1995
DOI: 10.1080/00032719508001107
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Determination of Urinary Oxalate Using Banana Oxalate Oxidase: Comparison with Immobilized Enzyme

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Cited by 14 publications
(4 citation statements)
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“…A value of 1.9 · 10 À3 mol L À1 for the K M was obtained. Although the apparent constant value obtained is higher than those for OOX in solution [33] (1.1 · 10 À4 mol L À1 ), Michaelis-Menten constant values for OOX in the range from 1.3 · 10 À1 to 1.6 · 10 À4 mol L À1 have been informed in the literature [34][35][36][37][38] for different procedures of immobilization. The increase in K M for OOX may be attributed to the mass transfer limitations of the substrate to access the immobilized enzyme [39] and also to the modification of the quaternary structure of the actives sites of the enzyme [40].…”
Section: Oxalate Biosensor Based On Nihcnfe/ppy Hybridmentioning
confidence: 98%
“…A value of 1.9 · 10 À3 mol L À1 for the K M was obtained. Although the apparent constant value obtained is higher than those for OOX in solution [33] (1.1 · 10 À4 mol L À1 ), Michaelis-Menten constant values for OOX in the range from 1.3 · 10 À1 to 1.6 · 10 À4 mol L À1 have been informed in the literature [34][35][36][37][38] for different procedures of immobilization. The increase in K M for OOX may be attributed to the mass transfer limitations of the substrate to access the immobilized enzyme [39] and also to the modification of the quaternary structure of the actives sites of the enzyme [40].…”
Section: Oxalate Biosensor Based On Nihcnfe/ppy Hybridmentioning
confidence: 98%
“…Oxalate oxidase (EC 1.2.3.4), belongs to the germin family of proteins, expressed predominantly in higher plants, catalyses the oxygen‐dependent oxidation of oxalate to carbon dioxide in a reaction that is coupled with the formation of hydrogen peroxide. Oxalate oxidase activity is found in a wide variety of plants, including barley seedling, roots and leaves, Amaranthus leaves, beet stems and leaves, sorghum leaves and maize, oats, rice and rye (Hurkman et al ., ; Lathika et al ., ). Flammulina velutipes oxalate decarboxylase (FvOXDC) is thought to be the best characterized oxalate decarboxylase from the wood‐rotting fungus reported till date (Chakraborty et al ., ).…”
Section: Introductionmentioning
confidence: 97%
“…To obtain a reliable sample for oxalate assay, a prior centrifugal separation is necessary (Classen and Hesse, 1987;Lathika et al, 1995;Coyle et al, 1989).…”
Section: Introductionmentioning
confidence: 98%