Purification and properties of an oxalate oxidase from leaves of grain sorghum hybrid CSH-5

Satyapal,; Pundir, C.S.

doi:10.1016/0167-4838(93)90188-w

Cited by 61 publications

(28 citation statements)

References 23 publications

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“…There is a slight increase in the activity of OxO with increase in concentration of Cu 2þ up to 1.5 mg/mL concentration after which the activity remains constant. The increase in activity of enzyme in the presence of Cu 2þ could be due to its facilitating effect in the binding of the substrate to the active site of enzyme [4]. These observations indicate that CNPs at 1.0 mg/mL concentration was able to cause maximum increase (30%) but minimum increase (10%) at 4.0 mg/mL, probably due to more efficient electron transfer and from the redox centre of enzyme [8].…”

Section: Analytic Use Of Cnps-oxomentioning

confidence: 56%

“…Assay of native OxO was carried out in a 15 mL test tube wrapped with black paper as described in [4]. The reaction mixture containing 1.8 mL 0.05 M sodium succinate buffer, pH 5.0, 0.1 mL CuSO 4 solution (10 À2 M) and 0.1 mL crude enzyme (0.1 mg/mL) was preincubated at 37 C for 2 min.…”

Section: Assay Of Oxomentioning

confidence: 99%

“…The homogenate was centrifuged at l5,000 Â g for 30 min at 4 C and the supernatant was collected and tested for OxO activity and proteins. The crude enzyme (15,000 Â g supernatant) was purified at 4-8 C by 0-80% (NH 4 ) 2 SO 4 fractionation, gel filtration on Sephadex G-200 and ion exchange chromatography on DEAE-Sephacel as described in [4]. The ultrafiltration of purified enzyme was carried out by Amicon concentrator at 4 C. The activity and protein content of purified enzyme were measured [4,7].…”

Section: Purification Of Oxomentioning

confidence: 99%

“…Ten-day-old seedlings of grain sorghum were raised in the laboratory as described in [4] and their leaves were collected and stored immediately at À20 C until use. The frozen leaves were homogenised with cold distilled water in 1 : 3 ratio (w/v) in a chilled mortar and pestle.…”

Section: Purification Of Oxomentioning

confidence: 99%

“…MNPs also enhance stability of enzyme [1,2,3]. Sorghum oxalate oxidase (OxO), a metalloprotein requires Cu 2þ for its activity [4]. The enzyme is widely used for determination of plasma and urinary oxalate which is essential for the diagnosis and medical management of urinary calculi and various intestinal diseases [5].…”

Section: Introductionmentioning

confidence: 99%

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Influence of copper nanoparticles on copper requiring enzyme

Chauhan

Hooda

Pundir

2012

Journal of Experimental Nanoscience

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This study describes the influence of copper nanoparticles (CNPs) on activity and kinetic properties of a Cu 2þ requiring sorghum oxalate oxidase (OxO). CNPs were synthesised by citrate-induced reduction of CuCl 2 and their size (range 13-58 nm) was determined by transmission electron microscopy. The CNPs were characterised by scanning electron microscopy and X-ray diffraction studies. These CNPs enhanced OxO activity by 30%. Thermal and storage stability were increased, while Km value for oxalate decreased in the presence of CNPs. CNPs protected OxO against chelation by diethyldithiocarbamate, a Cu 2þ specific chelator. The analytic use of OxO in the presence of CNP for determination of oxalate in food stuff is demonstrated.

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Section: Analytic Use Of Cnps-oxomentioning

confidence: 56%

Section: Assay Of Oxomentioning

confidence: 99%

Section: Purification Of Oxomentioning

confidence: 99%

Section: Purification Of Oxomentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Influence of copper nanoparticles on copper requiring enzyme

Chauhan

Hooda

Pundir

2012

Journal of Experimental Nanoscience

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Altered physicochemical characteristics of polyethylene glycol linked beet stem oxalate oxidase

Varalakshmi

Lathika

Raghavan

et al. 1995

Biotech & Bioengineering

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Oxalate oxidase (EC 1.2.3.4), obtained from the beet stem, was covalently linked to polyethylene glycol (PEG). Compared with native enzyme, the modified oxalate oxidase exhibited decreased electrophoretic mobility, increased storage stability, higher thermal stability, and resistance to heavy metal inactivation and proteolytic digestion. The chemical modification of oxalate oxidase with PEG also brought about a marked shift in its optimal pH, from pH 4.5 to 6.5, without altering its Michaelis constant (K(m)) significantly. These acquired properties of the immobilized oxalate oxidase render it suitable for possible applications in clinical, nutritional, and medical fields. (c) 1995 John Wiley & Sons, Inc.

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Effects of ionic substances in bleaching filtrates and of lignosulfonates on the activity of oxalate oxidase from barley

Winestrand

Larsson

Cassland

et al. 2011

Engineering in Life Sciences

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The effects of ionic substances in seven industrial filtrates from kraft pulping, mechanical pulping, and sulfite pulping on the activity of oxalate oxidase from barley were investigated by pre‐treatment of the filtrates with ion‐exchange resins prior to enzymatic degradation of the oxalic acid in the filtrates. The pre‐treatment resulted in increased oxalic acid degradation rates in all filtrates, except for one that was obtained from sulfite pulping. The possibility that lignosulfonates, which were present in the filtrate from sulfite pulping, could affect oxalate oxidase was investigated in a separate set of experiments involving four different preparations of lignosulfonates. At a lignosulfonate concentration of 50 mg/mL and a pH of 3.8, only 2–16% of the activity of oxalate oxidase remained. The results show the effects of anionic and cationic substances in bleaching filtrates on oxalate oxidase and indicate that there is an interaction between the enzyme, which has a positive net charge at pH 3.8, and the polymeric anionic lignosulfonates.

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Purification and properties of an oxalate oxidase from leaves of grain sorghum hybrid CSH-5

Cited by 61 publications

References 23 publications

Influence of copper nanoparticles on copper requiring enzyme

Influence of copper nanoparticles on copper requiring enzyme

Altered physicochemical characteristics of polyethylene glycol linked beet stem oxalate oxidase

Effects of ionic substances in bleaching filtrates and of lignosulfonates on the activity of oxalate oxidase from barley

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