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Literature summary for 3.1.3.1 extracted from

  • Pilar, M.C.; Ortega, N.; Perez-Mateos, M.; Busto, M.D.
    Alkaline phosphatase-polyresorcinol complex: characterization and application to seed coating (2009), J. Agric. Food Chem., 57, 1967-1974.
    View publication on PubMed

Application

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

Inhibitors Comment Organism Structure
phosphate
-
Escherichia coli

KM Value [mM]

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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Storage Stability

Storage Stability Organism
the storage stabilities of the immobilized phosphatase are higher than those of the native one Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
Escherichia coli 4-nitrophenol + phosphate
-
?

Synonyms

Synonyms Comment Organism
alkaline phosphatase
-
Escherichia coli

Temperature Optimum [°C]

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 Range [°C]

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 [°C]

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

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 Range

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 [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 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