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1 - 10
activity range, profile overview
1 - 4.5
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activity range, profile overview
1 - 5
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activity range of wild-type and mutant enzyme, profile overview
1 - 8
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pH profile, overview
1.5 - 3
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pH 1.5: about 50% of maximal activity, pH 3.0: about 55% of maximal activity. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
1.5 - 6.5
activity range, enzyme mutant R79G, profile, overview
1.8 - 6
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pH 1.8: about 45% of maximal activity, pH 6.0: about 45% of maximal activity
2 - 12
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pH 2.0: about 45% of maximal activity, 12.0: about 25% of maximal activity
2 - 5.7
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pH 2.0: about 10% of maximal activity, pH 5.7: about 40% of maximal activity, hydrolysis of myo-inositol hexakisphosphate
2.5
wild-type enzyme exhibits high activity at, bi-peak profile
2.5 - 3.5
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immobilized enzyme
2.5 - 6
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pH 2.5: about 35% of maximal activity, pH 6.0: about 25% of maximal activity, recombinant enzyme
2.5 - 8
activity range, profile overview, narrow optimum, over 50% activity only at pH 4.0-5.0
2.5 - 8.5
activity range, profile overview, over 50% of activity at pH 3.5-6.5
3 - 6
KM873028
activity range, mesophilic phytase, profile overview
3 - 6.5
activity range, profile overview
3.2 - 5.4
over 70% of the maximum activity within this pH range
3.5 - 6.5
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50% of maximal activity at pH 3.5 and pH 6.5
3.5 - 9
pH profiles of wild-type and mutant enzymes, no activity of mutant enzymes above pH 7.5, overview
3.5 - 9.5
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activity range, profile overview
3.8 - 5.8
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pH 3.8: about 55% of maximal activity, pH 5.8: about 70% of maximal activity
4 - 10
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activity range, pH profile, overview
4 - 5
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pH 3.0: nearly no activity, pH 4.0: optimum, pH 5.0: about 60% of maximal activity, pH 6.0: about 10% of maximal activity, reaction with 4-nitrophenyl phosphate
4 - 7.5
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pH 4.0: about 45% of maximal activity, pH 7.5: about 45% of maximal activitry, Q27T mutant enzyme, phytate as substrate
4 - 8
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pH 4.0: about 50% of maximal activity, pH 8.0: about 25% of maximal activity
4.2 - 6.5
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pH 4.2: about 80% of maximal activity, pH 6.5: about 70% of maximal activity
4.5 - 6.5
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pH 4.5: about 40% of maximal activity, pH 6.5: about 70% of maximal activity, hydrolysis of myo-inositol hexakisphosphate
4.5 - 8
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pH 4.5: about 55% of maximal activity, pH 8.5: about 25% of maximal activity
5 - 10
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pH 5.0: about 50% of maximal activity, pH 10.0: about 80% of maximal activity, presence of 10 mM CaCl2
5 - 7
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pH 5.0: about 90% of maximal activity, pH 7.0: about 50% of maximal activity, at 37°C
5 - 7.5
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pH 5.0: about 70% of maximal activity, pH 7.5: about 50% of maximal activity
5.5
wild-type enzyme exhibits high activity at, bi-peak profile
5.5 - 7.5
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pH 5.5: about 35% of maximal activity, pH 7.5: about 95% of maximal activity
5.6 - 7.4
the activity of the wild-tyype enzyme YmPhWT decreases drastically by 14fold from pH 5.6 to pH 7.4
6.3 - 8
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60-73% of maximal activity within this range
2 - 5.5
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pH 2.0: about 70% of maximal activity, pH 5.5: 40-50% of maximal activity enzyme, recombinant enzyme from different expression systems. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
2 - 5.5
more than 80% of maximum activity
2 - 6
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pH 2.0: about 65% of maximal activity, pH 6.0: about 85% of maximal activity
2 - 6
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2.0: about 55% of maximal activity, pH 6.0: 85% of maximal activity
2 - 6
pH 2.0: about 45% of maximal activiry, pH 6.0: about 50% of maximal activity, substrate: myo-inositol hexakisphosphate
2 - 6
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maximal activity at pH 5.0 followed by pH 2.0 (73% of maximal activity), no activity at pH 7.0-8.0
2 - 7.5
activity range, profile overview
2 - 7.5
activity range, profile overview. sharp drop in activity above pH 6.5
2 - 7.5
activity range, profile overview
2 - 9
activity range, deglycosylated recombinant enzyme
2 - 9
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the pH profile of the enzyme contains peaks at pH 3.0 and pH 7.0, with the activity at pH 3.0 being approximately 70% of the peak activity at pH 7.0
2 - 9
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over 70% of maximal activity within this range, profile overview
2.5 - 5
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pH 2.5: about 45% of maximal activity, pH 5.0: about 20% of maximal activity, reaction with 4-nitrophenyl phosphate, recombinant enzyme
2.5 - 5
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pH 2.5: about 60% of maximal activity, pH 5.0: optimum, pH 6.0: no activity, reaction with phytate, recombinant enzyme
2.5 - 5
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highest activity at pH 2.5, inactive at above pH 5.0
2.5 - 5.5
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pH-activity profile, with optima at pH 2.5 with 60% of maximal activity, and at pH 5.0-5.5 with maximal activity, and a local minimum at pH 3.5
2.5 - 5.5
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about 50% of maximal activity at pH 2.5 and pH 5.5
3 - 5.5
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pH 3.0: about 55% of maximal activity, pH 5.5: about 50% of maximal activity, hydrolysis of 4-nitrophenyl phosphate
3 - 5.5
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optimum pH 5.0, over 80% of maximal activity at pH 3.0-5.5, dramatical loss of activity above pH 5.5
3 - 7
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inactive below pH 3.0 or above pH 7.0
3 - 7
activity range, profile overview. Over 70% of maximal activity at pH 4.5-6.5
3 - 7
activity range, wild-type enzyme, profile, overview
3 - 8
activity range, profile overview
3 - 8
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enzyme is virtually inactive below pH 3.0 and above pH 8.0, phytase LP11, LP12 and LP2
3 - 9
more than 80% of maximum activity
3 - 9
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more than 70% of maximum activity
3.5 - 5.5
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pH 3.5: about 65% of maximal activity, pH 5.5: about 60% of maximal activity, Y27T/K68A mutant enzyme, 4-nitrophenyl phosphate as substrate
3.5 - 5.5
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pH 3.5: about 75% of maximal activity, pH 5.5: about 45% of maximal activity, Q27T mutant enzyme, 4-nitrophenyl phosphate as substrate
3.5 - 6
pH 3.5: about 40% of maximal activity, pH 6.0: about 80% of maximal activity, pH 6.5: about 30% of maximal activity. enzyme expressed in Saccharomyces cerevisiae
3.5 - 6
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pH 3.5: about 50% of maximal activity, pH 6.0: about 30% of maximal activity
3.5 - 6
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activity range, profile, overview
3.5 - 6
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activity range, profile, overview
3.5 - 6
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activity range, profile, overview
3.5 - 7
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pH 3.5: about 35% of maximal activity, pH 7.0: about 70% of maximal activity
3.5 - 7
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pH 3.5: about 35% of maximal activity, pH 7.0: about 70% of maximal activity, reaction with phytate
4 - 6
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pH 3.0: no activity, pH 4.0: optimum, pH 5.0: about 60% of maximal activity, pH 6.0: about 10% of maximal activity, 4-nitrophenyl phosphate as substrate
4 - 6
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pH 4.0: about 35% of maximal activity, pH 6.0: about 50% of maximal activity, myo-inositol hexakisphosphate as substrate
4 - 6
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pH 4.0: about 40% of maximal activity, pH 6.0: about 50% of maximal activity, reaction with phytate
4 - 7
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pH 4.0: about 50% of maximal activity, pH 7.0: about 45% of maximal activity, Y27T/K68A mutant enzyme, phytate as substrate
4 - 7
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enzyme is virtually inactive below pH 4.0 and above pH 7.0
4 - 7
over 50% of maximal activity within this range
4.5 - 5.5
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4.5 - 7
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pH 4.5: about 40% of maximal activity, pH 7.0: about 30% of maximal activity
4.5 - 7
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pH 4.5: about 30% of maximal activity, pH 8.5: about 40% of maximal activity
4.5 - 7
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pH 4.5: about 70% of maximal activity, pH 7.0: about 45% of maximal activity, hydrolysis of myo-inositol hexakisphosphate
4.5 - 8.5
activity range, profile overview
4.5 - 8.5
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pH 4.5: about 30% of maximal activity, pH 6.0: about 80% of maximal activity, pH 8.5: about 75% of maximal activity
6 - 8
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purified recombinant enzyme domains PhyH and PhyH-DII
6 - 9
high activity within this range, profile overview
6 - 9
activity range of recombinant isozyme LlALP2. Maximum activity at pH 8.0, 10% of maximal activity at pH 6.0, 60% of maximal activity at pH 9. The pH activity profile is similar to that of wild-type alkaline phytase isolated from lily pollen
6 - 9
activity range, inactive below and above, profile overview
additional information
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enzyme is able to retain almost complete phytase activity in the presence of commercial livestock feed even after 48 h over various pH tested
additional information
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pH profiles of wild-type and mutant phytases PhyA, overview
additional information
pH profiles of wild-type and mutant phytases PhyA, overview
additional information
mutant enzymes pH profiles, overview
additional information
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mutant enzymes pH profiles, overview
additional information
mutants D461N, G377T, T255E and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme
additional information
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mutants D461N, G377T, T255E and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme
additional information
the two types of phytases are complementary in phytate degradation over the pH range of pH 2.0-9.0
additional information
the two types of phytases are complementary in phytate degradation over the pH range of pH 2.0-9.0
additional information
pH-dependence of wild-type and mutant enzymes, overview