Application | Comment | Organism |
---|---|---|
biotechnology | alkaline phosphatase from Escherichia coli is immobilized by copolymerization with resorcinol. The phosphatase-polyresorcinol complex synthesized retains about 74% of the original enzymatic activity. On addition to soil, free enzyme is completely inactivated in 4 days, whereas the phosphatase-polyresorcinol complex is comparatively stable.Barley seed coated with the immobilized enzyme exhibits higher rhizosphere phosphatase activity. Under pot culture conditions, an increase in the soil inorganic phosphorus is detected when the seed is encapsulated with the phosphatase-polyresorcinol complex, and a positive influence on biomass and inorganic phosphorus concentration of shoot is observed | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
phosphate | - |
Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.07 | - |
4-nitrophenyl phosphate | pH 10.5, 37°C, free-enzyme | Escherichia coli | |
2.44 | - |
4-nitrophenyl phosphate | pH 10.5, 37°C, enzyme immobilized by phosphatase-polyresorcinol complex | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Storage Stability | Organism |
---|---|
the storage stabilities of the immobilized phosphatase are higher than those of the native one | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl phosphate + H2O | - |
Escherichia coli | 4-nitrophenol + phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
alkaline phosphatase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
90 | - |
maximal activity of both free enzyme and enzyme immobilized by phosphatase-polyresorcinol complex | Escherichia coli |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 50 | activity profile of free enzyme is comparable to immobilized enzyme | Escherichia coli |
70 | 90 | at temperature values between 70 and 90°C, the immobilized phosphatase shows an activity about 10% higher than that of the free enzyme | Escherichia coli |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the thermal stabilities of the immobilized phosphatase are higher than those of the native one | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
10.2 | - |
maximal activity of both free enzyme and enzyme immobilized by phosphatase-polyresorcinol complex | Escherichia coli |
10.5 | - |
assay at | Escherichia coli |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5 | 10 | activity profile of free enzyme is comparable to immobilized enzyme | Escherichia coli |
10 | 12 | free enzyme: 60-80% activity, immobilized enzyme: 45-55% activity | Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.069 | - |
phosphate | pH 10.5, 37°C, free-enzyme | Escherichia coli | |
0.423 | - |
phosphate | pH 10.5, 37°C, enzyme immobilized by phosphatase-polyresorcinol complex | Escherichia coli |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
2.8 | - |
pH 10.5, 37°C, free-enzyme | Escherichia coli | phosphate | |
4 | - |
pH 10.5, 37°C, enzyme immobilized by phosphatase-polyresorcinol complex | Escherichia coli | phosphate |