Information on EC 3.2.1.83 - kappa-carrageenase

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

EC NUMBER
COMMENTARY
3.2.1.83
-
RECOMMENDED NAME
GeneOntology No.
kappa-carrageenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans
show the reaction diagram
endo or random mechanism
Pseudomonas carrageenovora
-
Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans
show the reaction diagram
enzyme has an arginine residue at subsite -1, mechanism
-
Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans
show the reaction diagram
enzyme acts in solution as a random hydrolase
-
Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis of O-glycosyl bond
-
-
PATHWAY
KEGG Link
MetaCyc Link
kappa-carrageenan degradation
-
SYSTEMATIC NAME
IUBMB Comments
kappa-carrageenan 4-beta-D-glycanohydrolase (configuration-retaining)
The main products of hydrolysis are neocarrabiose-sulfate and neocarratetraose-sulfate [5]. Unlike EC 3.2.1.157 (iota-carrageenase), but similar to EC 3.2.1.81 (beta-agarase), this enzyme proceeds with retention of the anomeric configuration.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carrageenase, kappa-
-
-
-
-
kappa-carrageenanase
-
-
-
-
kappa-carrageenase
-
-
CAS REGISTRY NUMBER
COMMENTARY
37288-59-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain Dsij, isolated from Delesseria sanguinea
-
-
Manually annotated by BRENDA team
Calcalispora hiemalis
-
-
-
Manually annotated by BRENDA team
Culicidospora gravida
-
-
-
Manually annotated by BRENDA team
Cytophaga sp. 1k-C783
1k-C783
-
-
Manually annotated by BRENDA team
Cytophaga sp. MCA-2
-
-
-
Manually annotated by BRENDA team
Dactylella aquatica
-
-
-
Manually annotated by BRENDA team
Dendrospora erecta
-
-
-
Manually annotated by BRENDA team
Gyoerffyella speciosa
-
-
-
Manually annotated by BRENDA team
Heliscella stellata
-
-
-
Manually annotated by BRENDA team
Lateriramulosa uni-inflata
-
-
-
Manually annotated by BRENDA team
no activity in Tricladium angulatum
-
-
-
Manually annotated by BRENDA team
Pleuropedium tricladioides
-
-
-
Manually annotated by BRENDA team
Pseudoalteromonas porphyrae LL1
-
-
-
Manually annotated by BRENDA team
Pseudoalteromonas sp. AJ5-1
-
-
-
Manually annotated by BRENDA team
Pseudomonas carrageenovora
-
-
-
Manually annotated by BRENDA team
Pseudomonas carrageenovora
strain NCIMB 302 and strain 9
-
-
Manually annotated by BRENDA team
Pyramidospora densa
-
-
-
Manually annotated by BRENDA team
Taeniospora gracilis
-
-
-
Manually annotated by BRENDA team
Tamlana sp.
-
-
-
Manually annotated by BRENDA team
Tamlana sp. HC4
-
-
-
Manually annotated by BRENDA team
Tricellula aquatica
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
agar + H2O
?
show the reaction diagram
Pseudoalteromonas porphyrae, Pseudoalteromonas porphyrae LL1
-
1.5% activity compared to kappa-carrageenan
-
-
?
kappa-carrageenan + H2O
?
show the reaction diagram
-
-
-
-
?
kappa-carrageenan + H2O
?
show the reaction diagram
-
degradation
-
-
?
kappa-carrageenan + H2O
?
show the reaction diagram
-
on soluble kappa-carrageenan substrate, enzyme produces only large oligosaccharides at 50% of degradation. In contrast, at the same level of degradation in solid phase, enzyme generates terminal products such as kappa-neocarrabiose and kappa-neocarratetraose
-
-
?
kappa-carrageenan + H2O
?
show the reaction diagram
-
low-molecular-weight carrageenan oligosaccharides are obtained. Antitumor activities of the oligosaccharides are tested on Sarcoma 180 tumor transplanted in mice. The carrageenan oligosaccharide show much higher tumor inhibition (70.8%) and catalase activity at a dosage of 100 mg/kg compared with the control group
-
-
?
kappa-carrageenan + H2O
?
show the reaction diagram
-
the average molecular mass of solid carrageenan decreases very slowly, and tetrasaccharide production is high. kappa-carrageenase is a processive enzyme when acting on solid substrates. It has a random mode of action on soluble substrates. The conditions for processivity not only require that the active site possesses the adapted topology, but also that the substrate is in an appropriate physical and conformational state (processivity is similar for gel and powder)
-
-
?
kappa-carrageenan + H2O
?
show the reaction diagram
-
degradation, analysis of the degradation products by gel filtration, single-helix ordered conformation state for kappa-carrageenan. Degradation of carrageenan in the disordered state leads to a rapid decrease in molecular mass and the production of all possible neo-kappa-carrabiose oligomers
-
-
?
kappa-carrageenan + H2O
?
show the reaction diagram
Cytophaga sp. MCA-2
-
low-molecular-weight carrageenan oligosaccharides are obtained. Antitumor activities of the oligosaccharides are tested on Sarcoma 180 tumor transplanted in mice. The carrageenan oligosaccharide show much higher tumor inhibition (70.8%) and catalase activity at a dosage of 100 mg/kg compared with the control group
-
-
?
kappa-carrageenan + H2O
kappa-neocarrabiose sulfate + D-galactose
show the reaction diagram
Tamlana sp., Tamlana sp. HC4
-
the enzyme degrades kappa-carrageenan by hydrolyzing the beta-1,4 linkages to a series of homologous, even numbered oligosaccharides
-
-
?
kappa-carrageenan + H2O
kappa-neocarrabiose sulfate + kappa-neocarratetraose sulfate + kappa-neocarrahexaose sulfate + kappa-neocarraoctaose sulfate + kappa-neocarradecaose sulfate + D-galactose
show the reaction diagram
Pseudoalteromonas sp., Pseudoalteromonas sp. AJ5-1
-
-
main end-products
-
?
kappa-carrageenan + H2O
tetrasaccharides
show the reaction diagram
Pseudoalteromonas porphyrae, Pseudoalteromonas porphyrae LL1
-
100% activity
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
?
show the reaction diagram
-
-
-
-
-
iota-carrageenan + H2O
?
show the reaction diagram
Pseudoalteromonas porphyrae, Pseudoalteromonas porphyrae LL1
-
1% activity compared to kappa-carrageenan
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
Pseudomonas carrageenovora
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
Alatospora flagellata, Anguillospora crassa, Anguillospora longissima, Calcalispora hiemalis, Clavariopsis aquatica, Culicidospora gravida, Dactylella aquatica, Dendrospora erecta, Flagellospora penicillioides, Gyoerffyella gemellipara, Heliscella stellata, Nectria lugdunensis, Lateriramulosa uni-inflata, Lemonniera centrosphaera, Lemonniera cornuta, Margaritispora aquatica, Pleuropedium tricladioides, Pyramidospora densa, Sigmoidea prolifera, Taeniospora gracilis, Tetrachaetum elegans, Tetracladium marchalianum, Tetracladium maxilliforme, Tetracladium setigerum, Tricellula aquatica, Varicosporium elodeae, Volucrispora graminea
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
-
-
-
-
?
kappa-carrageenan + H2O
additional information
-
Pseudomonas carrageenovora
-
-
3-O-(3,6-anhydro-alpha-D-galactopyranosyl)-D-galactopyranose-4-O-sulfate, i.e. neocarrabiose-4-O-sufate, as the major degradation product
?
kappa-carrageenan + H2O
additional information
-
Pseudomonas carrageenovora
-
-
3-O-(3,6-anhydro-alpha-D-galactopyranosyl)-D-galactopyranose-4-O-sulfate, i.e. neocarrabiose-4-O-sufate, as the major degradation product
?
kappa-carrageenan + H2O
additional information
-
-
-
kappa-neocarratetraose
?
kappa-carrageenan + H2O
additional information
-
Cytophaga sp. 1k-C783
-
-
-
-
?
lambda-carrageenan + H2O
?
show the reaction diagram
Pseudoalteromonas porphyrae, Pseudoalteromonas porphyrae LL1
-
39.3% activity compared to kappa-carrageenan
-
-
?
additional information
?
-
-
the enzyme also catalyzes transglycosylation
-
-
-
additional information
?
-
-
raffinose and p-nitrophenyl-alpha-D-galactopyranoside are not hydrolyzed
-
-
-
additional information
?
-
Pseudomonas carrageenovora
-
induction by kappa-carrageenan
-
-
-
additional information
?
-
-
glucose, cellobiose and galactose inhibit enzyme production
-
-
-
additional information
?
-
-
hybrid kappa/iota-carrageeans extracted from Gigartina skottsbergii, Chondracanthus chamissoi, and Chondrus crispus are incubated with kappa-carrageenase. The degradation products of the kappa-carrageenase allow discriminating three modes of kappa-carrabiose distribution: blocks of kappa-carrabiose, kappa-carrabiose rich fraction containing iota-carrabiose units probably randomly distributed, and iota-carrabiose rich fraction which corresponds to the resistant fraction
-
-
-
additional information
?
-
-
isolated kappa-carrageenase can successfully generate protoplasts of Kappaphycus alvarezii. No activity with lambda-carrageenan, ioro-carrageenan and LMP agarose
-
-
-
additional information
?
-
Cytophaga sp. 1k-C783
-
glucose, cellobiose and galactose inhibit enzyme production
-
-
-
neocarrahexaitol + H2O
additional information
-
-
-
neocarrabiitol and beta-neocarratetraose are initially formed
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
kappa-carrageenan + H2O
?
show the reaction diagram
-
degradation
-
-
?
additional information
?
-
Pseudomonas carrageenovora
-
induction by kappa-carrageenan
-
-
-
additional information
?
-
Cytophaga sp., Cytophaga sp. 1k-C783
-
glucose, cellobiose and galactose inhibit enzyme production
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
116.5% activity at 10 mM
Fe2+
-
105.9% activity at 10 mM
Mg2+
-
119% activity at 10 mM
Na+
-
the activity is optimum in the presence of 50 mM NaCl
NaCl
-
optimal activity at 150 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
63.3% residual activity at 5 mM
AgNO3
-
1 mM, complete inhibition
AlCl3
-
1 mM, 39.7% inhibition
Ba2+
Tamlana sp.
-
53.25% residual activity at 1 mM
BaCl2
-
1 mM, 26.8% inhibition
Ca2+
Tamlana sp.
-
70.84% residual activity at 1 mM
Ca2+
-
96.9% residual activity at 10 mM
CaCl2
-
1 mM, 50.7% inhibition
Co2+
-
almost complete inhibition at 1 mM
Co2+
-
13.2% residual activity at 10 mM
Cu2+
Tamlana sp.
-
9.67% residual activity at 1 mM
Cu2+
-
almost complete inhibition at 1 mM
Cu2+
-
48.3% residual activity at 10 mM
CuSO4
-
1 mM, 31.3% inhibition
EDTA
Tamlana sp.
-
56.26% residual activity at 1 mM
EDTA
-
26% inhibition at 1 mM
EDTA
-
50.4% residual activity at 5 mM
EGTA
-
51.4% residual activity at 5 mM
Fe3+
Tamlana sp.
-
24.09% residual activity at 1 mM
-
Fe3+
-
11.4% residual activity at 10 mM
-
FeCl3
-
1 mM, 36.5% inhibition
Hg2+
-
3% residual activity at 10 mM
HgCl2
-
1 mM, complete inhibition
HgCl2
-
1 mM, 40.9% inhibition
iodoacetic acid
-
79.7% residual activity at 5 mM
K+
Tamlana sp.
-
49.13% residual activity at 1 mM
K+
-
96% residual activity at 10 mM
KCl
-
1 mM, 27.4% inhibition
KCl
-
1 mM, 38% inhibition
Li+
-
83.1% residual activity at 10 mM
Mg2+
Tamlana sp.
-
65.93% residual activity at 1 mM
MgCl2
-
1 mM, 15.4% inhibition
MgCl2
-
1 mM, 52.9% inhibition
Mn2+
Tamlana sp.
-
76.39% residual activity at 1 mM
Mn2+
-
2.5% residual activity at 10 mM
MnCl2
-
1 mM, 15.4% inhibition
Na+
Tamlana sp.
-
85.13%, 84.95% and 46.77% residual activity at 10, 100 and 200 mM, respectively
Na+
-
the activity is inhibited by more than 50 mM NaCl
Na+
-
90.5% residual activity at 10 mM
NaCl
-
1.5% or above, complete inhibition
NaCl
-
above 150 mM
NaI
-
strong inhibition at 200 mM, inhibition is caused by iodide binding
Ni2+
-
9.7% residual activity at 10 mM
phenylmethylsulfonyl fluoride
-
58.6% residual activity at 5 mM
SDS
-
81% inhibition at 1 mM
SDS
-
22.6% residual activity at 5 mM
Tris
-
strong inhibition at 200 mM
Zn2+
Tamlana sp.
-
16.17% residual activity at 1 mM
Zn2+
-
almost complete inhibition at 1 mM
Zn2+
-
47.3% residual activity at 10 mM
ZnCl2
-
1 mM, 50% inhibition
MnCl2
-
1 mM, 36% inhibition
additional information
-
not inhibited by Sr2+, Ba2+, K+, Ca2+, Mg2+ or Fe2+
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.244
-
kappa-carrageenan
-
-
-
additional information
-
additional information
-
Km-value for kappa-carrageenan is 6.66 mg/ml
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1
-
ZnCl2
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0774
-
Tamlana sp.
-
cell-free culture supernatant, in 25 mM Tris-HCl (pH 8.0) at 30C
6
-
-
measurement of production of reducing sugar
6.192
-
Tamlana sp.
-
after 80.38fold purification, in 25 mM Tris-HCl (pH 8.0) at 30C
19.8
-
-
crude enzyme, at pH 8.0, 55C
61
-
-
cell-free culture supernatant, in 25 mM Tris-HCl (pH 8.0) at 32C
4040
-
-
after 202.6fold purification, at pH 8.0, 55C
5778
-
-
after 95fold purification, in 25 mM Tris-HCl (pH 8.0) at 32C
additional information
-
Pseudomonas carrageenovora
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.6
-
-
and a second optimum at pH 7.7
7
-
-
in MOPS buffer
7.2
-
-
in Tris buffer
7.5
-
Pseudomonas carrageenovora
-
-
7.6
-
-
-
7.7
-
-
and a second optimum at pH 5.6
8
-
Pseudomonas carrageenovora
-
15 min assay
8
-
Tamlana sp.
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.8
9
-
pH 4.8: about 70% of maximal activity, pH 9.0: about 60% of maximal activity
5
8
-
pH 5.0: about 50% of maximal activity, pH 8.0: about 75% of maximal activity
5
9
-
broad range of activity
6
10
Pseudomonas carrageenovora
-
about 45% of maximal activity
7.4
8.4
-
about 60% of maximal activity at pH 7.4 and at pH 8.4
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
25
50
-
-
30
-
Tamlana sp.
-
-
40
-
Pseudomonas carrageenovora
-
15 min assay
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
45
-
15C: about 40% of maximal activity, 45C: about 50% of maximal activity
20
60
Pseudomonas carrageenovora
-
20C: about 60% of maximal activity, 60C: about 25% of maximal activity, 15 min assay
25
60
Tamlana sp.
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.5
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Pseudomonas carrageenovora
-
-
Manually annotated by BRENDA team
-
synthesized and released from resting cells and growing cells
Manually annotated by BRENDA team
Cytophaga sp. 1k-C783
-
synthesized and released from resting cells and growing cells
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Pseudomonas carrageenovora
-
-
-
Manually annotated by BRENDA team
Cytophaga sp. 1k-C783
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
32940
-
-
electrospray mass spectrometry
128000
-
-
gel filtrration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Pseudomonas carrageenovora
-
x * 35000, SDS-PAGE
?
-
x * 100000, SDS-PAGE
?
-
x * 35000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
?
Tamlana sp.
-
x * 66400, SDS-PAGE
?
-
x * 35000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
?
Cytophaga sp. 1k-C783
-
x * 100000, SDS-PAGE
-
?
Pseudoalteromonas porphyrae LL1
-
x * 40000, SDS-PAGE
-
?
Pseudoalteromonas sp. AJ5-1
-
x * 35000, SDS-PAGE
-
?
Tamlana sp. HC4
-
x * 66400, SDS-PAGE
-
monomer
-
1 * 128000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
processed upon secretion from a 44000 Da preproprotein to a 32000 Da secretion product, first by N-terminal removal of the 25-amino-acid signal peptide, then by cleavage of a 96-amino-acid C-terminal region from amino acids 302-397
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme expressed in Escherichia coli
-
seleno-methionyl derivative of protein
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
1 h, about 65% loss of activity
4.5
-
-
1 h, about 40% loss of activity
6
9
-
the activity of the enzyme is stable from pH 6.0 to 9.0, greater than 70.0% of the residual activity is maintained after treatment at pH from 6.0 to 9.0 and 4C for 6 h, 100% of activity is maintained after treatment at pH 8.0 and 4C for 6 h
6
-
-
1 h, about 30% loss of activity
7
-
-
1 h, stable
7.2
8.6
Tamlana sp.
-
the enzyme is stable over the range of pH 7.2-8.6 below 45C
8.5
-
-
1 h, about 50% loss of activity
9
-
-
1 h, about 75% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
50
-
the purified kappa-carrageenase is stable in the range of 0-30C and the residual enzyme activity is still retained at 96.1% of the control after treatment at 30C for 1 h. The enzyme is inactivated rapidly at temperatures higher than 30C and is almost inactivated at 50C within 1 h
5
-
Pseudomonas carrageenovora
-
stable for 2 weeks
20
-
-
40% loss of activity within 5 days, complete loss of activity within 12 days
28
75
-
the enzyme is stable at 28C, but 95% of the activity is lost at 50-75C for 30 min
30
-
-
2 h, stable
37
-
-
5 days, 50% loss of activity
40
-
Pseudomonas carrageenovora
-
stable for 3.5 h
40
-
-
stable for up to 1 h
45
60
Tamlana sp.
-
enzyme activity is stable (more than 91%) for 2 h at temperatures of above 45C. However, 90% of the activity is lost after incubation at 50-60C for 30 min
50
-
Pseudomonas carrageenovora
-
10 min, inactivated
50
-
-
15 min, more than 70% loss of activity
55
-
-
10 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
repeated freezing and thawing drastically reduces activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for at least 16 months
-
-20C, stable for several months
-
20C, 5 days, 40% loss of activity
-
frozen, stable for 15 days
-
4C, 0.2 M Tris-HCl buffer
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by metal-affinity chromatography followed by cation exchange chromatography
-
recombinant enzyme expressed in Escherichia coli
-
recombinant His-tagged enzyme from the periplasm of Escherichia coli strain BL21(DE3) by nickel affinity chromatography and cation exchange chromatography
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DEAE Sepharose column chromatography and HiTrap column chromatography
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ammonium sulfate precipitation, CM-cellulose 52 column chromatography, and Sephadex G-200 gel filtration
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Pseudomonas carrageenovora
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ammonium sulfate precipitation, Sephadex G-200 gel filtration, and DE-cellulose 52 anion-exchange chromatography
Tamlana sp.
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
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His-tagged enzyme expression in the periplasm of Escherichia coli strain BL21(DE3)
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overexpressed as a His-tagged fusion protein in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
Pseudomonas carrageenovora
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studies of carrageenan structure
molecular biology
Pseudomonas carrageenovora
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potential use in the future in the field of seaweed biotechnology for obtaining protoplasts, and in molecular biology to prevent severe separation problems occuring in the presence of phycocolloid oligomers
pharmacology
Pseudomonas carrageenovora
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potential use in the future: production of defined phycocolloid oligomers for pharmacy and immunology