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15 - 70
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the enzyme shows a pH-dependent response to the high pressure homogenization treatment, with reduction or maintenance of activity at pH 4.5-6.0 and a remarkable activity increase (30-300%) at pH 6.5 at all tested temperatures. i.e. 15°C, 50°C and 75°C. The enzyme's thermal tolerance is reduced due to high pressure homogenization treatment and the storage for 24 h at high temperatures of 50°C and 75°C also causes a reduction of activity
20 - 40
50% of enzyme activity is maintained after 90 min incubation at 20-40°C
20 - 60
the activity of recombinant GOD increases slightly at the reaction temperature ranging from 20-40°C, and then falls moderately till 60°C. The recombinant enzyme retains more than 90% of activity within 40°C. Over 30% of activity is lost at 50°C, whereas almost no activity is detected above 60°C
25
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10 h, purified enzyme, stable
25 - 70
-
70% relative activity after 30 min at 25°C, 100% activity after 30 min at 30°C, 90% relative activity after 30 min at 37°C, 75% relative activity after 30 min at 50°C, 30% relative activity after 30 min at 70°C
30 - 50
purified recombinant free enzyme and immobilized enzyme, the enzyme activity remains rather unchanged from 30-45°C and then drops at higher temperatures. The thermal stability of immobilized GOx is only slightly higher than that of the free enzyme
4 - 54
-
1 h, the enzyme retains at least 80% activity
40 - 60
purified recombinant enzyme, more than 90% activity remaining after incubation for 30 min at 50°C and 54% at temperatures up to 55°C
45 - 65
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at 45°C the enzyme half-life is 99 min and at 65°C it is 20.38 min under similar conditions
47
-
after 6 h of incubation the percentage of activity is 68%
50 - 60
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at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h, thermal denaturation is observed above 60°C
50 - 70
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the half-life is diminished from 210 min at 50°C to 0.61 min at 70°C, the inactivation rate constant decreases by up to 50% at temperatures between 50 and 70°C in the presence of 0.6 M trehalose
50.6
Tm-value of wild-type enzyme: 50.6°C
54
-
after 6 h of incubation the percentage of activity is 11%
55.8
-
transition temperature is independent of the protein concentration. The thermally denatured enzyme is a compact structure, a form of molten globule-like apoenzyme
56
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half-life of native enzyme without additive: 86 min, half-life of enzyme in presence of lysozyme: 322 min, half-life of enzyme in presence of 1 M NaCl: 1806 min, half-life of enzyme in presence of 0.2 M K2SO4: 1446 min
58.6
Tm-value of mutant enzyme Y169C/A211C
59
-
midpoint for thermal inactivation of residual activity and dissocation of FAD
62
-
midpoint for loss of secondary and tertiary structure
63
-
half-life of native enzyme without additive: 7.5 min, half-life of enzyme in presence of lysozyme: 24 min, half-life of enzyme in presence of 1 M NaCl: 146 min, half-life of enzyme in presence of 0.2 M K2SO4: 62 min
67
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half-life of native enzyme without additive: 4.5 min, half-life of enzyme in presence of lysozyme: 12 min, half-life of enzyme in presence of 1 M NaCl: 58 min, half-life of enzyme in presence of 0.2 M K2SO4: 27.5 min
72.4
-
denaturation point of native enzyme
72.8
-
denaturation point of periodate-oxidized enzyme
73
-
70% loss of activity after 60 min
75
purified recombinant free enzyme, loss of 50% activity
30
-
purified enzyme, completely stable for at least 180 min
30
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stable for a minimum of 180 min
30
1 h, 10% loss of activity, recombinant enzyme
30
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after 6 h of incubation the percentage of activity is 79%
35
-
half-life: 78.48 h
37
-
GOD has half-life of approximately 30 min at 37°C, immobilized GOD is more effective for applications at 37°C
37
-
at 37°C and in pH 7.5 buffer, the half life of the native enzyme is 48 h
37
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loss in specific activity of PEGylated GOx and native GOx in the absence of glucose and at 37°C, the PEGylated enzyme is more stable and retains 62.6% after 24 h and about 40% after 30 days, the native enzyme retains 67.3% after 24 h and about 20% after 30 days, overview
37
-
at 37°C and in pH 7.5 buffer, the half life of the recombinant enzyme yGOXpenag is 6 h
37
-
half-life: 30 min, purified enzyme
40
-
60 min
40
-
at or below both the BTL wild-type strain enzyme and the commercially available enzyme are stable for at least 48 h
40
-
up to, soluble enzyme
40
-
purified enzyme, half-life: 30 min
40
1 h, no loss of activity, mutant enzyme Y169C/A211C. Half-life of mutant enzyme Y169C/A211C: 720 min. Half-life of wild-type enzyme: 15 min
40
-
up to, soluble enzyme
40
-
at pH 2-4 and pH 7-8, half life: less than 1 day
40
half-life native enzyme: 103 min, half-life recombinant enzyme: 26 min
45
-
bound to Blue Dextran, in the absence of added FAD, 60% activity retained after 3 h
45
1 h, complete loss of activity, recombinant enzyme. 30 min, 60% loss of activity, mutant enzyme Y169C/A211C
45
-
30 min, considerable inactivation
45
half-life native enzyme: 23 min, half-life recombinant enzyme: 3 min
50
-
up to, immobilized enzyme
50
-
both native and carbonhydrate-depleted enzyme retain full activity below
50
-
up to, native and deglycosylated enzyme
50
-
the poly(methyl methacrylate)-bovine serum albumin particle-adsorbed GOx only loses 28% of its activity in comparison with a 64% activity loss of free GOx when it is incubated at 50°C for 35 h
50
stable up to. At 50°C the enzyme is inactivated by 30% over a period of 11 h. The thermal stability is unaffected by the depletion of carbohydrate
50
the purified recombinant enzyme retains 90% activity at 50°C for 30 min
50
-
the activity of the free enzyme decreases to 30% of the original value, the activity of the immobilized enzyme scarcely decreases
50
-
at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h, thermal denaturation is observed above 50°C
50
-
stable below, pH 5.6 for 15 min
55
-
native and carbohydrate-depleted enzyme, inactivation above
55
-
bound to Blue Dextran, in the absence of added FAD, 20% activity retained after 3 h
55
-
the commercially available enzyme is more stable than the BTL wild-type strain enzyme
55
purified dimeric enzyme, pH 5.8, stable up to, rapid inactivation above, the enzyme forms aggregates at incubation temperatures above 55°C, overview
55
-
purified enzyme, retains 57 % activity after 180 min
60
-
affinity-layered preparation retains 55% of the original activity after 2 h of preincubation, soluble enzyme loses almost 80% activity in 15 min
60
-
half-life of native enzyme without additive: 13 min, half-life of enzyme in presence of lysozyme: 46 min, half-life of enzyme in presence of 1 M NaCl: 434 min, half-life of enzyme in presence of 0.2 M K2SO4: 308 min
60
-
2 h, stable, insoluble enzyme complex
60
purified enzyme, residual activity after 10 min is 32.9% for the wild-type enzyme and 14.7% for enzyme mutant M12
60
t1/2: 10.5 min (wild-type enzyme), 9.0 (mutant enzyme T30V/I94V/A162T), 11.74 (mutant enzyme T30V/I94V/A162T/R537K/M556V), 15.75 (mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V)
60
cellular organism
-
complete inactivation
65
-
the commercially available enzyme is more stable than the BTL wild-type strain enzyme
65
-
purified enzyme, loss of 50% activity after 27 min
65
-
soluble enzyme: inactivation, mycelia-bound: 85% activity retained
70
t1/2: 5 min
70
-
purified enzyme, inactivation
70
-
native GOx retains 48% activity after 10 min, the bioactivity is completely lost after 1 h at 70°C. The bioactivity of the enzyme-polymer conjugates (GOx-PPEG-A, GOx-PAA, GOx-PMA and GOx-PTBA) only slowly declines, GOx-PPEG-A, GOx-PAA, GOx-PMA and GOx-PTBA retain about 61%, 67%, 79%, and 73%, after 10 min and 28%, 24%, 35%, and 37% after 1 h, respectively, at 70°C. The four polymers, hydrophilic or hydrophobic, improve the thermal stability of enzyme GOx. Enzyme modified by hydrophobic polymers (PMA and PTBA) exhibit better thermal stability than that modified by hydrophilic ones (PPEG-A and PAA)
70
-
inmobilized enzyme, more than 60% of the activity remains
70
-
completely inactivated after 15 min in the absence of glucose and 50% inactivated in the presence of glucose
80
-
the pure enzyme is inactive at 80°C, thermal resistance is high only at pH 7.0
80
purified recombinant immobilizedenzyme, loss of 50% activity
80
at 240 MPa and 80.0°C, the first order rate constant of inactivation (k(inact)) of aniline-modified enzyme is 0.02/min, or 3.7 times smaller than for the native enzyme, while the k(inact) for benzoate-modified enzyme is 0.26/min, or 2.8times smaller than for the native enzyme at the same temperature. At 240 MPa and 80.0°C, the k(inact) of the aniline-modified enzyme is 69times smaller than the k(inact) of native enzyme (15.3/min) at 0.1 MPa and 80.0°C
additional information
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comparison of stability of enzyme from different sources
additional information
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the enzyme is very stable at cold temperatures
additional information
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native and carbohydrate-depleted enzyme, no decrease of activity after 100 freeze-thaw cycles
additional information
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the irreversible nature of thermal inactivation is caused by a change in the state of association of apoenzyme. The dissociation of FAD results in the loss of secondary and tertiary structure, leading the unfolding and nonspecific aggregation of the enzyme molecule because of hydrophobic interactions of side chains
additional information
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thermal denaturation of glucose oxidase is an irreversible transition to the compact denatured form with a defined oligomeric structure that is significantly different from the chemically denatured state of the enzyme, unfolded monomer
additional information
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inactivation of the free enzyme within 10 min. Microencapsulation improves the thermal stability of GOx at temperatures up to 60°C due to stabilization of its active conformation but reduces the thermal stability of laccase because of the increased coordination between poly(ethyleneimine) and copper atoms in the enzyme's active site, 70% remaining activity after 60 min
additional information
analysis of thermal inactivation kinetics of enzyme GOD
additional information
glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification, method development, evaluation, and kinetics of thermal inactivation, detailed overview. Determination of the effect of temperature on the rate constant of inactivation of GOx at each of the selected pressures, and of the pressure effects on the rate constant of inactivation of GOx
additional information
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thermal inactivation thermodynamic parameters of GOx, overview
additional information
wild-type and mutant enzyme Y169C/A211C are cold adapted
additional information
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wild-type and mutant enzyme Y169C/A211C are cold adapted
additional information
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comparison of stability of enzyme from different sources
additional information
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enzyme denaturing process at different temperatures, localization of breaking points, analysis by molecular dynamics simulations, overview. Identification of the transition state of protein folding/unfolding, overview
additional information
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glucose stabilizes against heat inactivation