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Literature summary for 1.2.3.4 extracted from

  • Bhambi, M.; Pundir, C.S.
    Immobilization of grain-sorghum (Sorghum bicolor, var. CSH-14) leaf oxalate oxidase on to a modified mica chip and its application in the determination of urinary oxalate (2007), Biotechnol. Appl. Biochem., 47, 125-129.
    View publication on PubMed
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General Stability

General Stability Organism
the immobilized enzyme on modified mica chip retains 65.35% of the specific activity of free enzyme Sorghum bicolor

Inhibitors

Inhibitors Comment Organism Structure
ascorbate ascorbate causes 80% inhibition in the activity of immobilized enzyme Sorghum bicolor

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.53
-
 oxalic acid free enzyme Sorghum bicolor
0.7
-
 oxalic acid immobilized enzyme Sorghum bicolor

Organism

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

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, DEAE-Sephacel column chromatography, and Sephadex G-100 gel filtration Sorghum bicolor

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 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
-
 ?

Synonyms

Synonyms Comment Organism
OXO
-
 Sorghum bicolor

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 free enzyme Sorghum bicolor

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 free enzyme Sorghum bicolor
6.5
-
 the immobilized enzyme shows maximum activity at pH 6.5 when incubated at 40°C for 15 min Sorghum bicolor