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30 - 40
inactivation of recombinant PL I occurs above 30°C whereas the activity of native PL I is stable up to 40°C
30 - 60
PelA is stable during 30°C to 40°C and not very stable at 50°C (in 50 mM glycine-NaOH buffer, pH 10.0), about 60% activity is retained after 30 min incubation at 50°C and it almost completely loses activity when it is incubated at 60°C
35 - 45
-
optimal stability
37 - 50
-
purified recombinant His-tagged enzyme, 45 min, without substrate, pH 9.0-12.0, over 80% activity remaining
39
-
transition midpoint of pectate lyase C is 38.9°C
40 - 70
the enzyme loses 60% of its activity when incubated at 40°C for 1 h after treatment with EDTA, thermostability increases to approximately 80% of initial activity at 50 and 70°C in the presence of Ca2+ alone and both Ca2+ and polygalacturonic acid, respectively
44
-
transition midpoint of pectate lyase C is 44.3°C
45 - 50
purified recombinant PelN displays a half-life of around 9 h and 42 h at 50°C and 45°C, respectively
47.9
melting temperature, mutant N198Q
48.7
melting temperature, mutant N198D
48.9
melting temperature, mutant N198A
50.7
melting temperature, mutant N95S
55 - 70
more than 80% of the original enzyme activity is retained in Tris-HCl buffers with pH 7 and 8, after incubation for 30 min
57
-
20 min, complete inactivation
60 - 95
-
the enzyme keeps stable, possesses a high level of activity at 60°C and a half-life of almost 2 h at 95°C
86
melting temperature, presence of 0.6 mM Ca2+
2
-
48 h, enzyme from Alpine strain A15 loses 21% of initial activity
2
-
48 h, enzyme from Siberian strain AG25 loses 5% of initial activity
30
-
half-life: more than 75 h
30
-
purified recombinant enzyme, pH 9.0, 2 h, over 90% activity remaining
30
Erwinia aroidea
-
pH 7.0-8.5, stable
30
-
pH 9.0, 15 min, enzyme from Alpine strain A15 loses 40% of initial activity
30
-
pH 9.0, 15 min, enzyme from Siberian strain AG25 loses 35% of initial activity
30
-
room temperature, activity is lost within 2 days
30
-
pH 6.0-9.0, 3 h, stable
37
-
pH 6.5-9.6, 2 h, stable
37
-
purified recombinant His-tagged enzyme, 1 h, without substrate, pH 12.0, over 58% activity remaining
37
-
purified recombinant His-tagged enzyme, 1 h, without substrate, pH 7.0-10.0, over 80% activity remaining
40
pH 10.0, 4 h, retains more than 50% of the initial activity
40
-
purified recombinant enzyme, pH 9.0, 2 h, over 80% activity remaining
40
-
pH 9.0, 15 min, enzyme from Alpine strain A15 loses 10% of initial activity
40
-
pH 9.0, 15 min, enzyme from Siberian strain AG25 loses 95% of initial activity
40
-
5 min, 5-10% loss of activity
40
purified recombinant His-tagged enzyme, half-life is 288 min at pH 10.0
40
-
3 h, 93% loss of activity without CaCl2, 14% loss of activity in presence of 0.1 mM CaCl2
40
-
pH 7.0, 10 min, stable below
40
1h, more than 60% residual activity
40 - 50
-
pH 6.0, 30 min, stable
40 - 50
2 h, 90% residual activity
45
-
pH 9.4: stable for 300 h. pH 10.0: about 40% loss of activity after 300 h
45
-
10 min, about 10% loss of activity
45
purified recombinant enzyme, 2 h, 64.9% activity remaining, half-life is 360 min
47
-
20 min, stable
47
-
transition midpoint of pectate lyase C is 46.9°C
50
-
half-life: 1 h
50
EDW21517
half-live of inactivation is 2.7 min for wild-type, 3.1 min for mutant R227W, 6.9 min for mutant R227W/S145C/T50T, 190.5 min for mutant R227W/T206A/T222T, 800.3 min for mutant R227W/S145C/T206A
50
-
30 min, stable up to
50
pH 10.0, 4 h, retains only 1% of the initial activity
50
time at which the enzyme loses 50% of its initial activity, i.e. t50 value, is 10 min for wild-type, 240 min for mutant N186D/I211V/A254T/S271G/N289H, 1400 min for mutant E124I/T178A/N186D/I211V/A254T/S271G/N289H, respectively
50
-
purified recombinant enzyme, 2 h, 90% activity remaining
50
half-life 55 min, recombinant protein
50
-
half life: 11 min for isoenzyme PelA, 4 min for isoenzyme PelD, 2 min for isoenzyme PelE
50
-
recombinant enzyme, 90 min, 50% activity remaining
50
Erwinia aroidea
-
10 min, 50% loss of activity
50
-
10 min, about 35% of maximal activity
50
purified recombinant His-tagged enzyme, stable up to for 3 h, half-lives at pH 7.0-11.0 are 327-103 min, half-life of 147 min at pH 10.0, overview
50
-
10 min, stable in absence of Ca2+
50
-
1 h, loss of activity
50
-
10 min, pH 7.0, 35% loss of activity
50
-
purified recombinant His-tagged enzyme, 45 min, without substrate, pH 10.0, over 80% activity remaining
50
purified recombinant enzyme, half-life is 88 min
52
-
20 min, 38% loss of activity
52
melting temperature, wild-type
55
-
stable up to, in absence of CaCl2
55
enzyme is stable to incubation up to 55°C when incubated at various temperatures for 20 min in glycine-NaOH buffer (pH 9.4)
55
-
10 min, about 80% of maximal activity
55
-
10 min, stable in presence of Ca2+
60
Aspergillus luchuensis var. saitoi
-
1 h, 71% residual activity
60
-
readily inactivated above
60
-
Ca2+ slightly enhances thermostability up to 60°C
60
pH 7.5, stable in presence of Ca2+
60
-
pH 9.0, 15 min, about 20% loss of activity
60
purified enzyme, 20 min, recombinant enzyme from Pichia pastoris retaines 26% activity, recombinant enzyme from Escherichia coli is inactivated
60
-
purified recombinant enzyme, pH 9.0, half-life is 20 min, inactivation after 80 min
60
-
half-life: 20-30 min for isoenzyme PelB and PelC, isoenzymes PelA, PelD and PelE loses more than 80% of activity after 2 min
60
-
10 min, 50% loss of activity in absence of cations, 10% loss of activity in presence of Mn2+, Ca2+ or polygalacturonic acid
60
-
30 min, more than 30% of the activity remains
60
purified recombinant His-tagged enzyme, half-life is 207 min at pH 10.0
60
-
purified native Pel1, half-life is 14.2 min at pH 7.0, 16.4 min at pH 9.0, the half-life is increased by Ca2+
60
-
purified recombinant His-tagged enzyme, 45 min, without substrate, pH 10.0, 30% activity remaining
65
-
half-life: 13 h
65
-
10 min, 50% loss of activity
70
-
half-life 18 h
70
Aspergillus luchuensis var. saitoi
-
1 h, 61% residual activity
70
-
beyond 70°C, enzyme activity is severely inhibited. The half-life is 6.93 min at 70°C as compared to 31 min at 40°C
70
-
pH 9.0, 15 min, 50% loss of activity
70
-
purified recombinant enzyme, pH 9.0, half-life is about 12 min, inactivation after 60 min
70
purified recombinant His-tagged enzyme, half-life is 120 min at pH 10.0
70
-
2 h, about 10% loss of activity
70
pH 7, 10 min, absence of substrate, stable
75
-
10 min, thermal denaturation is reversible
75
-
15 min, 60% residual activity
80
-
half-life 12 h
80
Aspergillus luchuensis var. saitoi
-
1 h, 46% residual activity
80
-
half-life at pH 8.0 and 7.0 is 1.2 min, half-life at pH 9.0 is 0.8 min
80
-
5 min, complete inactivation
80
-
half-life: about 60 min
90
-
half-life 7 h
90
-
half-life of pectate lyase is 60fold higher in the presence of hydroxyapatite nanoparticles than in the presence of 1 mM CaCl2. Thermodynamic analysis of the nanoparticle-induced stability reveals an enhanced entropy-enthalpy compensation by hydroxyapatite nanoparticles since a reciprocal linearity of the enthalpy-entropy change to 90°C is observed
90
-
complete loss of activity after 5 min
additional information
-
Ca2+ slightly enhances thermal stability
additional information
Ca2+ increases thermal stability of the enzyme slightly
additional information
-
Ca2+ increases thermal stability of the enzyme slightly
additional information
-
thermal denaturation is not reversible. The enzyme has its maximal thermal stability at pH 5, CD-monitored thermal denaturation
additional information
-
improvement of thermostability and activity of pectate lyase in the presence of hydroxyapatite nanoparticles
additional information
-
Ca2+ and sodium polygalacturonate improve thermal stability
additional information
-
Ca2+ slightly enhances thermal stability