1.11.1.19: dye decolorizing peroxidase
This is an abbreviated version!
For detailed information about dye decolorizing peroxidase, go to the full flat file.
Word Map on EC 1.11.1.19
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1.11.1.19
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peroxidases
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heme
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lignin
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auricula-judae
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thanatephorus
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cucumeris
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veratryl
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auricularia
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irpex
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ligninolytic
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lacteus
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lignin-degrading
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kraft
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adusta
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bjerkandera
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chlorite
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nonphenolic
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2,6-dimethoxyphenol
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sapidus
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lignin-derived
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paper production
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degradation
- 1.11.1.19
- peroxidases
- heme
- lignin
- auricula-judae
-
thanatephorus
- cucumeris
-
veratryl
-
auricularia
- irpex
-
ligninolytic
- lacteus
-
lignin-degrading
-
kraft
- adusta
- bjerkandera
- chlorite
-
nonphenolic
- 2,6-dimethoxyphenol
- sapidus
-
lignin-derived
- paper production
- degradation
Reaction
Synonyms
AnaPX, AncDyPD-b1, DtpA, dye decolorizing peroxidases type B, dye-decolorizing peroxidase, DyP, DyP I, DyP II, DyP-I, DyP-type peroxidase, DyP-V, DyP1, DyP1B, DyP2, DyP3, DyP4, DyPA, EfeB, LiP BA45, LiP-SN, manganese-independent peroxidase I, manganese-independent peroxidase II, MnP BA30, POX, reactiveblue-5: hydrogen-peroxide oxidoreductase, TT1485, tyrA, YcdB, YfeX, YRW2 Mb, YwbN
ECTree
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pH Stability
pH Stability on EC 1.11.1.19 - dye decolorizing peroxidase
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2 - 4
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the enzyme maintains 50% of its original activity at pH 2.0 and 4.0 after incubation for 9 and 5 h at 50°C, respectively
742674
2 - 5.5
the enzyme activity is more than 90% between pH 2.0 and 5.5 after 1 h of incubation
765425
2.5
2.5 - 5
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isozymes DyP1, DyP2 and DyP3 are completely inactivated at pH 2.5. Isozymes DyP1, DyP2 and DyP3 exhibit approximately 20% activity at pH 3.0. Isozymes DyP1 and Dyp2 show almost 100% activity at pH 3.5, isozyme DyP3 shows about 95% activity at pH 3.5. Isozyme DyP1 shows less than 50% activity at pH 4.0, isozymes DyP2 and Dyp3 show about 50% activity at pH 4.0. Isozymes Dyp1, DyP2 and Dyp3 show about 30% activity at pH 4.5 and about 20% activity at pH 5.0
712519
3 - 5
-
the enzyme maintains 50% of its original activity at pH 3.0 and 5.0 after incubation for 10 and 6 h at 40°C, respectively
742674
3 - 6
3.5 - 9.5
when maintained at 40°C for 20 min, the enzyme is stable at pH values between 3.5 and 9.5. The enzyme shows 20% relative activity at pH 3.0 and 10.0, 40% relative activity at pH 4.0, about 65% relative activity at pH 4.5 and 9.0, about 80% relative activity at pH 5.0, more than 90% relative activity at pH 6.0-8.0
695785
4 - 6
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the immobilized enzyme has an optimum stability at pH ranging from 5.5 to 6.0 compared with pH ranging from 4.0 to 5.0 for the free peroxidase. In these pH ranges, both enzymes show 50% activity after 72 h incubation
764337
4 - 9
the enzyme shows more than 80% activity after 24 h at pH 4.0-9.0
743731
5 - 10
the enzyme shows more than 80% activity after incubation at pH 5.0-10.0 for 1 h at 37°C
743647
5 - 9
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more than 50% activity after 24 h between pH 5.0-9.0, total loss of activity after the enzyme is incubated at pH 3.0-4.0, and more than 90% loss of activity at pH 4.5
764606
7 - 10
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the enzyme maintains 100% of its original activity at pH values between 7 and 10 after incubation for 48 h at 40°C
742684
-
at pH 2.5, manganese-independent peroxidase I is quite stable and does not lose any activity within 4 h, while manganese-independent peroxidase II loses about 40% of its activity within the same time
710965
2.5
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the enzyme does not lose any activity during 4 h of incubation at pH 2.5
710977
-
the enzyme is very stable between pH 3.0-6.0 at 4°C, keeping 90% activity after 168 incubation. At 25°C, the enzyme retains 90% activity between pH 5.0 and 6.0 and 60% and 20% at pH 3.0 and 4.0, respectively, after 70 h incubation
765169
3 - 6
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more than 90% of initial free recombinant DyP activity remains active after incubation in citrate buffered solution at pH 3.0-5.0 for 48 h. Adsorption yields of recombinant DyP immobilized on FSM-16 and AlSBA-15 increases as pH decreased from 6.0 to 3.0, however, the activity yield of immobilized recombinant DyP decreases with decreasing pH
712777
3 - 6
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the adsorption yields of recombinant DyP immobilized in synthesized silica-based mesocellular foam increases as the pH decreased from 6.0 to 3.0, however, the activity yields of the immobilized recombinant DyP decreases with decreasing pH
712788