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Literature summary for 1.2.3.4 extracted from

  • Pundir, C.S.; Chauhan, N.S.; Bhambi, M.
    Activation of polyvinyl chloride sheet surface for covalent immobilization of oxalate oxidase and its evaluation as inert support in urinary oxalate determination (2008), Anal. Biochem., 374, 272-277.
    View publication on PubMed

General Stability

General Stability Organism
the polyvinyl chloride-immobilized enzyme retains 65% of specific activity of free enzyme Sorghum bicolor

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 34% decreased activity at 10 mM Ca2+ Sorghum bicolor

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.27
-
oxalic acid PVC-immobilized enzyme Sorghum bicolor
0.78
-
oxalic acid native enzyme Sorghum bicolor

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ 14% increased activity at 10 mM Cu2+ Sorghum bicolor
Mg2+ 40% increased activity at 10 mM Mg2+ Sorghum bicolor
Mn2+ 40% increased activity at 10 mM Mn2+ Sorghum bicolor
additional information the immobilized oxalate oxidase shows no increase in activity in the presence of 10 mM K+ or Na+ Sorghum bicolor

Organism

Organism UniProt Comment Textmining
Sorghum bicolor
-
line CSH-14
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Sorghum bicolor
-
seedling
-
Sorghum bicolor
-

Storage Stability

Storage Stability Organism
4°C, 0.05 M sodium phosphate buffer (pH 6.5), 100 days, the immobilized oxalate oxidase loses 15% of its initial activity-free oxalate oxidase after 150 uses Sorghum bicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxalic acid + O2 + 2 H+
-
Sorghum bicolor 2 CO2 + H2O2
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
native enzyme or PVC-immobilized enzyme Sorghum bicolor

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
native enzyme Sorghum bicolor
6.5
-
PVC-immobilized enzyme Sorghum bicolor