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0
-
no loss of activity upon short term storage on ice
25 - 40
-
isozyme R43, thermolabile, 30 min, loss of 50% activity at 25°C, inactivation at 40°C
25 - 75
more than 20% of the activity is retained after heating the enzyme at 85°C
30 - 50
recombinant enzyme, half-life is over 8 h
30 - 60
recombinant enzyme, half-life is over 8 h
37 - 55
-
very stable in this range for up to 8h, at 55°C for 24 h and at 60°C for 2 h still retains 20% original activity, inactive at 60°C for 4 h
40 - 60
-
purified native enzyme, 60 min, stable
41.5
standard buffer, thermal unfolding temperature
50 - 60
-
isozyme R18, 30 min, completely stable up to 50°C, inactivation at 60°C
50 - 80
-
loses most of its activity when heated for 10 min at 70°C
52
-
T50-value for mutant enzyme is 51.6°C
63
30 min, mutant D93G/S187F shows a loss of around 70-80% activity, mutant C235S shows a loss of about 10% activity
70 - 80
24% of activity when used for the standard assay with methyl ferulate as substrate
70 - 90
-
stable for 6h, loses 50% activity at 80°C within 3 h, loses all activity after 1 h at 90°C
74
presence of 2.5 M sodium malonate, thermal unfolding temperature
75 - 80
-
at 75°C retains at least 95% of its original activity for over 80 min. At 80°C, its half-life is 50 min, rendering FAE a highly thermostable protein
30
-
15 min, stable
30
-
fully stable at pH 7.0-9.0
30
-
stable up to, isoenzyme FAE-I
30
1 h, 55% residual activity
30
recombinant enzyme, half-life is over 8 h
30 - 40
-
60% of the activities are retained when FAE-1 and FAE-2 are preincubated at 50°C for 30 min
30 - 40
-
at 50°C 50% activity lost in 45 min, rapid inactivation at 60°C and above
30 - 40
recombinant enzyme, half-life is over 8 h
30 - 70
stable
30 - 70
recombinant enzyme, half-life is over 8 h
37
-
purified enzyme, no loss of activity within 2 h
37
-
after 2 h at 37°C, the FAE specific activity is 60% reduced
37 - 60
-
-
37 - 60
-
purified enzyme is stable over the range 37-55°C for up to 8h, but loses activity rapidly at temperatures above 60°C
40
-
8 h, 50% residual activity
40
-
purified enzyme, pH 4.5-8.0, 60 min, stable
40
purified isozyme AtFAE-2, 4 h incubation at pH 3.0-8.0, over 50% activity remaining
40
purified isozyme AtFAE-3, 4 h incubation at pH 3.0-8.0, over 50% activity remaining
40
-
15 min, 20% loss of activity
40
purified recombinant His-tagged enzyme, 60 min, completely stable
40
-
both FAE-I and FAE-II relatively stable
40
1 h, almost complete loss of activity
40
purified recombinant His-tagged enzyme, 60 min, completely stable
40
Q70Y21
unstable on incubation above 40°C
40
Thermochaetoides dissita
-
24 h, 99% residual activity
40
Thermochaetoides dissita
24 h, 99% residual activity
40
80% of maximal activity after 192 h, pH 6.8
40
recombinant enzyme, half-life is 7 h
45
stable at
45
-
purified recombinant enzyme, highly stable below
45
-
purified recombinant Fee1B is stable at temperature up to 40°C. The enzyme loses about 30% activity upon incubation at 45°C for 30 min
45
above, purified recombinant His-tagged enzyme, 60 min, rapid inactivation, loss of 68% activity after 5 min
45
-
stable up to, isoenzyme FAE-II
45
-
Fae-II and FaeC-12213
45
-
purified enzyme, 68% loss of activity within 5 min
45
above, purified recombinant His-tagged enzyme, 60 min, rapid inactivation, loss of 68% activity after 5 min
45
-
unstable above 45°C when incubated at pH 6.0 for 6 h
45
half-life is 72 h, inactivation after 96 h, pH 6.8
45 - 50
-
native and chimeric enzymes retain more than 90% of their activity after incubation at 45°C and 50°C for 30 min, respectively
45 - 50
10-16% loss of activity within 120 min
48
-
T50-value for mutant enzyme N79A is 48.1°C
48
-
T50-value for mutant enzyme N79Q is 47.7°C
50
-
-
50
-
60 min, wild-type enzyme retains 70% of its activity, mutant enzymes N79A and N79Q retain no activity
50
-
1 h, stable up to 50°C in absence of glycerol
50
half-lives of wild-type enzyme and mutants S92A and D174A is 8 min, half-life of mutant D93G is 9.4 min, and of mutant S187F 60.5 min
50
-
completely inactivated within 30 min at 70°C
50
purified isozyme AtFAE-1, 4 h incubation at pH 3.0-8.0, over 50% activity remaining
50
-
purified recombinant enzyme, loss of 45% activity after 60 min
50
-
15 min, about 70% of maximal activity
50
Thermochaetoides dissita
24 h, 98% residual activity
50
half-life is 7 h, pH 6.8
50
-
the enzyme is stable below 45°C, it quickly loses activity above 50°C
50
recombinant enzyme, half-life is 1.5 h
50
recombinant enzyme, half-life is below 1 h
55
-
stable at
55
-
addition of a higher amount of calcium ions (more than 0.3 mol/dm3) induces a decrease in enzymatic thermostability, independent of the amount of Ca2+ added
55
-
after incubation at 55°C, the chimeric enzyme retains 40% of its activity, whereas, the native enzyme almost loses its activity
55
30 min, FAEA produced in Aspergillus niger loses 15% of its activity, FAEA produced in Escherichia coli loses 94% of its activity
55
half-life of mutant D93G/S187F is 4.7 min, half-lives of mutants with further increased thermostability, best is mutant S163T with a half-life of 16.9 min, overview
55
-
purified recombinant FaeB and FaeC retain more than 90% of their activity after incubation at 55°C for 30 min. FaeC retains 40% of its activity after treatment at 65°C, whereas FaeB almost loses its activity
55
-
purified recombinant enzyme, loss of 50% activity after 5 min, inactivation after 40 min
55
half-life of wild-type 15 min, of mutant A126C/N152C 188 min, respectively
55
-
rapid inactivation above
55
wild-type, 1 h, 10.8%, mutant H105Y 34.3%, mutant F251L/H105Y 21.4%, mutant G49D 46.2%, mutant G49A 37.4% residual activity, respectively
55
half-life is 0.08 h, inactivation after 0.5 h, pH 6.8
55
half-life of wild-type 0.5 h, mutant T27I/S84L/V161I/G243C 70 h, mutant T27I/S84L/V161I/H195L/G243C/A259V 1680 h, respectively
60
-
2 h, 50% residual activity
60
-
1 h, 83% loss of activity in absence of glycerol, stale in presence of glycerol
60
wild-type half-life 8.3 min, half-lifes of mutants D93G/S187/C235I, D93G/S187F/C235N, D93G/S187F/C235S, D93G/S187F/C235V, D93G/S187F/C235R 9.8 to 14 min
60
half-life of wild-type 4 min, of mutant A126C/N152C 40 min, respectively
60
-
15 min, 50% loss of activity
60
-
25% loss of activity within 10 min, 40% loss of activity within 90 min
60
80% loss of activity within 10 min, residual activity stable for at least 50 min
60
rumen microorganism
-
10 min, 25% residual activity for free enzyme, 60% for immobilized enzyme
60
30 min, complete loss of activity
60
30 min, complete loss of activity
60
Q70Y21
almost complete loss of activity within 10 min
60
Thermochaetoides dissita
-
24 h, 73% residual activity
60
Thermochaetoides dissita
24 h, 73% residual activity
60
recombinant enzyme, half-life is 6 h
60
recombinant enzyme, inactivation
65
-
purified enzyme, 98% loss of activity within 5 min
65
half-life of mutant T27I/S84L/V161I/G243C 4 h, mutant T27I/S84L/V161I/H195L/G243C/A259V 140 h, respectively
70
-
stable up to
70
wild-type half-life 1.6 min, half-lifes of mutants D93G/S187/C235I, D93G/S187F/C235N, D93G/S187F/C235S, D93G/S187F/C235V, D93G/S187F/C235R 21 to 63 min
70
-
15 min, 80% loss of activity
70
-
purified native enzyme, 60 min, over 70% residual activity
70
-
activity rapidly decreases above, loses 30% activity after 15 min
70
recombinant enzyme, half-life is below 1 h
70
recombinant enzyme, inactivation
75
purified recombinant His-tagged enzyme, inactivation
75
-
purified enzyme, complete loss of activity within 5 min
75
purified recombinant His-tagged enzyme, inactivation
80
-
purified native enzyme, 60 min, over 34% residual activity
80
recombinant enzyme, half-life is 2.5 h
80
recombinant enzyme, inactivation
additional information
mutations T57I, V178A, and K37I are beneficial to the thermostability of AnFaeA with 1.5-3fold improvement in half-life
additional information
-
mutations T57I, V178A, and K37I are beneficial to the thermostability of AnFaeA with 1.5-3fold improvement in half-life
additional information
the unfolding of the parental enzyme is irreversible on all the tested conditions, while that of the Cys235 mutants is reversible, and their ability to refold is highly dependent on the denaturing temperature. Mutants denatured at 75°C are able to efficiently reverse the unfolding to regain native structure during the cooling process
additional information
-
the unfolding of the parental enzyme is irreversible on all the tested conditions, while that of the Cys235 mutants is reversible, and their ability to refold is highly dependent on the denaturing temperature. Mutants denatured at 75°C are able to efficiently reverse the unfolding to regain native structure during the cooling process
additional information
-
the enzyme retained 85% of its activity at 70°C while obove that temperature the catalytic ability is lost quickly