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1-butanol
30% v/v, recombinant enzyme expressed in Sulfolobus solfataricus shows 36% residual activity. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 18% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 29% residual activity
1-propanol
30% v/v, recombinant enzyme expressed in Sulfolobus solfataricus shows 76% residual activity. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 32% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 39% residual activity
benzene
-
pH 7.0, 60°C, 2 h, loss of 91.6% activity
cyclohexane
-
pH 7.0, 60°C, 2 h, loss of 98.7% activity
dichloromethane
the enzyme activity is reduced by 73-91% at 5-10% v/v
diethyl ether
-
30%, 124% residual activity
dodecane
-
5%, complete loss of activity
guanidine-HCl
half-completion of the unfolding transition: 2.0-2.1 M
hexadecane
-
5%, 51% residual activity
isoamyl alcohol
30% v/v, recombinant enzyme expressed in Sulfolobus solfataricus shows 36% residual activity. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 8% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 9% residual activity
isooctane
-
pH 7.0, 60°C, 2 h, completely stable
isopropyl ether
-
15% (v/v) isopropyl ether increases the esterase activity by about 60%, 50% (v/v) isopropyl ether produces a 10% increase in esterase activity
N,N-dimethylformamide
-
30%, 108% residual activity
n-decane
the enzyme activity is reduced by 11-23% at 5-10% v/v
n-heptane
the enzyme activity is stable at 5-10% v/v
n-octanol
the enzyme activity is reduced by 22-90% at 5-10% v/v
n-propanol
the enzyme activity is reduced by 93.5% at 10% v/v
octane
-
5%, complete loss of activity
Spa-80
-
decreases activity at 0.1% (v/v) and 1% (v/v)
taurocholic acid
-
slightly increases activity at 0.1% (v/v)
tetrahydrofuran
the enzyme activity is reduced by 33-96% at 5-10% v/v
Triton X-15
-
110% increase of activity in the presence of Triton X-15
Triton X-165
-
1649% increase of activity in the presence of Triton X-15
Triton X-305
-
1528% increase of activity in the presence of Triton X-15
Triton X-45
-
562% increase of activity in the presence of Triton X-15
xylene
the enzyme activity is reduced by 44% at 5-10% v/v
additional information
-
investigation of stability of the enzyme in organic solvents
1,4-dioxane
the enzyme activity is reduced by 60-95.5% at 5-10% v/v
1,4-dioxane
30%, about 60% inhibition, at 70°C, in 50 mM HEPES (pH 7.5) using 4-nitrophenyl butanoate as the substrate
1,4-dioxane
-
30%, about 60% inhibition, at 70°C, in 50 mM HEPES (pH 7.5) using 4-nitrophenyl butanoate as the substrate
-
2-propanol
1 h, 80%, 6% loss of activity
2-propanol
-
1 h, 80%, 6% loss of activity
-
2-propanol
-
40%, 60 min at 30°C, 91% residual activity
2-propanol
90%, 30°C, 30 min, stable
2-propanol
-
40%, 60 min at 30°C, 91% residual activity
-
2-propanol
-
90%, 30°C, 30 min, stable
-
2-propanol
30% v/v, recombinant enzyme expressed in Sulfolobus solfataricus shows 95% residual activity. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 30% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 35% residual activity
Acetone
-
30% (v/v) acetone decreases the activity by 40%, 50% acetone results in a severe reduction of activity
Acetone
-
30% (v/v) acetone decreases the activity by 40%, 50% acetone results in a severe reduction of activity
-
Acetone
the enzyme activity is reduced by 44% at 10% v/v
Acetone
20% v/v, 70-80% residual activity, 60% v/v, 45% residual activity
Acetone
21.8% residual activity after 1 h
Acetone
-
21.8% residual activity after 1 h
-
Acetone
-
30%, 130% residual activity
Acetone
-
40%, 60 min at 30°C, 61% residual activity
Acetone
-
40%, 60 min at 30°C, 61% residual activity
-
Acetone
30% v/v, recombinant enzyme expressed in Sulfolobus solfataricus shows 91% residual activity. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 63% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 81% residual activity
Acetone
-
30% v/v, recombinant enzyme expressed in Sulfolobus solfataricus shows 91% residual activity. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 63% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 81% residual activity
-
Acetone
50% (v/v), 2 h incubation, 60% loss of activity, substrate: 4-nitrophenyl butyrate
Acetone
50% (v/v), pH 9.0, 30°C, 60% loss of activity
Acetone
-
50% (v/v), 2 h incubation, 60% loss of activity, substrate: 4-nitrophenyl butyrate
-
Acetone
-
pH 7.0, 60°C, 2 h, loss of 82% activity
Acetone
-
15% v/v, 128% of initial activity, 30% v/v, 155% of initial activity
Acetone
-
15% v/v, 14% of initial activity
acetonitrile
-
30%, 120% residual activity
acetonitrile
1 h, 80%, no loss of activity
acetonitrile
-
1 h, 80%, no loss of activity
-
acetonitrile
-
inactivation
acetonitrile
-
inactivation
-
acetonitrile
30% v/v, recombinant enzyme expressed in Sulfolobus solfataricus shows 77% residual activity. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 40% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 50% residual activity
acetonitrile
-
30% v/v, recombinant enzyme expressed in Sulfolobus solfataricus shows 77% residual activity. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 40% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 50% residual activity
-
acetonitrile
30%, about 50% inhibition, at 70°C, in 50 mM HEPES (pH 7.5) using 4-nitrophenyl butanoate as the substrate
acetonitrile
-
30%, about 50% inhibition, at 70°C, in 50 mM HEPES (pH 7.5) using 4-nitrophenyl butanoate as the substrate
-
acetonitrile
-
82.8% activity at 10% (v/v)
acetonitrile
-
82.8% activity at 10% (v/v)
-
acetonitrile
-
15% v/v, 110% of initial activity, 30% v/v, 87% of initial activity
acetonitrile
-
15% v/v, 0% of initial activity
Butanol
22.9% residual activity after 1 h
Butanol
-
22.9% residual activity after 1 h
-
chloroform
-
5%, complete loss of activity
chloroform
30% v/v, complete inactivation of recombinant enzyme expressed in Sulfolobus solfataricus or Escherichia coli
chloroform
-
30% v/v, complete inactivation of recombinant enzyme expressed in Sulfolobus solfataricus or Escherichia coli
-
chloroform
50% (v/v), 2 h incubation, 66% loss of activity, substrate: 4-nitrophenyl butyrate
chloroform
50% (v/v), pH 9.0, 30°C, 66% loss of activity
dimethyl formamide
-
inactivation
dimethyl formamide
-
inactivation
-
dimethyl formamide
50% (v/v), 2 h incubation, 72% loss of activity, substrate: 4-nitrophenyl butyrate
dimethyl sulfoxide
-
30%, 110% residual activity
dimethyl sulfoxide
1 h, 80%, 10% loss of activity
dimethyl sulfoxide
30%, anout 90% inhibition, at 70°C, in 50 mM HEPES (pH 7.5) using 4-nitrophenyl butanoate as the substrate
dimethyl sulfoxide
-
30%, anout 90% inhibition, at 70°C, in 50 mM HEPES (pH 7.5) using 4-nitrophenyl butanoate as the substrate
-
dimethyl sulfoxide
-
5%, 146% of initial activity
dimethyl sulfoxide
-
up to 30% v/V, enzyme retains full activity
dimethyl sulfoxide
-
up to 15% v/V, enzyme retains full activity
dimethylformamide
1 h, 80%, 4% loss of activity
dimethylformamide
-
1 h, 80%, 4% loss of activity
-
dimethylformamide
50% (v/v), pH 9.0, 30°C, 72% loss of activity
dimethylformamide
-
74% activity at 10% (v/v)
dimethylformamide
-
74% activity at 10% (v/v)
-
dimethylformamide
-
5%, 99% of initial activity
dimethylformamide
-
15% v/v, 128% of initial activity, 30% v/v, 155% of initial activity
dimethylformamide
-
15% v/v, 34% of initial activity
dimethylsulfoxide
-
30% (v/v) dimethylsulfoxide decreases the activity by 40%, 50% (v/v) dimethylsulfoxide results in a severe reduction of activity
dimethylsulfoxide
-
30% (v/v) dimethylsulfoxide decreases the activity by 40%, 50% (v/v) dimethylsulfoxide results in a severe reduction of activity
-
dioxane
13.2% residual activity after 1 h
dioxane
-
5%, 141% of initial activity
DMSO
-
97% residual activity at 1% (v/v) after 30 min of incubation
DMSO
-
97% residual activity at 1% (v/v) after 30 min of incubation
-
DMSO
the enzyme activity is stable at 5-10% v/v
DMSO
30% v/v, recombinant enzyme expressed in Sulfolobus solfataricus shows 98% residual activity. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 73% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 81% residual activity
DMSO
-
55.9% activity at 10% (v/v)
DMSO
-
55.9% activity at 10% (v/v)
-
Ethanol
-
92% residual activity at 1% (v/v) after 30 min of incubation
Ethanol
-
92% residual activity at 1% (v/v) after 30 min of incubation
-
Ethanol
-
30% (v/v) ethanol increases the esterase activity by 20%
Ethanol
-
30% (v/v) ethanol increases the esterase activity by 20%
-
Ethanol
20% v/v, 70-80% residual activity, 60% v/v, almost complete inactivation
Ethanol
27.5% residual activity after 1 h
Ethanol
-
27.5% residual activity after 1 h
-
Ethanol
-
30%, 90% residual activity
Ethanol
1 h, 80%, no loss of activity
Ethanol
-
1 h, 80%, no loss of activity
-
Ethanol
-
40%, 60 min at 30°C, 90% residual activity
Ethanol
-
stable at high concentrations of polar organic solvents, such as ethanol and methanol as compared to other mesophilic counterparts
Ethanol
90%, 30°C, 30 min, stable
Ethanol
-
stable at high concentrations of polar organic solvents, such as ethanol and methanol as compared to other mesophilic counterparts
-
Ethanol
-
40%, 60 min at 30°C, 90% residual activity
-
Ethanol
-
90%, 30°C, 30 min, stable
-
Ethanol
up to 30% v/v, activity of recombinant enzyme expressed in Sulfolobus solfataricus is not affected or slightly increased. The recombinant enzyme expressed in Escherichia coli shows about 40% residual activity
Ethanol
-
up to 30% v/v, activity of recombinant enzyme expressed in Sulfolobus solfataricus is not affected or slightly increased. The recombinant enzyme expressed in Escherichia coli shows about 40% residual activity
-
Ethanol
50% (v/v), 2 h incubation, 67% loss of activity, substrate: 4-nitrophenyl butyrate
Ethanol
50% (v/v), pH 9.0, 30°C, 67% loss of activity
Ethanol
-
50% (v/v), 2 h incubation, 67% loss of activity, substrate: 4-nitrophenyl butyrate
-
Ethanol
-
50% (v/v), pH 9.0, 30°C, 67% loss of activity
-
Ethanol
-
75.9% activity at 10% (v/v)
Ethanol
-
75.9% activity at 10% (v/v)
-
Ethyl acetate
24.8% residual activity after 1 h
Ethyl acetate
-
24.8% residual activity after 1 h
-
formaldehyde
20% (v/v), 2 h incubation, 81% loss of activity, substrate: 4-nitrophenyl butyrate
formaldehyde
50% (v/v), pH 9.0, 30°C, 81% loss of activity
heptane
74.6% residual activity after 1 h
heptane
20% (v/v), 2 h incubation, 88% loss of activity, substrate: 4-nitrophenyl butyrate
heptane
50% (v/v), pH 9.0, 30°C, 88% loss of activity
heptane
-
pH 7.0, 60°C, 2 h, complete loss of activity
hexane
59.2% residual activity after 1 h
hexane
-
5%, complete loss of activity
hexane
30% v/v, recombinant enzyme expressed in Sulfolobus solfataricus shows 36% residual activity. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 10% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 9% residual activity
isopropanol
-
99% residual activity at 1% (v/v) after 30 min of incubation
isopropanol
-
99% residual activity at 1% (v/v) after 30 min of incubation
-
isopropanol
-
15% v/v, 155% of initial activity, 30% v/v, 117% of initial activity
isopropanol
-
15% v/v, 75% of initial activity
Methanol
-
30% (v/v) methanol increases the esterase activity by 10%
Methanol
-
30% (v/v) methanol increases the esterase activity by 10%
-
Methanol
the enzyme activity is reduced by 38% at 10% v/v
Methanol
20% v/v, 70-80% residual activity, 60% v/v, 45% residual activity
Methanol
12.7% residual activity after 1 h
Methanol
-
12.7% residual activity after 1 h
-
Methanol
-
30%, 115% residual activity
Methanol
1 h, 80%,% loss of activity
Methanol
-
1 h, 80%,% loss of activity
-
Methanol
-
40%, 60 min at 30°C, 86% residual activity
Methanol
-
stable at high concentrations of polar organic solvents, such as ethanol and methanol as compared to other mesophilic counterparts
Methanol
90%, 30°C, 30 min, stable
Methanol
-
stable at high concentrations of polar organic solvents, such as ethanol and methanol as compared to other mesophilic counterparts
-
Methanol
-
40%, 60 min at 30°C, 86% residual activity
-
Methanol
-
90%, 30°C, 30 min, stable
-
Methanol
30% v/v, activity of recombinant enzyme expressed in Sulfolobus solfataricus is not affected. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 61% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 76% residual activity
Methanol
-
30% v/v, activity of recombinant enzyme expressed in Sulfolobus solfataricus is not affected. The recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I) shows 61% residual activity. The recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II) shows 76% residual activity
-
Methanol
50% (v/v), 2 h incubation, 58% loss of activity, substrate: 4-nitrophenyl butyrate
Methanol
50% (v/v), pH 9.0, 30°C, 58% loss of activity
Methanol
-
50% (v/v), 2 h incubation, 58% loss of activity, substrate: 4-nitrophenyl butyrate
-
Methanol
-
50% (v/v), pH 9.0, 30°C, 58% loss of activity
-
Methanol
-
80.7% activity at 10% (v/v)
Methanol
-
80.7% activity at 10% (v/v)
-
Methanol
-
15% v/v, 111% of initial activity, 30% v/v, 130% of initial activity
Methanol
-
15% v/v, 90% of initial activity
n-hexane
the enzyme activity is stable at 5-10% v/v
n-hexane
20% (v/v), 2 h incubation, 67% loss of activity, substrate: 4-nitrophenyl butyrate
n-hexane
50% (v/v), pH 9.0, 30°C, 77% loss of activity
n-hexane
-
pH 7.0, 60°C, 2 h, complete loss of activity
propanol
20% v/v, 70-80% residual activity, 60% v/v, almost complete inactivation
propanol
13.1% residual activity after 1 h
propanol
-
30%, 104% residual activity
propanol
50% (v/v), 2 h incubation, 59% loss of activity, substrate: 4-nitrophenyl butyrate
propanol
50% (v/v), pH 9.0, 30°C, 59% loss of activity
SDS
-
the denaturing effect of SDS is noticeable at 10 mM
SDS
-
the denaturing effect of SDS is noticeable at 10 mM
-
SDS
-
for solutions containing 0.05 mM substrate, the optimal SDS concentration is 2.8 mM, and increasing the SDS concentration to 22 mM leads to complete inhibition of activity, solutions containing 0.5 mM substrate display optimal activity in 5.6 mM SDS and near complete inhibition observed in 65 mM SDS
SDS
-
the enzyme activity is not affected by the presence of SDS at up 0.1%
SDS
-
the enzyme activity is not affected by the presence of SDS at up 0.1%
-
SDS
5%, 30°C, 30 min, about 70% loss of activity
SDS
-
5%, 30°C, 30 min, about 70% loss of activity
-
tert-butyl alcohol
20%, about 90% inhibition, at 70°C, in 50 mM HEPES (pH 7.5) using 4-nitrophenyl butanoate as the substrate
tert-butyl alcohol
-
20%, about 90% inhibition, at 70°C, in 50 mM HEPES (pH 7.5) using 4-nitrophenyl butanoate as the substrate
-
toluene
the enzyme activity is reduced by 46.5-62% at 5-10% v/v
toluene
-
5%, complete loss of activity
toluene
20% (v/v), 2 h incubation, 86% loss of activity, substrate: 4-nitrophenyl butyrate
toluene
50% (v/v), pH 9.0, 30°C, 86% loss of activity
Triton X-100
-
960% increase of activity in the presence of Triton X-100
Triton X-100
-
decreases activity at 0.1% (v/v) and 1% (v/v)
Tween
-
more than 1200% increase of activity in the presence of Tween 20, 40, 60 or 80
Tween
-
0.1% Tween-80 increases activity by 160%, in the presence of 1% detergent, Tween-80 increases activity by 126%
urea
half-completion of the unfolding transition at 7.1 M
urea
-
bovine serum albumin esterase activity is retained in 8 M urea
urea
8 M, 30°C, 30 min, about 80% loss of activity
urea
-
8 M, 30°C, 30 min, about 80% loss of activity
-