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K+
Lactobacillus gayonii
-
slight activation
Sr2+
Lactobacillus gayonii
-
slight activation
Ba2+
activating
Ba2+
inhibits galactose isomerization, remaining activity 94%
Ba2+
120% activity at 1 mM
Ca2+
serves as catalyst
Ca2+
the addition of Ca2+ has slightly positive but no significant effect on the enzyme activity
Ca2+
106% of the activity with Mn2+
Ca2+
-
serves as catalyst
Ca2+
enhances galactose isomerization by 12%
Ca2+
-
the most effective enzyme activator with the reaction rate by 150%
Ca2+
Halalkalibacterium halodurans
serves as catalyst
Ca2+
-
serves as catalyst
Ca2+
Lactobacillus gayonii
-
serves as catalyst
Ca2+
-
serves as catalyst
Ca2+
-
serves as catalyst
Ca2+
-
serves as catalyst
Ca2+
-
serves as catalyst
Co2+
activates and increase thermostability of the enzyme
Co2+
1 mM required for activity
Co2+
3fold increase in activity, assay in presence of 0.5 mM
Co2+
-
or Mn2+, required. 443% of initial activity at 1 mM
Co2+
-
does not restore activity after dialysis with EDTA
Co2+
-
60% activation compared to Mn2+
Co2+
activating, highest activity of the mutated enzyme at 1.0 mM
Co2+
increase in activity at 80°C only, no effect at 65°C
Co2+
enhances galactose isomerization by 11%, maximum activity occurs at 3 mM Mn2+
Co2+
required for maximal activity and stability
Co2+
Lactobacillus gayonii
-
slight activation
Co2+
Lactobacillus gayonii
-
activates to about half the extent of Mn2+
Co2+
201% activity at 1 mM, Co2+ is required for enzymatic activity and thermostability
Co2+
-
Mn2+, Mg2+ or Co2+ required
Co2+
this enzyme exhibits a weak requirement for metal ions for its maximal activity evaluated at 0.6 mM Mn2+ and 0.8 mM Co2+ (115.38% activity in the presence of Mn2+ and Co2+)
Co2+
1 mM, 4.2fold activation
Co2+
-
restores activity after dialysis against EDTA
Co2+
addition of CoSO4 reactivates the enzyme to 45% after inactivation with EDTA
Co2+
-
improves the enzymatic activity to 121% at 5 mM
Co2+
0.05 mM Co2+, can improve both catalytic activity and thermostability at higher temperatures
Co2+
-
Mn2+ or Co2+ required, about 1 mM Co2+ restores activity of dialyzed enzyme
Co2+
-
preferred cofactor
Co2+
-
divalent cation, maximal activity in presence of both Mn2+ and Co2+
Co2+
-
1mM for the free enzyme and for the immobilized enzyme in Escherichis coli cells
Co2+
-
the enzyme activity is significantly increased by adding 1 mM Co2+ (2.9fold)
Co2+
0.5 mM, 190% of the activity of EDTA-treated enzyme
Co2+
1 mM, 110% of initial activity
Cu2+
inhibitory
Cu2+
inhibits galactose isomerization remaining activity 42%
Fe2+
activating
Fe2+
-
106% relative activity at 1 mM
Fe2+
inhibits galactose isomerization remaining activity 98%
Fe2+
addition of FeSO4 reactivates the enzyme to 76% after inactivation with EDTA
Mg2+
1 mM required for activity
Mg2+
-
240% of initial activity at 1 mM
Mg2+
the addition of Mg2+ has slightly positive but no significant effect on the enzyme activity
Mg2+
117% of the activity with Mn2+
Mg2+
-
50% activation compared to Mn2+
Mg2+
enhances galactose isomerization by 9%
Mg2+
-
the enzyme has low metal requirement of only 0.8 mM Mg2+ for its maximal activity and thermostability. At 35°C, the addition of 1 mM Mg2+ to the EDTA-treated enzyme increases the specific activity from 65 to 201 units/mg
Mg2+
-
the enzyme activity is increased nearly 1.8fold after addition of 0.8 mM Mg2+
Mg2+
-
Mg2+, Mn2+ or Co2+ required
Mg2+
1 mM, 120% of initial activity
Mn2+
activates and increase thermostability of the enzyme
Mn2+
1 mM required for activity
Mn2+
3fold increase in activity, assay in presence of 1 mM
Mn2+
-
or Co2+, required. 497% of initial activity at 1 mM
Mn2+
required, 42% activation at 1 mM
Mn2+
-
essential for catalysis, but also competitive inhibitor for L-arabinose
Mn2+
-
restores activity after dialysis against EDTA
Mn2+
activates the enzyme
Mn2+
-
used in assay conditions
Mn2+
-
required for activity
Mn2+
presence of Mn2+ stabilizes protein 1.9- and 9fold at 60°C and 70°C, respectively
Mn2+
-
strong activator, approximately 0.06 eqiuvalents of Mn2+/subunit
Mn2+
activating, highest activity of the wild type enzyme at 1.0 mM
Mn2+
increase in activity at 80°C only, no effect at 65°C
Mn2+
is closely bound to the protein even after treatment with EDTA
Mn2+
-
404% relative activity at 1 mM, the enzyme has an absolute requirement for the divalent metal ion Mn2+ for both catalytic activity and thermostability
Mn2+
-
about 2fold increase in activity at 1 mM Mn2+
Mn2+
-
the enzyme is not metal-dependent for catalytic activity but Mn2+ significantly enhances the activity of its apo enzyme and increases thermostability
Mn2+
required to achieve maximum activity, competitive activator, increases thermal stability of AI, enhances galactose isomerization by 34%, maximum activity occurs at 5 mM Mn2+
Mn2+
Halalkalibacterium halodurans
-
approximately 0.06 eqiuvalents of Mn2+/subunit
Mn2+
-
activates the enzyme
Mn2+
required for maximal activity and stability
Mn2+
Lactobacillus gayonii
-
required
Mn2+
Lactobacillus gayonii
-
required, Km: 0.00525 mM
Mn2+
Lactobacillus gayonii
-
activates the enzyme
Mn2+
-
the enzyme has low metal requirement of only 0.8 mM Mn2+ for its maximal activity and thermostability (above 35°C). At 35°C, the addition of 1 mM Mn2+ to the EDTA-treated enzyme increases the specific activity from 65 to 204 units/mg
Mn2+
-
the enzyme activity is increased nearly 1.8fold after addition of 0.8 mM Mn2+
Mn2+
298% activity at 1 mM, Mn2+ is required for enzymatic activity and thermostability
Mn2+
-
Mn2+, Mg2+ or Co2+ required
Mn2+
activates 2.5fold at 1 mM
Mn2+
this enzyme exhibits a weak requirement for metall ions for its maximal activity evaluated at 0.6 mM Mn2+ and 0.8 mM Co2+ (115.38% activity in the presence of Mn2+ and Co2+)
Mn2+
1 mM, 3.4fold activation
Mn2+
-
restores activity after dialysis against EDTA
Mn2+
addition of MnCl2 reactivates the enzyme to 100% after inactivation with EDTA
Mn2+
-
highest activity with Mn2+. The optimum Mn2+ concentration for the free and calcium alginate-immobilized enzyme is 5 mM (132% activity)
Mn2+
0.1 mM Mn2+,increases activity to 167.3% and can improve both catalytic activity and thermostability at higher temperatures
Mn2+
-
Mn2+ or Co2+ required, about 5 mM Mn2+ restores activity of dialyzed enzyme
Mn2+
-
the enzyme is not metal-dependent for catalytic activity but Mn2+ significantly (3fold) enhances the activity of its apo enzyme and increases thermostability
Mn2+
-
divalent cation, maximal activity in presence of both Mn2+ and Co2+
Mn2+
-
1mM for the free enzyme, 10 mM for the immobilized enzyme in Escherichis coli cells
Mn2+
-
best activator for enzymatic activity and thermostability. The enzyme activity is significantly increased by adding 1 mM Mn2+ (4.3fold)
Mn2+
0.5 mM, 270% of the activity of EDTA-treated enzyme
Mn2+
1 mM, 111% of initial activity
Ni2+
about 135% activity at 1 mM
Zn2+
-
307% of initial activity at 1 mM
Zn2+
129% activity at 1 mM
Zn2+
-
improves the enzymatic activity to 115% at 5 mM
additional information
metal ions are essential for catalytic activity, but metal ions, such as Mg2+, Ni2+, and Ba2+, are poor activators, while Fe2+, Ca2+, and Zn2+ have no effect on the activity
additional information
-
metal ions are essential for catalytic activity, but metal ions, such as Mg2+, Ni2+, and Ba2+, are poor activators, while Fe2+, Ca2+, and Zn2+ have no effect on the activity
additional information
the enzyme is not dependent on divalent metal ions, since it is only marginally activated by Mg2+, Mn2+ or Ca2+
additional information
-
the enzyme is not dependent on divalent metal ions, since it is only marginally activated by Mg2+, Mn2+ or Ca2+
additional information
-
no stimulation by Ca2+, Ba2+, Fe2+, Hg2+, or Cu2+ at 1 mM each
additional information
the enzyme is not stimulated by Mg2+, Ca2+, Zn2+, Fe2+, or Ni2+ at 1 mM each, and is unaffected by EDTA at concentrations ranging from 1 to 10 mM
additional information
-
the enzyme is not stimulated by Mg2+, Ca2+, Zn2+, Fe2+, or Ni2+ at 1 mM each, and is unaffected by EDTA at concentrations ranging from 1 to 10 mM
additional information
the enzyme has very low requirement for metal ions for catalytic activity, but it is stabilized by divalent metal ions (Mg2+, Mn2+)
additional information
-
the enzyme has very low requirement for metal ions for catalytic activity, but it is stabilized by divalent metal ions (Mg2+, Mn2+)
additional information
-
activity and thermostability are totally independent of metallic ions up to 65°C, above 65°C, the enzyme's activity is also independent of metallic ions of its activity, but its thermostability is improved in the presence of only 0.2 mM Co2+ and 1 mM Mn2+
additional information
activity and thermostability are totally independent of metallic ions up to 65°C, above 65°C, the enzyme's activity is also independent of metallic ions of its activity, but its thermostability is improved in the presence of only 0.2 mM Co2+ and 1 mM Mn2+
additional information
-
Ca2+, Ni2+, Zn2+, Mg2+, Fe2+, Cu2+ show no effect
additional information
Ca2+, Ni2+, Zn2+, Mg2+, Fe2+, Cu2+ show no effect
additional information
-
not significantly stimulated by Mg2+
additional information
the enzyme has no activity in the absence of metal ions
additional information
-
the enzyme has no activity in the absence of metal ions
additional information
Halalkalibacterium halodurans
-
the conversion of D-galactose into D-tagatose is not dependent on divalent metal ions
additional information
-
the enzyme is not affected by Zn2+, Ca2+, Co2+, Fe2+, and Ba2+
additional information
not influenced by Ca2+ and Ni2+
additional information
not influenced by Mg2+ and Ca2+
additional information
-
not influenced by Mg2+ and Ca2+
additional information
-
not activated by Mg2+, Fe2+, and Ca2+
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K269E
pH optimum shifts from pH 6 to 7
M33R
-
the mutant has the pH optimum of stability shifted upward from acidic to basic pH
Q202R
-
the mutant has the pH optimum of stability shifted upward from acidic to basic pH
V50R
-
the mutant has the pH optimum of stability shifted upward from acidic to basic pH
Y218R
-
the mutant has the pH optimum of stability shifted upward from acidic to basic pH
D478A
mutant retains more than 80 % of the maximum relative activity of the wild-type at 75°C
D478K
mutant displays a decreased optimum pH value
D478N
mutant shows increased activity for D-galactose isomerization and retains more than 80 % of the maximum relative activity of the wild-type at 75°C. Mutant displays a decreased optimum pH value
D478Q
mutant shows increased activity for D-galactose isomerization and retains more than 80 % of the maximum relative activity of the wild-type at 75°C and displays a decreased optimum pH value
D478R
mutant displays a decreased optimum pH value
D478A
-
mutant retains more than 80 % of the maximum relative activity of the wild-type at 75°C
-
D478K
-
mutant displays a decreased optimum pH value
-
D478N
-
mutant shows increased activity for D-galactose isomerization and retains more than 80 % of the maximum relative activity of the wild-type at 75°C. Mutant displays a decreased optimum pH value
-
D478Q
-
mutant shows increased activity for D-galactose isomerization and retains more than 80 % of the maximum relative activity of the wild-type at 75°C and displays a decreased optimum pH value
-
D478R
-
mutant displays a decreased optimum pH value
-
R200E
-
the mutant has the pH optimum of stability shifted downward from basic to acidic pH
R216E
-
the mutant has the pH optimum of stability shifted downward from basic to acidic pH
R31E
-
the mutant has the pH optimum of stability shifted downward from basic to acidic pH
R48E
-
the mutant has the pH optimum of stability shifted downward from basic to acidic pH
R200E
-
the mutant has the pH optimum of stability shifted downward from basic to acidic pH
-
R216E
-
the mutant has the pH optimum of stability shifted downward from basic to acidic pH
-
R31E
-
the mutant has the pH optimum of stability shifted downward from basic to acidic pH
-
R48E
-
the mutant has the pH optimum of stability shifted downward from basic to acidic pH
-
I370A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
L345A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
M185A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
M349A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
T276A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
W439A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
Y333A
site-directed mutagenesis, the catalytic site mutant shows 97.2% reduced activity compared to the wild-type enzyme
Y333D
site-directed mutagenesis, the catalytic site mutant shows no activity
Y333E
site-directed mutagenesis, the catalytic site mutant shows no activity
Y333I
site-directed mutagenesis, the catalytic site mutant shows 72% reduced activity compared to the wild-type enzyme
Y333K
site-directed mutagenesis, the catalytic site mutant shows no activity
Y333V
site-directed mutagenesis, the catalytic site mutant shows 82% reduced activity compared to the wild-type enzyme
Y333X
replacing Y333 with the aromatic amino acid Phe does not alter catalytic efficiency toward L-arabinose. In contrast, the activities of mutants containing a hydrophobic amino acid, Ala, Val, or Leu, decrease as the size of the hydrophobic side chain of the amino acid decreases. However, mutants containing hydrophilic and charged amino acids, such as Asp, Glu, and Lys, show almost no activity with L-arabinose
H347A
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
H446A
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
H446A
-
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
-
G270D
-
the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
L282M
-
the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
Q299K
-
mutant displays similar optimum conditions as beta-galactosidase
R25C
-
the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
T451P
-
the enzyme shows 31% increased activity compared to the wild type enzyme
Y496C
-
the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
A408V
site directed mutagenesis
A408V/K475N
site directed mutagenesis
A475N
site directed mutagenesis
D118V
-
the mutant shows 42% of wild type activity
D195V
-
the mutant shows 29% of wild type activity
D228N
site directed mutagenesis
D228N/D384G/T393S/N428K/K475N
site directed mutagenesis, GSAI 152
D308A
site directed mutagenesis
D309V
-
the mutant shows 78% of wild type activity
D333V
-
the mutant shows 40% of wild type activity
D384G
site directed mutagenesis
E133L
-
the mutant shows 65% of wild type activity
E233L
-
the mutant shows wild type activity
E261L
-
the mutant shows 29% of wild type activity
E306A
site directed mutagenesis, no activity
E331A
site directed mutagenesis, no activity
E332L
-
the mutant shows 67% of wild type activity
E351A
site directed mutagenesis
F279Q
site directed mutagenesis
F329A
site directed mutagenesis
G408V
site directed mutagenesis
H175N
-
the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
H348A
site directed mutagenesis, no activity
H446A
site directed mutagenesis
H447A
site directed mutagenesis, no activity
K196F
-
the mutant shows 56% of wild type activity
K475N
site directed mutagenesis
L408V
site directed mutagenesis
M322V/S393T/V408A
error prone PCR mutagenesis using gali 152 as template, gali 153 with changes in 3 amino acids revealed a higher activity than gali 152
N175H
site-directed mutagenesis, the N175H mutant has a broad optimal temperature range from 50 to 65°C
N406L
-
the mutant shows 57% of wild type activity
N428K
site directed mutagenesis
Q268K/H175N
-
the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
Q268K/N175H
site-directed mutagenesis, the Q268K mutant is more acidotolerant, the N175H mutant has a broad optimal temperature range from 50 to 65°C
Q408V
site directed mutagenesis
Q475N
site directed mutagenesis
R408V
site directed mutagenesis
R475N
site directed mutagenesis
T393S
site directed mutagenesis
V322M
site directed mutagenesis
V322M/T393S/A408V
site directed mutagenesis, GSAI 153
M322V/S393T/V408A
-
error prone PCR mutagenesis using gali 152 as template, gali 153 with changes in 3 amino acids revealed a higher activity than gali 152
-
H175N
-
the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
-
N175H
-
site-directed mutagenesis, the N175H mutant has a broad optimal temperature range from 50 to 65°C
-
Q268K/H175N
-
the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
-
Q268K/N175H
-
site-directed mutagenesis, the Q268K mutant is more acidotolerant, the N175H mutant has a broad optimal temperature range from 50 to 65°C
-
C450S
site directed mutagenesis
F280N/C450S/N475K
mutat catalyzes the isomerization of D-galactose to D-tagatose
G384D
site directed mutagenesis
K320R
site directed mutagenesis
K320R/N475K
site directed mutagenesis
K428N
site directed mutagenesis
K428N/N475K
site directed mutagenesis
M322V
site directed mutagenesis
N228D
site directed mutagenesis
N475K
site directed mutagenesis
N475Q
site directed mutagenesis
N475R
site directed mutagenesis
S393T
site directed mutagenesis
V408A
site directed mutagenesis
V408A/N475K
site directed mutagenesis
W164G
site directed mutagenesis
W17Q/N90A/L129F
-
about 30% increase in specific activity
Y164F
site directed mutagenesis
Y164G
site directed mutagenesis
Y164H
site directed mutagenesis
E268K
Halalkalibacterium halodurans
-
pH optimum shifts from pH 8 to 7
D268E
the mutant shows 58% activity compared to the wild type enzyme
D268K
the mutant shows 48% activity compared to the wild type enzyme
D268K/D269K
the mutant shows 65% activity compared to the wild type enzyme
D268K/D269K/D299K
the mutant with 115% activity compared to the wild type enzyme exhibits significant optimum pH shifts (from 6.5 to 5.0) and enhancement of pH stability (half-life time increased from 30 to 62 h at pH 6.0). With the addition of borate, D-galactose is isomerized into D-tagatose by this mutant at pH 5.0, resulting in a high conversion rate of 62%
D268K/D299K
the mutant shows 42% activity compared to the wild type enzyme
D268R
the mutant shows 88% activity compared to the wild type enzyme
D269E
the mutant shows 62% activity compared to the wild type enzyme
D269K
the mutant shows 130% activity compared to the wild type enzyme
D269K/D299K
the mutant shows 84% activity compared to the wild type enzyme
D269R
the mutant shows 88% activity compared to the wild type enzyme
D299E
the mutant shows 109% activity compared to the wild type enzyme
D299K
the mutant shows 90% activity compared to the wild type enzyme
D299R
the mutant shows 68% activity compared to the wild type enzyme
D268E
-
the mutant shows 58% activity compared to the wild type enzyme
-
D268K
-
the mutant shows 48% activity compared to the wild type enzyme
-
D268K/D269K/D299K
-
the mutant with 115% activity compared to the wild type enzyme exhibits significant optimum pH shifts (from 6.5 to 5.0) and enhancement of pH stability (half-life time increased from 30 to 62 h at pH 6.0). With the addition of borate, D-galactose is isomerized into D-tagatose by this mutant at pH 5.0, resulting in a high conversion rate of 62%
-
D268R
-
the mutant shows 88% activity compared to the wild type enzyme
-
D269E
-
the mutant shows 62% activity compared to the wild type enzyme
-
E305A
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
E305A
site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme
E330A
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
E330A
site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme
E305A
-
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
-
E305A
-
site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme
-
E330A
-
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
-
E330A
-
site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme
-
Q268K
site-directed mutagenesis, the mutant enzyme shows increased acidotolerance and is more stable at acidic pH than the wild-type enzyme
Q268K
-
the mutant shows a pH optimum of 6.0-6.5 and a higher stability at acidic pH compared to the wild type enzyme, the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
Q268K
-
the mutant shows a pH optimum of 6.0-6.5 and a higher stability at acidic pH compared to the wild type enzyme, the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
-
Q268K
-
site-directed mutagenesis, the mutant enzyme shows increased acidotolerance and is more stable at acidic pH than the wild-type enzyme
-
C450S/N475K
site directed mutagenesis, 20% higher tagatose conversion than the wild type enzyme
C450S/N475K
-
mutant strain is able to produce 95 g L-ribulose per l from 500 g L-arabinose per l under optimum conditions of pH 8, 70°C, and 10 units enzyme per ml with a conversion yield of 19% over 2 h. The half-lives of the mutated enzyme at 70 and 75°C are 35 and 4.5 h, respectively
C450S/N475K
mutant catalyzes the isomerization of D-galactose to D-tagatose
additional information
-
immobilization of Escherichia coli cells, recombinantly expressing the L-arabinose isomerase from Bacillus licheniformis, on alginate stabilizes the cells, optimal at 2% w/v alginate, 0.1 M Ca2+, 50 g/l cell mass, and 4 h curing time, 89% remaining enzyme activity after 33 days at 50°C
additional information
-
immobilization of the enzyme on different matrices, e.g. activated carboxymethylcellulose, Eupergit C, CNBr-activated agarose, chitosan, and alginate, for semi-continous production of L-ribulose, method optimization, overview. 85.1% remaining activity after 8 cycles and 86.4% activity compared to the wild-type enzyme
additional information
expression of N- and C-terminal His-tagged protein in Escherichia coli. The C-His-tagged enzyme is preferentially hexameric in solution, whereas the N-His-tagged protein is mainly monomeric. The N-His-tagged variant shows a maximum bioconversion yield of 26% at 50°C for D-tagatose biosynthesis, the C-His-tagged variant is more active and stable at alkaline pH than the N-His-tagged variant
additional information
-
expression of N- and C-terminal His-tagged protein in Escherichia coli. The C-His-tagged enzyme is preferentially hexameric in solution, whereas the N-His-tagged protein is mainly monomeric. The N-His-tagged variant shows a maximum bioconversion yield of 26% at 50°C for D-tagatose biosynthesis, the C-His-tagged variant is more active and stable at alkaline pH than the N-His-tagged variant
additional information
-
expression of N- and C-terminal His-tagged protein in Escherichia coli. The C-His-tagged enzyme is preferentially hexameric in solution, whereas the N-His-tagged protein is mainly monomeric. The N-His-tagged variant shows a maximum bioconversion yield of 26% at 50°C for D-tagatose biosynthesis, the C-His-tagged variant is more active and stable at alkaline pH than the N-His-tagged variant
-
additional information
-
mutation results in a change in the structure of isomerase which causes thermolability
additional information
-
mutation results in a change in the structure of isomerase which causes thermolability
-
additional information
-
five point mutations increase the activity 11fold in the first round of evolution, and three point mutations in the second round of evolution increase the activity 5fold beyond the activity from the first round
additional information
construction of three Bacillus stearothermophilus US100 L-arabinose isomerase mutants with increased activity for D-galactose and increased D-tagatose production
additional information
-
construction of three Bacillus stearothermophilus US100 L-arabinose isomerase mutants with increased activity for D-galactose and increased D-tagatose production
additional information
evaluation and optimization of Escherichia coli and Bacilus subtilis expression systems for toxic byproducts in L-ribulose and/or D-tagatose production by the recombinant engineered enzyme
additional information
-
construction of three Bacillus stearothermophilus US100 L-arabinose isomerase mutants with increased activity for D-galactose and increased D-tagatose production
-
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food industry
production of D-tagatose
food industry
production of D-tagatose
food industry
-
production of D-tagatose
food industry
production of D-tagatose as a low-calorie sugar-substituting sweetener
food industry
production of D-tagatose as a low-calorie sugar-substituting sweetener
food industry
production of D-tagatose as a low-calorie sugar-substituting sweetener
food industry
production of D-tagatose as a low-calorie sugar-substituting sweetener lower pH is preferable for industrial production
food industry
-
production of D-tagatose as a low-calorie sugar-substituting sweetener, reactor was run for 50 days
food industry
production of D-tagatose as a low-calorie sugar-substituting sweetener, the D-tagatose yield from the mutated enzyme is higher than from the wild type
food industry
-
hyperthermophilic L-arabinose isomerase is useful in the commercial production of D-tagatose as a low-calorie bulk sweetener
food industry
-
hyperthermophilic L-arabinose isomerase is useful in the commercial production of D-tagatose as a low-calorie bulk sweetener
food industry
-
production of D-tagatose as a low-calorie sugar-substituting sweetener
-
food industry
-
production of D-tagatose as a low-calorie sugar-substituting sweetener, the D-tagatose yield from the mutated enzyme is higher than from the wild type
-
industry
a novel way of producing L-ribose from the readily available raw material L-arabinose is described
industry
-
a novel way of producing L-ribose from the readily available raw material L-arabinose is described
-
nutrition
-
the enzyme may be a good model for analysis of metal-mediated thermostabilization and for industrial application in the production of D-tagatose as a novel sweetener
nutrition
AI from Bacillus thermodenitrificans can be useful for the industrial production of D-tagatose because its optimum temperature is the highest reported for thermophilic AIs and because its activity does not require the addition of Co2+
nutrition
the product D-tagatose is currently introduced as a low-calorie bulk sweetener
nutrition
-
the product D-tagatose is used as a low-calorie bulk sweetener
nutrition
-
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
-
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
Lactobacillus gayonii
-
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
-
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
-
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
-
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
Halalkalibacterium halodurans
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
-
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
-
when mice are fed with a lactobacillus lactis strain secreting the enzyme and galactose, tagatose is produced in vivo and reduces the glycemia index
synthesis
-
an Escherichia coli galactose kinase gene knockout strain, which contains the L-arabinose isomerase gene to isomerize D-galactose to D-tagatose, shows a higher conversion yield of tagatose because galactose is not metabolized by endogenous galactose kinase. In whole cells of the galactose kinase knockout strain, the isomerase-catalyzed reaction exhibits an equilibrium shift towards tagatose, producing a tagatose fraction of 68% at 37°C, whereas the purified L-arabinose isomerase gives a tagatose equilibriumfraction of 36%
synthesis
-
expression of the Escherichia coli genes araA, araB, and araD encoding L-arabinose isomerase, L-ribulokinase, and L-ribulose-5-phosphate 4-epimerase, respectively, in Corynebacterium glutamicum under the control of a constitutive promoter. The recombinant strain is able to grow on mineral salts medium containing L-arabinose as the sole carbon and energy source. Under oxygen deprivation and with L-arabinose as the sole carbon and energy source, carbon flow of the recombinant strain is redirected to produce up to 40, 37, and 11%, respectively, of the theoretical yields of succinic, lactic, and acetic acids. Usinga sugar mixture containing 5% D-glucose and 1% L-arabinose under oxygen deprivation, cells metabolize L-arabinose at a constant rate, resulting in combined organic acids yield based on the amount of sugar mixture consumed after D-glucose depletion of 83% that is comparable to that before D-glucose depletion, 89%
synthesis
-
production of D-tagatose from D-galactose by L-arabinose isomerase immobilized on chitopearl beads. Half-lives of immobilized enzyme at 70°C, 75°C, 80°C, 85°C and 90°C are 388, 106, 54, 36, and 22 h, respectively. With pH control at 7.5, D-tagatose production at 70°C in a stirred tank reactor doubles compared to conditions without pH control
synthesis
-
production of ethanol after improvement of a bacterial L-arabinose utilization pathway consisting of L-arabinose isomerase from Bacillus licheniformis and L-ribulokinase and L-ribulose-5-phosphate-4-epimerase from Escherichia coli after expression of the corresponding genes in Saccharomyces cerevisiae.Yeast transformants expressing the codon-optimized genes show strongly improved L-arabinose conversion rates. The ethanol production rate from L-arabinose can be increased more than 2.5fold from 0.014 g ethanol per h and g dry weight to 0.036 g ethanol per h and g dry weight and the ethanol yield can be increased from 0.24 g ethanol per g consumed L-arabinose to 0.39 g ethanol per g consumed L-arabinose
synthesis
-
production of the intracellular enzymes L-arabinose isomerase and D-xylose isomerase in Lactobacillus bifermentans. After 9 h cultivation in optimized medium, Arabinose isomerase and xylose isomerase activities are 9.4 and 7.24 U/ml, respectively. For optimal growth, the strain requires Tween 80 at 1 g/l and a source of inorganic nitrogen, e.g., ammonium citrate. The bacterium has no requirement for sodium acetate for either growth or production of isomerases. The production rate of enzymes is increased when metal ions are added, primarily manganese
synthesis
-
strain carrying mutant C450S/N475K is able to produce 95 g L-ribulose per l from 500 g L-arabinose per l under optimum conditions of pH 8, 70°C, and 10 units enzyme per ml with a conversion yield of 19% over 2 h. The half-lives of the mutated enzyme at 70 and 75°C are 35 and 4.5 h, respectively
synthesis
-
alginate-immobilized Escherichia coli cells, recombinantly expressing the L-arabinose isomerase from Bacillus licheniformis, shows high stability and are suitable for L-ribulose production at low costs
synthesis
engineered enzyme mutants are useful for production of D-tagatose
synthesis
-
L-ribose production of the enzyme in a coupled assay system with mannose-6-phosphate isomerase, EC 5.3.1.8, in recombinant Escherichia coli ER2566, AI/MPI ratio, 1:2.5, method optimization. L-Ribose is a potential starting material for the synthesis of many L-nucleoside-based pharmaceutical compounds
synthesis
the enzyme is useful in production of low-calorie sweetener D-tagatose. Tagatose also may potentially be useful as a prescription drug additive, to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavored lipstick
synthesis
-
the enzyme is a biocatalyst for the production of L-ribulose
synthesis
-
the enzyme is used for the commercial production of D-tagatose
synthesis
-
coexpression of beta-D-galactosidase gene and L-arabinose isomerase mutant Q299K for synthesis of D-tagatose. Recombinant cells exhibit maximum D-tagatose producing activity at 34°C and pH 6.5 and in the presence of borate, 10 mM Fe2+, and 1 mM Mn2+. Cells can hydrolyze more than 95% lactose and convert 43% D-galactose into D-tagatose
synthesis
coexpression with a thermostable beta-galactosidase from Thermus thermophilus HB27 in Escherichia coli. The recombinant cells show optimal catalytic temperature and pH at 70°C and 7.0, respectively. With the addition of borate, D-tagatose is produced directly from lactose in 16 h in a concentration of 101 g/l, a yield of 20.2%, and a productivity of 6.3 g/l/h
synthesis
-
enzyme is displayed on the spore surface of Bacillus subtilis DB403 by using an anchoring protein and a peptide linker. This displayed protein shows high specific activity and stability and is used as a immobilized biocatalyst for producing D-tagatose through batch and semi-continuous biotransformation. The conversion rate of D-tagatose from 125 g/l D-galactose achieved 79.7% at 28 h, and the volumetric productivity reaches 4.3 g/l/h at 20 h with good reusability
synthesis
-
expression of L-arabinose isomerase in fusion with the signal peptide of usp45 leads to secretion of the enzyme in induced cultures. Secretion is imrpoved by use of Lactobacillus lactis strains deficient for major proteases, ClpP and HtrA, or by use of an enhancer of protein secretion in Lactobacillus lactis fused to the recombinant isomerase gene fused to the signal peptide
synthesis
-
production of ribose by immobilized recombinant Escherichia coli cells expressing the L-arabinose isomerase gene and mannose-6-phosphate isomerase mutant W17Q/N90A/L129F. The immobilized cells produce 99 g/l L-ribose from 300 g/l L-arabinose in 3 h at pH 7.5 and 60 °C in the presence of 1 mM Co2+, with a conversion yield of 33 % (w/w) and a productivity of 33 g/l/h
synthesis
under optimal conditions, recombinant Escherichia coli cells expressing AraA can convert 150 g/l and 250 g/l D-galactose to D-tagatose with conversion rates of 32% (32 h) and 27% (48 h)
synthesis
-
the enzyme is used for the commercial production of D-tagatose
-
synthesis
-
enzyme is displayed on the spore surface of Bacillus subtilis DB403 by using an anchoring protein and a peptide linker. This displayed protein shows high specific activity and stability and is used as a immobilized biocatalyst for producing D-tagatose through batch and semi-continuous biotransformation. The conversion rate of D-tagatose from 125 g/l D-galactose achieved 79.7% at 28 h, and the volumetric productivity reaches 4.3 g/l/h at 20 h with good reusability
-
synthesis
-
under optimal conditions, recombinant Escherichia coli cells expressing AraA can convert 150 g/l and 250 g/l D-galactose to D-tagatose with conversion rates of 32% (32 h) and 27% (48 h)
-
synthesis
-
engineered enzyme mutants are useful for production of D-tagatose
-
synthesis
-
coexpression with a thermostable beta-galactosidase from Thermus thermophilus HB27 in Escherichia coli. The recombinant cells show optimal catalytic temperature and pH at 70°C and 7.0, respectively. With the addition of borate, D-tagatose is produced directly from lactose in 16 h in a concentration of 101 g/l, a yield of 20.2%, and a productivity of 6.3 g/l/h
-
additional information
-
additionally, D-tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
-
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
Lactobacillus gayonii
-
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
-
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
-
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
-
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
Halalkalibacterium halodurans
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
-
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LeBlanc, D.J.; Mortlock, R.P.
Regulation of the L-arabinose catabolic pathway in Aerobacter aerogenes
Arch. Biochem. Biophys.
156
390-396
1973
Klebsiella aerogenes
brenda
Sa-Nogueira, I.; Nogueira, T.V.; Soares, S.; de Lencastre, H.
The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression
Microbiology
143
957-969
1997
Bacillus subtilis, Escherichia coli
brenda
Heath, E.C.; Horecker, B.L.; Smyrniotis, P.Z.; Takagi, Y.
Pentose fermentation by Lactobacillus plantarum. II. L-Arabinose isomerase
J. Biol. Chem.
231
1031-1037
1958
Lactiplantibacillus plantarum
brenda
Nakamatu, T.; Yamanaka, K.
Crystallization and properties of L-arabinose isomerase from Lactobacillus gayonii
Biochim. Biophys. Acta
178
156-165
1969
Lactobacillus gayonii
brenda
Pauley, J.; Power, J.; Irr, J.
L-Arabinose isomerase formation in a conditional mutant of gene araA of Escherichia coli B/r
J. Bacteriol.
112
1247-1253
1972
Escherichia coli, Escherichia coli B/r
brenda
Yamanka, K.; Izumori, K.
Purification and properties of L-arabinose isomerase from Streptomyces sp.
Agric. Biol. Chem.
37
521-526
1973
Streptomyces sp.
-
brenda
Patrick, J.; Lee, N.
L-Arabinose isomerase
Methods Enzymol.
41B
453-458
1975
Escherichia coli, Escherichia coli B/r
brenda
Yamanaka, K.
L-Arabinose isomerase from Lactobacillus gayonii
Methods Enzymol.
41B
458-461
1975
Lactobacillus gayonii
brenda
Izumori, K.; Ueda, Y.; Yamanaka, K.
Pentose metabolism in Mycobacterium smegmatis: comparison of L-arabinose isomerase induced by L-arabinose and D-galactose
J. Bacteriol.
133
413-414
1978
Mycolicibacterium smegmatis
brenda
Wallace, L.J.; Eiserling, F.A.; Wilcox, G.
The shape of L-arabinose isomerase from Escherichia coli
J. Biol. Chem.
253
3717-3720
1978
Escherichia coli
brenda
Lin, H.C.; Lei, S.P.; Wilcox, G.
The araBAD operon of Salmonella typhimurium LT2. II. Nucleotide sequence of araA and primary structure of its product, L-arabinose isomerase
Gene
34
123-128
1985
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Sa-Nogueira, I.; Paveia, H.; De Lencastre, H.
Isolation of constitutive mutants for L-arabinose utilization in Bacillus subtilis
J. Bacteriol.
170
2855-2857
1988
Bacillus subtilis
brenda
Deanda, K.; Zhang, M.; Eddy, C.; Picataggio, S.
Development of an arabinose-fermenting Zymomonas mobilis strain by metabolic pathway engineering
Appl. Environ. Microbiol.
62
4465-4470
1996
Escherichia coli
brenda
Banerjee, S.; Anderson, F.; Farber, G.K.
The evolution of sugar isomerases
Protein Eng.
8
1189-1195
1995
Escherichia coli
brenda
Lee, D.W.; Jang, H.J.; Choe, E.A.; Kim, B.C.; Lee, S.J.; Kim, S.B.; Hong, Y.H.; Pyun, Y.R.
Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima
Appl. Environ. Microbiol.
70
1397-1404
2004
Thermotoga maritima
brenda
Kim, B.C.; Lee, Y.H.; Lee, H.S.; Lee, D.W.; Choe, E.A.; Pyun, Y.R.
Cloning, expression and characterization of L-arabinose isomerase from Thermotoga neapolitana: bioconversion of D-galactose to D-tagatose using the enzyme
FEMS Microbiol. Lett.
212
121-126
2002
Thermotoga neapolitana, Thermotoga neapolitana 5068
brenda
Lee, S.J.; Lee, D.W.; Choe, E.A.; Hong, Y.H.; Kim, S.B.; Kim, B.C.; Pyun, Y.R.
Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum
Appl. Environ. Microbiol.
71
7888-7896
2005
Halalkalibacterium halodurans, Alicyclobacillus acidocaldarius (Q2VMT2), Alicyclobacillus acidocaldarius
brenda
Jorgensen, F.; Hansen, O.C.; Stougaard, P.
Enzymatic conversion of D-galactose to D-tagatose: heterologous expression and characterisation of a thermostable L-arabinose isomerase from Thermoanaerobacter mathranii
Appl. Microbiol. Biotechnol.
64
816-822
2004
Thermotoga maritima, Thermoanaerobacter mathranii (Q70G56), Thermoanaerobacter mathranii
brenda
Kim, P.
Current studies on biological tagatose production using L-arabinose isomerase: a review and future perspective
Appl. Microbiol. Biotechnol.
65
243-249
2004
Klebsiella aerogenes, Geobacillus stearothermophilus, Lactobacillus gayonii, Thermotoga neapolitana, Thermus sp., Vibrio parahaemolyticus, Thermoanaerobacter mathranii, Salmonella enterica subsp. enterica serovar Typhimurium (P06189), Escherichia coli (P08202), Escherichia coli (P58538), Escherichia coli (Q8FL89), Salmonella enterica subsp. enterica serovar Typhi (P58539), Yersinia pestis (P58540), Bacillus subtilis (P94523), Shigella flexneri (Q7UDT4), Lactiplantibacillus plantarum (Q88S84), Bacteroides thetaiotaomicron (Q8AAW1), Oceanobacillus iheyensis (Q8EMP4), Bifidobacterium longum (Q8G7J3), Clostridium acetobutylicum (Q97JE0), Clostridium acetobutylicum (Q97JE4), Halalkalibacterium halodurans (Q9KBQ2), Thermotoga maritima (Q9WYB3)
brenda
Lee, D.W.; Choe, E.A.; Kim, S.B.; Eom, S.H.; Hong, Y.H.; Lee, S.J.; Lee, H.S.; Lee, D.Y.; Pyun, Y.R.
Distinct metal dependence for catalytic and structural functions in the L-arabinose isomerases from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus
Arch. Biochem. Biophys.
434
333-343
2005
Geobacillus stearothermophilus, Halalkalibacterium halodurans
brenda
Rhimi, M.; Bejar, S.
Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive l-arabinose isomerase from the Bacillus stearothermophilus US100 strain
Biochim. Biophys. Acta
1760
191-199
2006
Geobacillus stearothermophilus, Geobacillus stearothermophilus (Q9S467), Geobacillus stearothermophilus US100
brenda
Jung, E.S.; Kim, H.J.; Oh, D.K.
Tagatose production by immobilized recombinant Escherichia coli cells containing Geobacillus stearothermophilus l-arabinose isomerase mutant in a packed-bed bioreactor
Biotechnol. Prog.
21
1335-1340
2005
Geobacillus stearothermophilus
brenda
Kim, H.J.; Oh, D.K.
Purification and characterization of an L-arabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing D-tagatose
J. Biotechnol.
120
162-173
2005
Geobacillus thermodenitrificans (Q6W9D4), Geobacillus thermodenitrificans
brenda
Baek, D.H.; Lee, Y.; Sin, H.S.; Oh, D.K.
A new thermophile strain of Geobacillus thermodenitrificans having L-arabinose isomerase activity for tagatose production
J. Microbiol. Biotechnol.
14
312-316
2004
Geobacillus thermodenitrificans, Geobacillus thermodenitrificans CBD-A1
-
brenda
Kawaguchi, H.; Sasaki, M.; Vertes, A.A.; Inui, M.; Yukawa, H.
Engineering of an L-arabinose metabolic pathway in Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
77
1053-1062
2008
Escherichia coli
brenda
Oh, H.J.; Kim, H.J.; Oh, D.K.
Increase in D-tagatose production rate by site-directed mutagenesis of L-arabinose isomerase from Geobacillus thermodenitrificans
Biotechnol. Lett.
28
145-149
2006
Geobacillus thermodenitrificans (Q6W9D4)
brenda
Hong, Y.H.; Lee, D.W.; Lee, S.J.; Choe, E.A.; Kim, S.B.; Lee, Y.H.; Cheigh, C.I.; Pyun, Y.R.
Production of D-tagatose at high temperatures using immobilized Escherichia coli cells expressing L-arabinose isomerase from Thermotoga neapolitana
Biotechnol. Lett.
29
569-574
2007
Thermotoga neapolitana
brenda
Chouayekh, H.; Bejar, W.; Rhimi, M.; Jelleli, K.; Mseddi, M.; Bejar, S.
Characterization of an l-arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH
FEMS Microbiol. Lett.
277
260-267
2007
Lactiplantibacillus plantarum (A9J246), Lactiplantibacillus plantarum NC8 (A9J246)
brenda
Kim, H.J.; Kim, J.H.; Oh, H.J.; Oh, D.K.
Characterization of a mutated Geobacillus stearothermophilus L-arabinose isomerase that increases the production rate of D-tagatose
J. Appl. Microbiol.
101
213-221
2006
Geobacillus stearothermophilus (Q9S467), Geobacillus stearothermophilus, Geobacillus stearothermophilus KCCM12265 (Q9S467)
brenda
Rhimi, M.; Juy, M.; Aghajari, N.; Haser, R.; Bejar, S.
Probing the essential catalytic residues and substrate affinity in the thermoactive Bacillus stearothermophilus US100 L-arabinose isomerase by site-directed mutagenesis
J. Bacteriol.
189
3556-3563
2007
Geobacillus stearothermophilus (Q9S467), Geobacillus stearothermophilus
brenda
Manjasetty, B.A.; Chance, M.R.
Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production
J. Mol. Biol.
360
297-309
2006
Escherichia coli (P08202), Escherichia coli
brenda
Oh, D.K.; Oh, H.J.; Kim, H.J.; Cheon, J.; Kim, P.
Modification of optimal pH in L-arabinose isomerase from Geobacillus stearothermophilus for D-galactose isomerization
J. Mol. Catal. B
43
108-112
2006
Geobacillus stearothermophilus (Q9S467)
-
brenda
Zhang, H.; Jiang, B.; Pan, B.
Purification and characterization of L-arabinose isomerase from Lactobacillus plantarum producing D-tagatose
World J. Microbiol. Biotechnol.
23
641-646
2007
Lactiplantibacillus plantarum (Q88S84)
brenda
Wiedemann, B.; Boles, E.
Codon-optimized bacterial genes improve L-arabinose fermentation in recombinant Saccharomyces cerevisiae
Appl. Environ. Microbiol.
74
2043-2050
2008
Bacillus licheniformis
brenda
Lim, B.C.; Kim, H.J.; Oh, D.K.
Tagatose production with pH control in a stirred tank reactor containing immobilized L-arabinose from Thermotoga neapolitana
Appl. Biochem. Biotechnol.
149
245-253
2008
Thermotoga neapolitana
brenda
Kim, J.H.; Lim, B.C.; Yeom, S.J.; Kim, Y.S.; Kim, H.J.; Lee, J.K.; Lee, S.H.; Kim, S.W.; Oh, D.K.
Differential selectivity of the Escherichia coli cell membrane shifts the equilibrium for the enzyme-catalyzed isomerization of galactose to tagatose
Appl. Environ. Microbiol.
74
2307-2313
2008
Escherichia coli
brenda
Prabhu, P.; Tiwari, M.K.; Jeya, M.; Gunasekaran, P.; Kim, I.W.; Lee, J.K.
Cloning and characterization of a novel L-arabinose isomerase from Bacillus licheniformis
Appl. Microbiol. Biotechnol.
81
283-290
2008
Bacillus licheniformis
brenda
Yeom, S.J.; Ji, J.H.; Yoon, R.Y.; Oh, D.K.
L-Ribulose production from L-arabinose by an L-arabinose isomerase mutant from Geobacillus thermodenitrificans
Biotechnol. Lett.
30
1789-1793
2008
Geobacillus thermodenitrificans
brenda
Givry, S.; Duchiron, F.
Optimization of culture medium and growth conditions for production of L-arabinose isomerase and D-xylose isomerase by Lactobacillus bifermentans
Microbiology
77
281-287
2008
Loigolactobacillus bifermentans
-
brenda
Yeom, S.J.; Kim, N.H.; Park, C.S.; Oh, D.K.
L-ribose production from L-arabinose by using purified L-arabinose isomerase and mannose-6-phosphate isomerase from Geobacillus thermodenitrificans
Appl. Environ. Microbiol.
75
6941-6943
2009
Geobacillus thermodenitrificans
brenda
Prabhu, P.; Jeya, M.; Lee, J.K.
Probing the molecular determinant for the catalytic efficiency of L-arabinose isomerase from Bacillus licheniformis
Appl. Environ. Microbiol.
76
1653-1660
2010
Bacillus licheniformis (Q65J10), Bacillus licheniformis
brenda
Helanto, M.; Kiviharju, K.; Granstroem, T.; Leisola, M.; Nyyssoelae, A.
Biotechnological production of L-ribose from L-arabinose
Appl. Microbiol. Biotechnol.
83
77-83
2009
Acinetobacter sp. (Q93UQ5), Acinetobacter sp. DL-28 (Q93UQ5)
brenda
Kim, J.H.; Prabhu, P.; Jeya, M.; Tiwari, M.K.; Moon, H.J.; Singh, R.K.; Lee, J.K.
Characterization of an L-arabinose isomerase from Bacillus subtilis
Appl. Microbiol. Biotechnol.
85
1839-1847
2010
Bacillus subtilis (C7F8M0), Bacillus subtilis, Bacillus subtilis 168 (C7F8M0)
brenda
Cheng, L.; Mu, W.; Zhang, T.; Jiang, B.
An L-arabinose isomerase from Acidothermus cellulolytics ATCC 43068: cloning, expression, purification, and characterization
Appl. Microbiol. Biotechnol.
86
1089-1097
2010
Acidothermus cellulolyticus (A0LT86), Acidothermus cellulolyticus
brenda
Rhimi, M.; Aghajari, N.; Juy, M.; Chouayekh, H.; Maguin, E.; Haser, R.; Bejar, S.
Rational design of Bacillus stearothermophilus US100 L-arabinose isomerase: potential applications for D-tagatose production
Biochimie
91
650-653
2009
Geobacillus stearothermophilus (Q9S467), Geobacillus stearothermophilus, Geobacillus stearothermophilus US100 (Q9S467)
brenda
Zhang, Y.W.; Prabhu, P.; Lee, J.K.
Immobilization of Bacillus licheniformis L-arabinose isomerase for semi-continuous L-ribulose production
Biosci. Biotechnol. Biochem.
73
2234-2239
2009
Bacillus licheniformis
brenda
Cheon, J.; Kim, S.; Park, S.; Han, J.; Kim, P.
Characterization of L-arabinose isomerase in Bacillus subtilis, a GRAS host, for the production of edible tagatose
Food Biotechnol.
23
8-16
2009
Geobacillus stearothermophilus (Q9S467)
-
brenda
Sakakibara, Y.; Saha, B.C.; Taylor, P.
Microbial production of xylitol from L-arabinose by metabolically engineered Escherichia coli
J. Biosci. Bioeng.
107
506-511
2009
Escherichia coli K-12, Escherichia coli K-12 AB707
brenda
Zhang, Y.W.; Prabhu, P.; Lee, J.K.; Kim, I.W.
Enhanced stability of Bacillus licheniformis L-arabinose isomerase by immobilization with alginate
Prep. Biochem. Biotechnol.
40
65-75
2010
Bacillus licheniformis
brenda
Zhang, Y.W.; Jeya, M.; Lee, J.K.
L-Ribulose production by an Escherichia coli harboring L-arabinose isomerase from Bacillus licheniformis
Appl. Microbiol. Biotechnol.
87
1993-1999
2010
Bacillus licheniformis
brenda
Zhang, Y.W.; Jeya, M.; Lee, J.K.
Enhanced activity and stability of L-arabinose isomerase by immobilization on aminopropyl glass
Appl. Microbiol. Biotechnol.
89
1435-1442
2011
Bacillus licheniformis
brenda
Prabhu, P.; Jeya, M.; Lee, J.K.
In silico studies on the substrate specificity of an L-arabinose isomerase from Bacillus licheniformis
Bioorg. Med. Chem. Lett.
20
4436-4439
2010
Bacillus licheniformis (Q65J10), Bacillus licheniformis
brenda
Zhang, Y.; Prabhu, P.; Lee, J.
Alginate immobilization of recombinant Escherichia coli whole cells harboring L-arabinose isomerase for L-ribulose production
Bioprocess Biosyst. Eng.
33
741-748
2010
Bacillus licheniformis
brenda
Rhimi, M.; Ilhammami, R.; Bajic, G.; Boudebbouze, S.; Maguin, E.; Haser, R.; Aghajari, N.
The acid tolerant L-arabinose isomerase from the food grade Lactobacillus sakei 23K is an attractive D-tagatose producer
Biores. Technol.
101
9171-9177
2010
Latilactobacillus sakei, Latilactobacillus sakei 23K
brenda
Rhimi, M.; Chouayekh, H.; Gouillouard, I.; Maguin, E.; Bejar, S.
Production of D-tagatose, a low caloric sweetener during milk fermentation using L-arabinose isomerase
Biores. Technol.
102
3309-3315
2011
Geobacillus stearothermophilus, Geobacillus stearothermophilus US100
brenda
Li, Y.; Zhu, Y.; Liu, A.; Sun, Y.
Identification and characterization of a novel L-arabinose isomerase from Anoxybacillus flavithermus useful in D-tagatose production
Extremophiles
15
441-450
2011
Anoxybacillus flavithermus (F6KRI7), Anoxybacillus flavithermus, Anoxybacillus flavithermus TC-06 (F6KRI7)
brenda
Kim, H.; Uhm, T.; Kim, S.; Kim, P.
Escherichia coli arabinose isomerase and Staphylococcus aureus tagatose-6-phosphate isomerase: Which is a better template for directed evolution of non-natural substrate isomerization?
J. Microbiol. Biotechnol.
20
1018-1021
2010
Escherichia coli
brenda
Xu, Z.; Qing, Y.; Li, S.; Feng, X.; Xu, H.; Ouyang, P.
A novel L-arabinose isomerase from Lactobacillus fermentum CGMCC2921 for D-tagatose production: Gene cloning, purification and characterization
J. Mol. Catal. B
70
1-7
2011
Limosilactobacillus fermentum (D9ILD9), Limosilactobacillus fermentum CGMCC2921 (D9ILD9)
-
brenda
Cheng, L.; Mu, W.; Jiang, B.
Thermostable L-arabinose isomerase from Bacillus stearothermophilus IAM 11001 for D-tagatose production: gene cloning, purification and characterisation
J. Sci. Food Agric.
90
1327-1333
2010
Geobacillus stearothermophilus, Geobacillus stearothermophilus IAM 11001
brenda
Cao, T.P.; Choi, J.M.; Lee, S.J.; Lee, Y.J.; Lee, S.K.; Jun, Y.; Lee, D.W.; Lee, S.H.
Crystallization and preliminary X-ray crystallographic analysis of L-arabinose isomerase from thermophilic Geobacillus kaustophilus
Acta Crystallogr. Sect. F
70
108-112
2014
Geobacillus kaustophilus
brenda
Salonen, N.; Nyyssoelae, A.; Salonen, K.; Turunen, O.
Bifidobacterium longum L-arabinose isomerase - overexpression in Lactococcus lactis, purification, and characterization
Appl. Biochem. Biotechnol.
168
392-405
2012
Bifidobacterium longum (I3ZR32), Bifidobacterium longum, Bifidobacterium longum NRRL B-41409 (I3ZR32), Bifidobacterium longum NRRL B-41409
brenda
Kim, K.R.; Seo, E.S.; Oh, D.K.
L-ribose production from L-arabinose by immobilized recombinant Escherichia coli co-expressing the L-arabinose isomerase and mannose-6-phosphate isomerase genes from Geobacillus thermodenitrificans
Appl. Biochem. Biotechnol.
172
275-288
2014
Geobacillus thermodenitrificans
brenda
Lee, S.J.; Lee, S.J.; Lee, Y.J.; Kim, S.B.; Kim, S.K.; Lee, D.W.
Homologous alkalophilic and acidophilic L-arabinose isomerases reveal region-specific contributions to the pH dependence of activity and stability
Appl. Environ. Microbiol.
78
8813-8816
2012
Alicyclobacillus acidocaldarius, Alicyclobacillus sp., Alicyclobacillus sp. TP7
brenda
Liang, M.; Chen, M.; Liu, X.; Zhai, Y.; Liu, X.W.; Zhang, H.; Xiao, M.; Wang, P.
Bioconversion of D-galactose to D-tagatose: continuous packed bed reaction with an immobilized thermostable L-arabinose isomerase and efficient purification by selective microbial degradation
Appl. Microbiol. Biotechnol.
93
1469-1474
2012
Thermoanaerobacter mathranii
brenda
Xu, Z.; Li, S.; Feng, X.; Zhan, Y.; Xu, H.
Function of aspartic acid residues in optimum pH control of L-arabinose isomerase from Lactobacillus fermentum
Appl. Microbiol. Biotechnol.
98
3987-3996
2014
Limosilactobacillus fermentum (D9ILD9), Limosilactobacillus fermentum, Limosilactobacillus fermentum CGMCC2921 (D9ILD9)
brenda
Hung, X.; Tseng, W.; Liu, S.; Tzou, W.; Fang, T.
Characterization of a thermophilic L-arabinose isomerase from Thermoanaerobacterium saccharolyticum NTOU1
Biochem. Eng. J.
83
121-128
2014
Thermoanaerobacterium saccharolyticum (K7SW59), Thermoanaerobacterium saccharolyticum NTOU1 (K7SW59)
-
brenda
Seo, M.J.
Characterization of an L-arabinose isomerase from Bacillus thermoglucosidasius for D-tagatose production
Biosci. Biotechnol. Biochem.
77
385-388
2013
Parageobacillus thermoglucosidasius (Q6VAK6), Parageobacillus thermoglucosidasius, Parageobacillus thermoglucosidasius KCTC 1828 (Q6VAK6)
brenda
Jebors, S.; Tauran, Y.; Aghajari, N.; Boudebbouze, S.; Maguin, E.; Haser, R.; Coleman, A.W.; Rhimi, M.
Supramolecular stabilization of acid tolerant L-arabinose isomerase from Lactobacillus sakei
Chem. Commun. (Camb. )
47
12307-12309
2011
Latilactobacillus sakei
brenda
Lee, Y.J.; Lee, S.J.; Kim, S.B.; Lee, S.J.; Lee, S.H.; Lee, D.W.
Structural insights into conserved L-arabinose metabolic enzymes reveal the substrate binding site of a thermophilic L-arabinose isomerase
FEBS Lett.
588
1064-1070
2014
Geobacillus stearothermophilus
brenda
Hong, Y.H.; Lee, D.W.; Pyun, Y.R.; Lee, S.H.
Creation of metal-independent hyperthermophilic L-arabinose isomerase by homologous recombination
J. Agric. Food Chem.
59
12939-12947
2011
Geobacillus stearothermophilus, Thermotoga maritima
brenda
Torres, P.; Manzo, R.; Rubiolo, A.; Batista-Viera, F.; Mammarella, E.
Purification of an L-arabinose isomerase from Enterococcus faecium DBFIQ E36 employing a biospecific affinity strategy
J. Mol. Catal. B
102
99-105
2014
Enterococcus faecium, Enterococcus faecium DBFIQ E36
-
brenda
Wang, Y.; Luo, X.; Li, X.; Zhang, T.
Production of D-tagatose with recombinant Escherichia coli strain secreting beta-galactosidase and L-arabinose isomerase from E. coli K-12
J. Pure Appl. Microbiol.
7
1497-1504
2013
Escherichia coli
-
brenda
Wanarska, M.; Kur, J.
A method for the production of D-tagatose using a recombinant Pichia pastoris strain secreting beta-D-galactosidase from Arthrobacter chlorophenolicus and a recombinant L-arabinose isomerase from Arthrobacter sp. 22c
Microb. Cell Fact.
11
113
2012
Arthrobacter sp. (H6UGW9), Arthrobacter sp., Arthrobacter sp. 22c (H6UGW9)
brenda
Men, Y.; Zhu, Y.; Zhang, L.; Kang, Z.; Izumori, K.; Sun, Y.; Ma, Y.
Enzymatic conversion of D-galactose to D-tagatose: cloning, overexpression and characterization of L-arabinose isomerase from Pediococcus pentosaceus PC-5
Microbiol. Res.
169
171-178
2014
Pediococcus pentosaceus (G1JRK8), Pediococcus pentosaceus, Pediococcus pentosaceus PC-5 (G1JRK8), Pediococcus pentosaceus PC-5
brenda
Zhou, X.; Wu, J.C.
Heterologous expression and characterization of Bacillus coagulans L-arabinose isomerase
World J. Microbiol. Biotechnol.
28
2205-2212
2012
Weizmannia coagulans
brenda
Xu, Z.; Li, S.; Liang, J.; Feng, X.; Xu, H.
Protein purification, crystallization and preliminary X-ray diffraction analysis of L-arabinose isomerase from Lactobacillus fermentum CGMCC2921
Acta Crystallogr. Sect. F
71
28-33
2015
Limosilactobacillus fermentum (D9ILD9), Limosilactobacillus fermentum CGMCC2921 (D9ILD9)
brenda
Kim, K.; Seo, E.; Oh, D.
L-ribose production from L-arabinose by immobilized recombinant Escherichia coli co-expressing the L-arabinose isomerase and mannose-6-phosphate isomerase genes from Geobacillus thermodenitrificans
Appl. Biochem. Biotechnol.
172
275-288
2014
Geobacillus thermodenitrificans
brenda
Fan, C.; Xu, W.; Zhang, T.; Zhou, L.; Jiang, B.; Mu, W.
Engineering of Alicyclobacillus hesperidum L-arabinose isomerase for improved catalytic activity and reduced pH optimum using random and site-directed mutagenesis
Appl. Biochem. Biotechnol.
177
1480-1492
2015
Alicyclobacillus hesperidum (J9E728), Alicyclobacillus hesperidum, Alicyclobacillus hesperidum URH17-3-68 (J9E728), Alicyclobacillus hesperidum URH17-3-68
brenda
Kim, B.J.; Hong, S.H.; Shin, K.C.; Jo, Y.S.; Oh, D.K.
Characterization of a F280N variant of L-arabinose isomerase from Geobacillus thermodenitrificans identified as a D-galactose isomerase
Appl. Microbiol. Biotechnol.
98
9271-9281
2014
Geobacillus thermodenitrificans (Q6W9D4), Geobacillus thermodenitrificans
brenda
Choi, J.M.; Lee, Y.J.; Cao, T.P.; Shin, S.M.; Park, M.K.; Lee, H.S.; di Luccio, E.; Kim, S.B.; Lee, S.J.; Lee, S.J.; Lee, S.H.; Lee, D.W.
Structure of the thermophilic L-arabinose isomerase from Geobacillus kaustophilus reveals metal-mediated intersubunit interactions for activity and thermostability
Arch. Biochem. Biophys.
596
51-62
2016
Geobacillus kaustophilus (Q5KYP7), Geobacillus kaustophilus
brenda
Xu, Z.; Xu, Z.; Tang, B.; Li, S.; Gao, J.; Chi, B.; Xu, H.
Construction and co-expression of polycistronic plasmids encoding thermophilic L-arabinose isomerase and hyperthermophilic beta-galactosidase for single-step production of D-tagatose
Biochem. Eng. J.
109
28-34
2016
Limosilactobacillus fermentum (D9ILD9), Limosilactobacillus fermentum CGMCC2921 (D9ILD9)
-
brenda
Guo, Q.; An, Y.; Yun, J.; Yang, M.; Magocha, T.; Zhu, J.; Xue, Y.; Qi, Y.; Hossain, Z.; Sun, W.; Qi, X.
Enhanced D-tagatose production by spore surface-displayed L-arabinose isomerase from isolated Lactobacillus brevis PC16 and biotransformation
Biores. Technol.
247
940-946
2018
Levilactobacillus brevis, Levilactobacillus brevis PC16
brenda
Mei, W.; Wang, L.; Zang, Y.; Zheng, Z.; Ouyang, J.
Characterization of an L-arabinose isomerase from Bacillus coagulans NL01 and its application for D-tagatose production
BMC Biotechnol.
16
55
2016
Weizmannia coagulans (A0A191W0D9), Weizmannia coagulans NL01 (A0A191W0D9)
brenda
Zhan, Y.; Xu, Z.; Li, S.; Liu, X.; Xu, L.; Feng, X.; Xu, H.
Coexpression of ?-D-galactosidase and L-arabinose isomerase in the production of D-tagatose a functional sweetener
J. Agric. Food Chem.
62
2412-2417
2014
Escherichia coli
brenda
Rhimi, M.; Bermudez-Humaran, L.; Huang, Y.; Boudebbouze, S.; Gaci, N.; Garnier, A.; Gratadoux, J.; Mkaouar, H.; Langella, P.; Maguin, E.
The secreted L-arabinose isomerase displays anti-hyperglycemic effects in mice
Microb. Cell Fact.
14
204
2015
Latilactobacillus sakei
brenda
Xu, W.; Fan, C.; Zhang, T.; Jiang, B.; Mu, W.
Cloning, expression, and characterization of a novel L-arabinose isomerase from the psychrotolerant bacterium Pseudoalteromonas haloplanktis
Mol. Biotechnol.
58
695-706
2016
Pseudoalteromonas haloplanktis (Q3IG38), Pseudoalteromonas haloplanktis, Pseudoalteromonas haloplanktis ATCC 14393 (Q3IG38), Pseudoalteromonas haloplanktis ATCC 14393
brenda
de Sousa, M.; Manzo, R.M.; Garcia, J.L.; Mammarella, E.J.; Goncalves, L.R.B.; Pessela, B.C.
Engineering the L-arabinose isomerase from Enterococcus faecium for D-tagatose synthesis
Molecules
22
2164
2017
Enterococcus faecium (A0A1L2F0V9), Enterococcus faecium, Enterococcus faecium DBFIQ E36 (A0A1L2F0V9)
brenda
Nguyen, T.; Hong, M.; Chang, P.; Lee, B.; Yoo, S.
Biochemical properties of L-arabinose isomerase from Clostridium hylemonae to produce D-tagatose as a functional sweetener
PLoS ONE
13
e0196099
2018
[Clostridium] hylemonae (C0C0X3), [Clostridium] hylemonae, [Clostridium] hylemonae DSM 15053 (C0C0X3)
brenda