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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

General Stability

General Stability on EC 3.2.1.26 - beta-fructofuranosidase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of up to 200 mM NaCl or 50 mM sucrose does not significantly alter INV1p stability
enzyme activity almost constant within investigated time range of 250 min at room temperature
-
enzyme embedded within a polyacrylamide gel and freeze dried retains only 25% of their original activity
-
enzyme ionically immobilized on the polyethyleneco-vinyl alcohol hollow fiber, for both repeated and continous usages, the activity falls to ca. 60% of the initial activity in the early stage and after that almost keeps the value
-
freezing in 3 M glycerol for 10 days reduces avctivity to 47%, freezing in 3 M glycine causes only 16-19% loss of invertase activity
-
half-life in response to chymotrypsin attack: 315 min
-
half-life of the enzyme immobilized by the ionic bond on bead DEAHP-cellulose: 215 days
-
high pressure processing at 50°C/600 MPa for 30 min disrupts the secondary structure and tertiary structure of purified soluble acid invertase, but no aggregation of purified soluble acid invertase is observed after high pressure processing
-
operational stability of immobilized invertase: 40% of the initial activity remaining after 45 cycles of 1 min duration, producing 90.6 mg sucrose within 45 min by 2.5 mg immobilized enzyme
-
pectin exhibits a concentration-dependent protection for purified acid invertase against high pressure processing at 50°C/600 MPa for 30 min
-
polyol activated enzyme is stable up to 72 hours
-
recovery of isoenzyme AIV II activity in purification is less than that of isoenzyme AIV II due to its lower stability
-
stable to repeated freezing and thawing
-
the deglycosylated enzyme is more sensitive than the native enzyme to proteases such as pronase E and subtilisin. The deglycosylated enzyme is more sensitive at pH 4 to 7 and 40°C to 50°C
-
the enzyme can be significantly inactivated by high pressure processing with pressure (50-600 MPa) at 45°C and 50°C, and be activated by high pressure processing (50-400 MPa) at 40°C. The secondary structure of the enzyme is not sensitive to high pressure processing, and its tertiary structure is modified by high pressure processing. High pressure processing at 400 MPa/50°C for 2.5 min induces dissociation of the enzyme, and high pressure processing at 600 MPa/50°C for 30 min results aggregation and fibril formation of the enzyme
-
the invertase is completely split by treatment with endo-beta-N-acetylglucosaminidase H from Streptomyces griseus. The proteinaceous split product is still active and has a MW of 12000 Da
-