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20 - 60
Pichia putida
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10% loss of activity at 20°C after 24 h, complete loss of activity after 10 min at 60°C
22
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50% loss of activity after 10 min in 0.1 M potassium phosphate buffer, pH 6.0. 50% loss of activity after 60 min in 0.1 M potassium phosphate buffer, pH 7.0, 50% loss of activity after 28 h in 0.1 M Tris-HCl buffer, pH 8.0. 50% loss of activity after 16 h in 0.1 M Tris-HCl buffer, pH 9.0
25
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pH 5.0, 3 h, complete inactivation at pH 5.0 after 3 h
35
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30 min, loss of 50% activity, inactivation after 100 min
37
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the enzyme loses its activity after 5 h and 15 h at pH 3.0 and pH 7.0, respectively
40 - 80
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the immobilized enzyme is fairly stable at temperature up to 60°C. Above 70°C, its activity declines rapidly as the temperature increased, but the immobilized enzyme is not completely inactivated even at 80°C
42
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purified recombinant His-tagged enzyme, pH 8.0, 60 min, stable
51
melting temperature of mutant F101S, 5 mM phoshate buffer pH 7.5
58
melting temperature of wild-type, 5 mM phoshate buffer pH 7.5
65
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15 min, complete inactivation above
30
wild-type, stable for at least 3 h
30
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the enzyme is highly temperature-sensitive, loss of 20% activity within 100 min
30
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the half-life of the encapsulated enzyme (about 59.4 h) is 20fold higher than the free enzyme (about 3 h) at 30°C
30
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20 min, more than 80% residual activity, recombinant protein
30
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15 min, about 30% loss of activity
30
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pH 6.0-8.5. 60 min, stable
32
melting temperature of wild-type
32
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2 h, 80% loss of activity
4
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24 h, loss of only 5% of activity
4
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1 month, more than 50% of the activity is retained
40
mutant S101A/V355T/F357R/M359R, 3 h, 10% residual activity. Mutant S101A/D250G/F253R/V355T/F357R/M359R, 3 h, almost 50% residual activity
40
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0.1 M potassium phosphate buffer, pH 7.0, 20 min, almost all the enzyme activity remains
40
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inactivation after 30 min
40
6 h, 40% residual activity
40
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the enzyme activity is enhanced to 2fold by incubation at pH 6.0 and 40°C for 60 min, whereas the Km values for ethanol and ethylene glycol do not change
40
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15 min, about 85% loss of activity
45
Hansenula sp.
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pH 7, 10 mM sodium phosphate, about 40% loss of activity after 3 h, about 40% loss of activity after 6 h, about 70% loss of activity after 23 h. Stabilizing immobilization by ionic adsorption on agarose coated with 600 kDa polyethylenimine. The adsorption of the proteins on the polymeric bed allows the stabilization of the quaternary structure. The effect of the enzyme concentration on thermal enzyme stability disappears in these immobilized preparations. A high stability is obtained without a significant decrease in enzyme activity during immobilization (recovered activity was over 50%)
45
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pH 7, 10 mM sodium phosphate, about 50% loss of activity after 3 h, about 60% loss of activity after 6 h, about 80% loss of activity after 23 h. Stabilizing immobilization by ionic adsorption on agarose coated with 600 kDa polyethylenimine. The adsorption of the proteins on the polymeric bed allows the stabilization of the quaternary structure. The effect of the enzyme concentration on thermal enzyme stability disappears in these immobilized preparations. A high stability is obtained without a significant decrease in enzyme activity during immobilization (recovered activity was over 50%)
45
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free enzyme loses more than 40% of its initial activity within 2 h at 45°C
45
24 h, more than 65% reisudal activity, immobilized enzyme. The free AOX retains only 15% activity
45
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60 min, stable below
45
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pH 7, 10 mM sodium phosphate, 1 h, 90% loss of activity
50
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0.1 M potassium phosphate buffer, pH 7.0, 20 min, about 60% of the activity remains
50
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purified recombinant His-tagged enzyme, pH 8.0, 50 min, 50% activity remaining
50
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20 min, more than 40% residual activity for recombinant protein, complete loss of activity for native protein
50
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30 min, enzyme retains full activity
50
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60 min, inactivation
50
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15 min, complete inactivation
50
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pH 7.5, 15 min, stable below
52
metling temperature of mutant S101A/D250G/F253R/V355T/F357R/M359R
52
melting temperature of mutant F101N, 5 mM phoshate buffer pH 7.5
55
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0.1 M potassium phosphate buffer, pH 7.0, 20 min, about 25% of the activity remains
55
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purified recombinant His-tagged enzyme, pH 8.0, 30 min, inactivation
55
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15 min, pH 8.0, purified extracellular enzyme, completely stable
55
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15 min, 34% loss of activity
60
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0.1 M potassium phosphate buffer, pH 7.0, 20 min, complete inactivation
60
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10 min, complete inactivation
60
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30 min, enzyme is almost completely inactivated
60
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15 min, pH 8.0, purified intracellular enzyme, completely stable
additional information
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in a commercial preparation, one of AOX's isozymes is more resistant to thermal inactivation at atmospheric or high pressures. The resistant fraction is 4-34 times more stable than the labile fraction. High hydrostatic pressure stabilizes AOX against thermal inactivation. A 14fold stabilization is observed at 49.4°C for the labile fraction at 200 MPa relative to atmospheric pressure. The activation energy of inactivation at 40-160 MPa ranges from 95 to 184 kJ per mol for the resistant fraction and from 232 to 402 kJ per mol for the labile fraction
additional information
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there are two fractions of AOx with different thermal stability. High hydrostatic pressure increases the activity of the heat labile (L) + resistant (R) combined fractions but not of the R fraction alone. The activity of the L + R fractions increases 2.4fold at 160 MPa and 30°C compared to the activity at 0.1 MPa. At higher temperatures, the increase in activity with pressure is greater due to the combined stabilization and activation effects. The reaction rate of the R fraction at 50 °C is 17.9 or 17.7 microM min-1 at 80 or 160 MPa, respectively, and is not significantly different from the activity of the L + R fractions under the same conditions (18.4 micro min-1)
additional information
presence of alginic acid (0.35%) enhances thermal stability, resulting in 72% increase in its half-life at 40°C under the operational conditions
additional information
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presence of alginic acid (0.35%) enhances thermal stability, resulting in 72% increase in its half-life at 40°C under the operational conditions