Information on EC 2.4.1.5 - dextransucrase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.4.1.5
-
RECOMMENDED NAME
GeneOntology No.
dextransucrase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sucrose + [(1->6)-alpha-D-glucosyl]n = D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Starch and sucrose metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
sucrose:(1->6)-alpha-D-glucan 6-alpha-D-glucosyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9032-14-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene dexYG
-
-
Manually annotated by BRENDA team
strain 121
-
-
Manually annotated by BRENDA team
strain 121
-
-
Manually annotated by BRENDA team
strain HJ-P4, gene LcDS
UniProt
Manually annotated by BRENDA team
strain KACC 91035, isolated from dongchimi-kimchi, a watery radish kimchi
-
-
Manually annotated by BRENDA team
formerly Leuconostoc mesenteroides B-742
-
-
Manually annotated by BRENDA team
strain EG001, isolated from lactic acid bacteria in Kimchi, a traditional Korean fermented food
UniProt
Manually annotated by BRENDA team
strain EG001, isolated from lactic acid bacteria in Kimchi, a traditional Korean fermented food
UniProt
Manually annotated by BRENDA team
strain B-1299
-
-
Manually annotated by BRENDA team
B-1375
-
-
Manually annotated by BRENDA team
strain B-512 FMC
-
-
Manually annotated by BRENDA team
strain B-512F
-
-
Manually annotated by BRENDA team
B-512FM
-
-
Manually annotated by BRENDA team
B-742CB
-
-
Manually annotated by BRENDA team
Birmingham strain
-
-
Manually annotated by BRENDA team
strain CGMCC 1.544, gene dsrX
-
-
Manually annotated by BRENDA team
strain FT 045 B
-
-
Manually annotated by BRENDA team
a constitutive mutant of Leuconostoc mesenteroides FT045B
-
-
Manually annotated by BRENDA team
IAM 1046
-
-
Manually annotated by BRENDA team
IBT-PQ
-
-
Manually annotated by BRENDA team
isolated from fermented cabbage
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides Lm 28
strain Lm 28
-
-
Manually annotated by BRENDA team
strain LM-0326, gene dexYG
-
-
Manually annotated by BRENDA team
NRRL B-1416
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRl B-512(F)
NRRl B-512(F)
-
-
Manually annotated by BRENDA team
strain NRRL B512-F
-
-
Manually annotated by BRENDA team
strain PCSIR-4
-
-
Manually annotated by BRENDA team
Sikhae
-
-
Manually annotated by BRENDA team
strain NRRL B-1146
-
-
Manually annotated by BRENDA team
isolated from soil from a sugarcane field in Assam, India
-
-
Manually annotated by BRENDA team
6715
-
-
Manually annotated by BRENDA team
E49
-
-
Manually annotated by BRENDA team
HS6
-
-
Manually annotated by BRENDA team
strain ATCC 10409
-
-
Manually annotated by BRENDA team
isolated from wheat sourdough, single copy gene
-
-
Manually annotated by BRENDA team
isolated from wheat sourdough, single copy gene
UniProt
Manually annotated by BRENDA team
isolated from wheat sourdough, single copy gene
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1'-beta-D-fructofuranosyl alpha-acarbose
D-fructose + acarbose
show the reaction diagram
alpha-D-glucopyranosyl fluoride + ?
?
show the reaction diagram
luteolin + sucrose
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
show the reaction diagram
myricetin + sucrose
?
show the reaction diagram
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
sucrose + 1,5-anhydro-D-fructose
alpha-D-glucopyranosyl-(1,6)-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose
show the reaction diagram
sucrose + 2-chloroethanol
2-chloroethyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + 3-methyl-1-butanol
D-fructose + 3-methylbutyl alpha-D-glucoside
show the reaction diagram
sucrose + 4-chlorobutanol
4-chlorobutyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + 6-chlorohexanol
6-chlorohexyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + acceptor
?
show the reaction diagram
-
-
-
-
?
sucrose + alpha-butylglucopyranoside
alpha-D-glucopyranosyl-(1,6)-O-butyl-alpha-D-glucopyranoside + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-butyl-alpha-D-glucopyranoside
show the reaction diagram
-
-
-
-
?
sucrose + alpha-D-glucopyranoside
?
show the reaction diagram
sucrose + butan-1-ol
butyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + dextran
?
show the reaction diagram
sucrose + dextran
D-fructose + ?
show the reaction diagram
sucrose + ethanol
D-fructose + ethyl alpha-D-glucoside
show the reaction diagram
sucrose + ethanol
ethyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + gentobiose
?
show the reaction diagram
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + hydroquinone
D-fructose + 4-hydroxyphenyl-alpha-D-glucopyranoside
show the reaction diagram
sucrose + isomaltohexaose
?
show the reaction diagram
sucrose + isomaltose
D-fructose + isomaltotriose
show the reaction diagram
sucrose + L-ascorbic acid
D-fructose + L-ascorbic acid 2-glucoside
show the reaction diagram
sucrose + maltose
?
show the reaction diagram
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + methanol
D-fructose + methyl alpha-D-glucoside
show the reaction diagram
sucrose + methanol
methyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + N-(tert-butoxycarbonyl)-L-serine methyl ester
N-tert-butoxycarbonyl-3-O-alpha-D-glucopyranosyl-L-serine methyl ester + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + n-propanol
D-fructose + propyl alpha-D-glucoside
show the reaction diagram
sucrose + N-tert-butoxycarbonyl-D-serine methyl ester
N-tert-butoxycarbonyl-3-O-alpha-D-glycopyranosyl-D-serine methyl ester + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + propan-1-ol
propyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + salicin
?
show the reaction diagram
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + tert-butanol
D-fructose + tert-butyl alpha-D-glucoside
show the reaction diagram
-
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
sucrose + dextran
D-fructose + ?
show the reaction diagram
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CoCl2
-
activates 22% at 4 mM
FeSO4
-
inhibits 26.5% at 0.1 mM, but activates 39.5% at 0.05 mM
K+
activates by 13.6% at 2 mM
Li+
activates by 15.8% at 2 mM
Mg2+
-
1 mM, stimulates activity of enzyme N
MgSO4
-
activates 115.6% at 0.1 mM, 20% at 0.05 mM
Mn2+
-
activates the native and the recombinant enzyme
MnSO4
-
activates 68% at 0.1 mM, but inhibits at 0.05 mM by 26%
NaCl
-
activates 11% at 0.1 mM
Ni2+
activates by 7% at 2 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1'-beta-D-fructofuranosyl alpha-acarbose
-
strong inhibition
2,4,6-trinitrobenzene-sulphonic acid
-
inactivation
2-deoxy-2-fluoro-alpha-D-glucopyranosyl fluoride
-
competitive
2-mercaptoethanol
-
120 mM, 17% inhibition
3-Deoxy-3-fluoro-alpha-D-glucopyranosyl fluoride
-
competitive
3-deoxy-3-thio-alpha-D-glucopyranosyl fluoride
-
competitive
6'-Amino-6'-deoxysucrose
-
competitive
6-Deoxy-6-fluoro-alpha-D-glucopyranoside
-
very weak, noncompetitive
6-Deoxysucrose
-
-
acarbose
-
strong inhibition
Al3+
-
strongly inhibits the native and the recombinant enzyme
alpha-D-glucopyranosyl fluoride
-
-
CaCl2
-
inhibits at 0.1 mM by 64%
Cd2+
23% inhibition at 2 mM
D-fructose
-
competitive
D-gluconic acid
-
-
D-glucono-1,5-lactone
-
competitive
D-glucuronic acid
-
reduced, noncompetitive
dextran derivatives
-
in which 5-50% of the D-glucose units are oxidized, acts as potent and specific inhibitor. 10%-oxidized derivatives of dextran fraction ranging in MW from 10000 Da to 2000000 Da
-
diethyldicarbonate
-
-
dithiothreitol
-
100 mM, 41% inhibition
FeSO4
-
inhibits 26.5% at 0.1 mM, but activates 39.5% at 0.05 mM
Glutaraldehyde
-
does not support enzyme stability, but inhibits the enzyme activity
Guanidine-HCl
methyl 6-amino-6-deoxyglucoside
-
competitive
methyl 6-deoxy-6-fluoro-alpha-D-glucopyranoside
-
very weak, noncompetitive
methyl 6-deoxy-alpha-D-glucopyranoside
-
weak competitive
methyl alpha-D-glucopyranoside
-
-
methyl-alpha-D-glucoside
Methyl-deoxy-alpha-D-glucopyranoside
-
weak, competitive
MnSO4
-
activates 68% at 0.1 mM, but inhibits at 0.05 mM by 26%
N-Methyl-D-glucamine
-
competitive
Na+
-
slightly inhibits the native, but not the recombinant enzyme
Nojirimycin
-
noncompetitive
o-phthalaldehyde
Periodate-oxidized dextrans
-
-
-
phenylmercuric acetate
pyridoxal-5'-phosphate
-
inactivation
Rb+
56% inhibition at 2 mM
Ribocitrin
-
-
Sn2+
34% inhibition at 2 mM
Sucrose
-
the 155000 Da enzyme form is more sensitive to substrate inhibition than the 170000 Da precursor form
Tris
-
competitive with sucrose
ZnSO4
-
inhibits 27% at 0.05 mM and 24.5% at 0.1 mM
additional information
-
no effect by 7 M urea on enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dextrans
methyl-alpha-D-glucoside
-
50 mM, activates release of D-fructose, sucrase activity, inhibits synthesis of dextran, transferase activity
additional information
-
citrate buffer at 0.3 M results in highest activity of wild-type and mutant strains, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
189
1'-beta-D-fructofuranosyl alpha-acarbose
-
-
26
alpha-D-glucopyranosyl fluoride
-
-
0.0086 - 101.7
Sucrose
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.085 - 3.2
Dextran
0.4 - 1070
Sucrose
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.35
1'-beta-D-fructofuranosyl alpha-acarbose
-
-
63
2-deoxy-2-fluoro-alpha-D-glucopyranosyl fluoride
-
-
93
3-Deoxy-3-fluoro-alpha-D-glucopyranosyl fluoride
-
-
53
3-deoxy-3-thio-alpha-D-glucopyranosyl fluoride
-
-
6.6 - 18
6'-Amino-6'-deoxysucrose
1.6
6-Deoxysucrose
-
-
36
alpha-D-glucopyranosyl fluoride
-
-
6.3 - 7.5
D-gluconic acid
0.2 - 1.1
EDTA
27
fructose
-
-
9.4
glucono-delta-lactone
-
sucrose concentration 12.2-97.4 mM
9.5 - 13.9
glucuronic acid
400
methyl 6-deoxy-6-fluoro-alpha-D-glucopyranoside
-
-
267
methyl 6-deoxy-alpha-D-glucopyranoside
-
-
97
methyl alpha-D-glucopyranoside
-
-
27.3
Methyl-6-amino-6-deoxyglucoside
-
sucrose concentration 1.2-4.9 mM
12
methyl-alpha-D-glucoside
-
sucrose concentration 12.2-97.4 mM
30 - 68.3
N-Methyl-D-glucamine
1.5
Nojirimycin
-
sucrose concentration 12.2-97.4 mM
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.012
-
purified recombinant mutant DRN4
0.027
-
purified recombinant mutant DRN2
0.037
-
purified recombinant wild-type DSRB742
0.185
-
purified recombinant mutant DRN3
0.287
-
purified recombinant mutant DRN1
0.6
-
crude enzyme, culture supernatant, pH 5.4, 30C
1.2
purified recombinant chimeric DSXR, dextransucrase activity, pH 5.8, 28C
13.9
-
purified recombinant wild-type DSRBCB4
18
-
PEG 400-purified enzyme, pH 5.4, 30C
23
-
purified enzyme, pH 5.4, 30C
23.8
-
enzyme purified by the phase-partition using PEG 400
31.3
-
partially purified wild-type enzyme, pH 4.5, 30C
35.3
-
purified native enzyme
36
-
PEG 1500-purified enzyme, pH 5.4, 30C
42.1
-
enzyme purified by the phase-partition using PEG 600
54
-
cellobio-oligosaccharides synthesis
97.37
-
recombinant enzyme in crude enzyme extract
126
purified recombinant enzyme
141
-
155000 Da enzyme form
145
-
170000 Da precursor
173.2
-
partially purified mutant enzyme, pH 5.0, 35C
686
purified recombinant enzyme, in presence of 0.1 mM Ca2+
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
wild-type enzyme
5.5 - 6.9
-
enzyme II
6.3 - 6.5
-
enzyme I
6.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 8
activity range, dependent on the buffer system
3.5 - 6.8
activity range of the recombinant enzyme, profile, overview
3.5 - 8
activity range
4 - 7.5
-
mutant enzyme, maximal activity at pH 5.0, 25% of maximal activity at pH 4.0, and 7.5% of maximal activity at pH 7.5
4 - 7
-
pH 4.0: about 40% of maximal activity, pH 7.0: about 60% of maximal activity
4.5 - 6.5
-
activity range analyzed
4.6 - 5.6
-
measurement range, 85% of maximal activity at pH 4.6
5 - 6.4
highly reduced activity below pH 5.0 and above pH 6.4
5 - 7
-
about 40% of maximal activity at pH 5.0 and pH 7.0
additional information
-
no enzyme activity at neutral pH by the wild-type strain
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
-
recombinant enzyme
35 - 40
-
enzyme II
40 - 45
-
enzyme I
40
-
native enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 45
-
mutant enzyme, activity range
8 - 36
-
8C: 22% of activity maximum, 36C: 30% of activity maximum
10 - 42
activity range of the recombinant enzyme, profile, overview
15 - 30
-
62% of maximal activity at 15C
15 - 40
-
wild-type enzyme, activity range
20 - 40
-
20C: about 60% of maximal activity, 40C: about 50% of maximal activity
20 - 50
22 - 30
-
measurement range
25 - 35
-
activity range analyzed
37 - 51
-
80% of activity maximum at 37C and 51C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
DsrP, sequence calculation
4.6
sequence calculation
5.26
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
-
enzyme I and II, disc gel electrophoresis
94000
-
gel filtration
100000
130000 - 133000
-
disc gel electrophoresis
160000 - 180000
intracellular dextransucrase 1 and extracellular dextransucrase
180000
220000 - 240000
intracellular dextransucrse 2
additional information
-
the enzyme has two major forms: MW 177000 Da and MW 158000 Da
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
no glycoprotein
proteolytic modification
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7.5
purified recombinant enzyme, stable
720214
4 - 8.5
LcDS is very stable within that pH range
705094
4 - 5
-
purified recombinant enzyme, quite stable
687884
4
-
B-512(F) enzyme unstable, Sikhae enzyme more stable
489249
4.5 - 5.5
-
the crude enzyme is stable at 30 C for 30 h at pH ranging from 4.5 to 5.5, partially purified enzyme is stable in non-fermented cashew apple juice at pH 5.0 for 96 h at 30 C, overview
703787
4.6 - 7.2
-
4C, 24 h, 50% loss of activity at pH 4.6 and 7.2, enzyme II
489267
4.7 - 8.5
-
4C, 24 h, 50% loss of activity at pH 4.7 and 8.5, enzyme I
489267
5 - 7
-
recombinant enzyme, quite stable
706904
5 - 6.4
partially purified recombinant fusion enzyme DXSR, stable with above 80% of maximal activity
703491
5 - 6.5
-
stability optimum, free enzyme
489261
5 - 6
over 80% of maximal activity within this range, but the activity decreases rapidly outside this pH range
703750
5.2 - 8.5
-
4C, 0.1% bovine serum albumin, stable for 24 h, rapid inactivation below pH 5.0
489268
5.2
-
stability optimum, immobilized enzyme
489261
5.3 - 5.8
-
4C, 24 h, enzyme II stable
489267
5.4
-
30C, native enzyme loses 90% of its inital activity in only 2 h
658333
5.5
-
4C, 24 h, enzyme N is stable
489264
6 - 9
-
4C, stable at 4C for 24 h, 4 mg/ml dextrans
489263
6
-
4C, 24 h, enzyme I is stable
489264
6.2 - 6.9
-
4C, 24 h, enzyme I stable
489267
7 - 9
-
4C, stable for 24 h, without dextran in solution
489263
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 60
-
the native DsrX shows higher stability than the recombinant DsrX at the temperature range from 4C to 60C for 2 h, native enzyme shows 84% remaining activity at 40C after 2 h, while recombinant enzyme shows only 3.1%
10 - 30
-
purified enzyme, stable at, rapid loss of activity above. Loss of 65% activity within 20 h at 30C without added stabilizer, in presence of Tween 80 the enzyme loses only 8% activity. Loss of 92% activity at 30C within 4 days
15 - 37
stable, rapid decrease in activity above 37C
20 - 30
purified recombinant enzyme, in 20 mM sodium acetate, pH 5.4, 30 min, stable, rapid loss of activity above 30C
25
-
immobilized enzyme, 60 min, maximally stable
28
partially purified recombinant fusion enzyme DXSR, stable
50
-
240 min, crude enzyme, inactivation
additional information
-
stability of immobilized enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ significantly stabilizes the soluble enzyme
-
Ca2+ stabilizes the enzyme
-
dextran T10 stabilizes
-
enzyme deactivation follows first order rate kinetics
-
glutaraldehyde does not support the stability, rather it inhibits the enzyme activity, also glycerol, PEG 8000, and dextran (500 kDa) do not stabilize the enzyme
-
maximal stabilization of soluble enzyme by 5 mM Ca2+
-
native enzyme loses 90% of its inital activity in only 2 h at pH 5.4, 30C, immobilization on Eupergit C 250L significantly stabilizes dextransucrase. Despite a fast partial inactivation in the first 2 h, the enzyme immobilized on Eupergit C 250L maintains more than 40% of the initial activity over the following 2 days, the enzyme immobilized on Eupergit C maintains about 15% of the initial activity after 1 day
-
stability is significantly increased by 33% glycerol and 0.1% bovine serum albumin
-
stability of crude dextransucrase from Leuconostoc citreum strain B-742 in synthetic and in cashew apple juice culture broth, evaluation, overview
-
the best conditions for the enzyme are 50% v/v dimethyl sulfoxide and immobilization in alginate beads
-
the enzyme can be stabilized by high-molecular-weight dextran, polyethyleneglycol or nonionic detergents such as Tween 80
-
Tween 80 stabilizes the purified enzyme, maximally at 30C
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
-
at 50%, reduces the enzyme activity by 94%
acetonitrile
-
at 20%, reduces the enzyme activity by 80%
dimethyl sulfoxide
-
the best conditions for the enzyme are 50% v/v dimethyl sulfoxide and immobilization in alginate beads
DMSO
-
at 90%, reduces the enzyme activity by 91%
Ethanol
-
at 50%, reduces the enzyme activity by 80%
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, purified enzyme, loss of 25% activity within 14 days at 30C
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25C, crude enzyme in cashew apple juice, pH 6.5, 48 h , quite stable
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25C, purified recombinant enzyme, 59% activity remaining after 4 days
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4C or -70C, stable during extended storage
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4C, 0.1% bovine serum albumin, pH 5.2-8.5, stable for 24 h
-
4C, pH 6.0-9.0, 4 mg/ml dextran, 24 h stable, without dextran the stable range is narrowed to pH 7.0-9.0
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4C, purified enzyme, loss of 92% activity within 4 days at 30C
-
4C, purified recombinant enzyme, 50% activity remaining after 7 weeks
-
4C, purified recombinant enzyme, in 20 mM sodium acetate, pH 5.4, about 10% activity loss after 6 days, and about 35% activity loss after 20 days
in a deep-freezer, 33% glycerol, 0.1% bovine serum albumin, less than 20% loss of activity after several months
-
on standing at 4C for 30 days the native enzyme is dissociated into three inactive proteins
-
storage stability decreased by addition of dextranase
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 forms: I and II; NRRL B-1299
-
2 forms: I and N, enzyme I is gradually converted into enzyme N upon ageing, conversion is stimulated in the presence of NaCl; NRRL B-1299
-
2 forms: MW 177000 and MW 158000; NRRL B-512(F)
-
dextransucrase II; NRRL B-512(F)
-
extracellular enzyme from kimchi by anion exchange chromatography
-
multiple forms: I, II and III; NRRL B-512(F)
-
native enzyme 61fold from strain NRRL B-640 by repeated polyethylene glycol fractionation and gel filtration; native enzyme from strain nRRL-B 640 by polyethylene glycol fractionation and gel filtration, with 23-40fold purification by 10% w/v PEG 1500 and 35-60fold of total purification, method optimization, overview
-
native enzyme by PEG 1500 fractionation
-
native enzyme partially by ammonium sulfate fractionation and dialysis, recombinant N-terminally His6-tagged DsrX from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
native enzyme partially from strain PCSIR-4 2.5fold by ethanol
-
native extracellular enzyme by a single-step fractionation using polyethylene glycols of different molecular mass, 31fold purification by PEG 400 and 45fold purification by PEG 1500
-
NRRL B-512(F); partial; Sikhae
-
recombiant His-tagged enzyme from Escherichia coli by metal affinity chromatography. Various methods such as precipitation by ammonium sulphate, ethanol, or polyethylene glycol, phase partitioning, ultrafiltration and chromatography are used to purify the enzyme, detailed overview. Purification of dextransucrase is rendered difficult by the presence of viscous dextran in the medium
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recombiant His-tagged wild-type and mutant enzymes about 6fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant enzyme
-
recombinant enzyme 11.4fold from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation and nickel affinity chromatography
-
recombinant enzyme 5.1fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
recombinant His-tagged DSRC39-2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatogaphy