1.11.1.10: chloride peroxidase
This is an abbreviated version!
For detailed information about chloride peroxidase, go to the full flat file.
Word Map on EC 1.11.1.10
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1.11.1.10
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fumago
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caldariomyces
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horseradish
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chlorination
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peroxidases
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halogen
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halide
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haloperoxidase
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bromination
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lactoperoxidase
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inaequalis
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ferryl
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curvularia
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soret
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bromoperoxidase
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monochlorodimedone
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low-spin
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p450cam
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vanadium-dependent
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thioanisole
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peroxidase-catalyzed
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thiolate-ligated
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pyrrocinia
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oxoferryl
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n,n-dimethylaniline
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peroxygenases
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agrocybe
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vanadium-containing
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hypohalous
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aegerita
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degradation
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synthesis
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environmental protection
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biotechnology
- 1.11.1.10
- fumago
-
caldariomyces
- horseradish
-
chlorination
- peroxidases
-
halogen
- halide
- haloperoxidase
-
bromination
- lactoperoxidase
- inaequalis
-
ferryl
-
curvularia
-
soret
-
bromoperoxidase
- monochlorodimedone
-
low-spin
-
p450cam
-
vanadium-dependent
- thioanisole
-
peroxidase-catalyzed
-
thiolate-ligated
- pyrrocinia
-
oxoferryl
- n,n-dimethylaniline
-
peroxygenases
-
agrocybe
-
vanadium-containing
-
hypohalous
- aegerita
- degradation
- synthesis
- environmental protection
- biotechnology
Reaction
Synonyms
CCPO, Chloride peroxidase, chloroperoxidase, chloroproxidase, CPO, CPO-I, CPO2, haeme-thiolate peroxidase, heme-containing CPO, heme-thiolate chloroperoxidase, More, peroxidase, chloride, Vanadium chloride peroxidase, vCPO
ECTree
1.11.1.10 chloride peroxidaseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 1.11.1.10 - chloride peroxidase
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
20 - 70
the immobilized CPO retains more than 60% of its initial activity after 10 h incubation at 50ºC, while free CPO completely loses its activity. At 70°C, free CPO keeps only about 10% of its initial activity, while immobilized MGO-CPO retains approximately 30% of initial activity after 1 h
25
35
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at 35°C, the reaction rate initially increases, but the enzyme rapidly becomes inactivated and the reaction rate decreases
40
40 - 50
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thermostability is greatly improved in a reverse micelle composed of surfactant-water-isooctane-pentanol: at 40°C, CPO essentially loses all its activity after 5 h incubation, while 58-76% catalytic activity is retained for both reactions in the two reverse micelle media. At 50°C, about 44-75% catalytic activity remains for both reactions in reverse micelle after 2 h compared with no observed activity in pure buffer under the same conditions
45 - 55
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at 45°C, the conjugated-CPO preserved loses about 7% of its initial activity whereas the free enzyme loses about 34% of its initial activity during a 120 min incubation period. At 55°C, the conjugated-CPO and free CPO retain their activity about to a level of 53% and 11%, respectively
50
60
70
80
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1 h, about 95% loss of activity of crystals cross-linked with glutaraldehyde and complete than 90% loss of activity of soluble enzyme
90
free CPO can remain below 15% of its initial activity after 1 h incubation at 90°C, while the immobilized enzyme can keep about 30% of activity at the same condition
additional information
25
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about 95% loss of activity of the pure enzyme in 0.05 M citrate buffer, pH 5, about 60% loss of activity in presence of 0.1 M PEG 200 and PEG 400, about 40% loss of activity in presence of 0.1 M di(ethylene glycol), about 80% loss of activity in presence of 0.1 M di(propylene glycol)
25
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the activity of CPO is almost demolished in the presence of 0.01 M glucose after only 9 h. Dioctyl sulfosuccinate sodium salt, PEG200, and glycerol exhibit strong stabilizing effect and are capable of preventing CPO from inactivation in the 432 h incubation period
40
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the stability of CPO is decreased by glucose, fructose, galactose, xylose, dextran, and surfactant dioctyl sulfosuccinate sodium salt. Stability can be increased by PEG200, glycerol, trehalose, and gum sugar. In the absence of the additives, CPO loses almost all of its activity after 90 h. However, in PEG200 solutions, 88.5% activity is retained after 329 h. The storage time of CPO in trehalose and gum sugar can be prolonged to 233 and 113 h, respectively
50
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1 h, 50% loss of activity of crystals cross-linked with glutaraldehyde and of soluble enzyme
50
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6 h, native CPO retains about 10% peroxidase activity and 20% sulfoxidation activity in aqueous buffer. CPOs modified by citraconic anhydride, phthalic anhydride or maleic anhydride, retain about 30% peroxidase activity and 30% sulfoxidation activity
50
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t1/2 of the free enzyme is 148.9 min, t1/2 for immobilized enzyme is 285.7 min
50
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the native enzyme loses almost all of its activity after 10 h of incubation, in 0.2 M glycerol the enzyme retains activity for up to 200 h. In the presence of 0.05 M PEG200, the enzyme remains as active as freshly prepared samples in the first 10 h. After 192 h of incubation, 13% activity could still be retained. Enzyme retains 24% of its activity after 24 h of standing in dextran-containing buffers
50
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40% activity after 40 min for immobilized enzyme, 0.02% activity after 40 min for free enzyme
50
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pH 5.0, native CPO, half-live 2 h. All chemically modified CPOs are more stable than the native CPO
60
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1 h, about 10% loss of activity of crystals cross-linked with glutaraldehyde and more than 90% loss of activity of soluble enzyme
60
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activity of CPO is almost completely lost in the first 50 min of incubation in the absence of additives. In the presence of PEG200, trehalose, galactose, glycerol, gum sugar, and dextran, 26.5%, 17.7%, 15.6%, 12.4%, 2.6%, and 1.7%, respectively, of enzyme activity can be rescued
60
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t1/2 of the free enzyme is 25.6 min, t1/2 for immobilized enzyme is 34.1 min
60
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after 1 h: approximately 60% residual activity for cross-linked enzyme aggregates, free enzyme is deactivated (<5% residual activity)
70
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1 h, about 10% loss of activity of crystals cross-linked with glutaraldehyde and more than 95% loss of activity of soluble enzyme
70
free CPO can remain only 16.2% of its initial activity after 1 h incubation at 70°C, while the immobilized enzyme can keep almost 100% of activity at the same condition
additional information
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crystal crosslinking with glutaraldehyde yields a chloroperoxidase preparation with enhanced thermal resistance compared to soluble enzyme
additional information
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PEG200 and glycerol are the most efficient stabilizer for CPO in temperatures ranging from 25°C to 60°C
additional information
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the thermostability of peroxidase of CPO is increased about 2fold upon these chemical modification by citraconic anhydride, phthalic anhydride or maleic anhydride. The thermostability of sulfoxidation activity of CPO is increased about 1.2fold upon these chemical modification by citraconic anhydride, phthalic anhydride or maleic anhydride
