase, beta-D-fructofuranosidase, beta-D-fructofuranosidase fructohydrolase, beta-D-fructofuranoside fructohydrolase, beta-FFase, beta-fructofuranosidase, beta-fructofuranosidase I, beta-fructofuranoside fructohydrolyase, beta-fructosidase, beta-h-fructosidase, BfrA, BlsacA, Bmsuc1, cell wall invertase, cell wall invertase 4, cell wall-bound invertase, cell wall-bound ivertase, cell-wall invertase, cell-wall invertase 1, CIN, Cin1, CIN12, Cin5, CINV1, CscA, CWI, CWIN, CWIN1, Cwinv-1, cwINV1, cytosolic invertase, EINV1, EINV2, EINV3, EINV4, FCWI, Ffase, FFase I, Ffh, fructofuranosidase, beta-, fructosylinvertase, glucosucrase, INAC-INV, INCW2, INV, Inv-CW, INV-E, Inv-V, INV1p, INV2, INVA, INVB, invertase, invertase 1, invertase 2, Invertase E1, invertase SUC2, invertin, lbbetafruct2, lbbetafruct3, Lin5, Lin6, Lin7, Lyc e 2.01, Lyc e 2.02, maxinvert L 1000, More, neutral invertase, NI, Nin88, OsCIN1, OsCIN2, OsCIN3, Protein B46, re-INVB, SacA, saccharase, SAI, soluble acid invertase, Suc2, SucB, sucrase, Sucrase E1, Sucrose-6-phosphate hydrolase, TIV-1, Uninv, uninv2, Vacuolar invertase, vacuolar invertase 1, vacuolar invertase CvINV, vacuolar invertase NvINV, VIN, VIN1, VIN2, Vinv-1, VINV1, VINV2, VINV3, yeast invertase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.26 beta-fructofuranosidase

Application

Application on EC 3.2.1.26 - beta-fructofuranosidase

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
analysis
-
comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major
biofuel production
food industry
industry
nutrition
pharmacology
synthesis
additional information
-
stabilization of enzyme against thermal denaturation by intermolecular and intramolecular crosslinking of the surface nucleophilic functional groups with diisocyanate homobifunctional reagents of various lengths. Crosslinking with 1,4-diisocyanatobutane is most effective in enhancing thermostability. Stability is improved dramatically by crosslinking 0.5 mg/ml of protein with 30 micromol/ml of the reagent. Molecular engineering by crosslinking reduces the first-order thermal denaturation constant at 60°C from 1.567 per min for the native enzyme to 0.437 per min for the stabilized enzyme. The best crosslinking treatment increases the activation energy for denaturation from 391 kJ per mol for the native protein to 466 kJ per mol for the stabilized enzyme