A novel urinary oxalate determination method via a catalase model compound with oxalate oxidase

Zuo, Guanke; Jiang, Xiaoxiang; Liu, Hui; Zhang, Jingyan

doi:10.1039/b9ay00247b

Cited by 15 publications

(7 citation statements)

References 29 publications

(31 reference statements)

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“…While the reduction extent of CRGO increased, about 90% activity of the immobilized OxOx was maintained after ten cycles (Figure 7b and c). The immobilization of OxOx has been extensively explored for its critical application in clinical oxalate determination since 1980 19, 20. Many solid materials have been employed for this purpose, and the best enzyme loading so far discovered is 182 mg g −1 on alkylamine glass beads; however, the activity of the immobilized OxOx was only 5.17% that of the free OxOx 11c.…”

Section: Resultsmentioning

confidence: 99%

Assembly of Graphene Oxide–Enzyme Conjugates through Hydrophobic Interaction

Zhang

Huang

et al. 2011

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Biochemical and biomedical applications of graphene oxide (GO) critically rely on the interaction of biomolecules with it. It has been previously reported that the biological activity of the GO-enzyme conjugate decreases due to electrostatic interaction between the enzymes and GO. Herein, the immobilization of horseradish peroxidase (HRP) and oxalate oxidase (OxOx) on chemically reduced graphene oxide (CRGO) are reported. The enzymes can be adsorbed onto CRGO directly with a tenfold higher enzyme loading than that on GO, and maximum enzyme loadings reach 1.3 and 12 mg mg(-1) for HRP and OxOx, respectively. Significantly, the more CRGO is reduced, the higher the enzyme loading. The CRGO-HRP conjugates also exhibit higher enzyme activity and stability than GO-HRP. Excellent properties of the CRGO-enzyme conjugates are attributed to hydrophobic interaction between the enzymes and the CRGO. The hydrophobic interaction mode of the CRGO-enzyme conjugates can be applied to other hydrophobic proteins, and thus could dramatically improve the performance of immobilized proteins. The results indicate that CRGO is a potential substrate for efficient enzyme immobilization, and is an ideal candidate as a macromolecule carrier and biosensor.

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Section: Resultsmentioning

confidence: 99%

Assembly of Graphene Oxide–Enzyme Conjugates through Hydrophobic Interaction

Zhang

Huang

et al. 2011

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“… 4 Methods for efficient and economical quantitation of oxalate in aqueous samples are needed. Published enzyme-based methods have become commercially available 5 , 6 but are cost-prohibitive and potentially susceptible to interference from sample components. For example, urine must be decolorized before analysis.…”

Section: Introductionmentioning

confidence: 99%

A Copper(II) Macrocycle Complex for Sensing Biologically Relevant Organic Anions in a Competitive Fluorescence Assay: Oxalate Sensor or Urate Sensor?

et al. 2020

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Fluorescence sensing of oxalate has garnered some attention in the past two decades as a result of this anion’s prominence and impact on society. Previous work on oxalate sensors and other divalent anion sensors has led to the conclusion that the sensors are selective for the anion under investigation. However, sensor selectivity is often determined by testing against a relatively small array of “guest” molecules or analytes and studies often exclude potentially interfering compounds. For example, studies on oxalate sensors have excluded compounds such as citrate and urate, which are anions in the biological matrices where oxalate is measured ( e.g ., urine, blood, and bacterial lysate). In the present study, we reassessed the selectivity of a dinuclear copper(II) macrocycle (Cu 2 L) in an eosin Y displacement assay using biologically relevant anions. Although previously reported as selective for oxalate, we found greater indicator displacement (fluorescence response) for urate and oxaloacetate and a significant response to citrate. These anions are larger than oxalate and do not appear to fit into the putative binding pocket of Cu 2 L. Consistent with previous reports, Cu 2 L did not release eosin Y in the presence of several other dicarboxylates, including adipate, glutarate, malate (except at 10 mM), fumarate, succinate, or malonate (except at 10 mM), and the monocarboxylate acetate. This was demonstrated by the failure of the anions to reverse eosin Y quenching by Cu 2 L. We also assessed, for the first time, other monocarboxylates, including butyrate, pyruvate, lactate, propionate, and formate. None of these anions were able to displace eosin Y, indicating no interaction with Cu 2 L that interfered with the eosin Y binding site. Single-crystal X-ray crystallography revealed that nonselective binding of the anions is likely partly caused by readily accessible copper(II) ions on the external surface of Cu 2 L. In addition, π–π stacking of urate with the aromatic groups of Cu 2 L cannot be ruled out as a contributor to binding. We conclude that Cu 2 L is not suitable for oxalate sensing in a biological matrix unless interfering compounds are selectively removed or masked.

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“…Urinary oxalate determination based on immobilization of catalase and oxalate oxidase has been described [189]. Urinary oxalate is first decomposed by oxalate oxidase into carbon dioxide and hydrogen peroxide.…”

Section: +mentioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

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135

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Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

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A novel urinary oxalate determination method via a catalase model compound with oxalate oxidase

Cited by 15 publications

References 29 publications

Assembly of Graphene Oxide–Enzyme Conjugates through Hydrophobic Interaction

Assembly of Graphene Oxide–Enzyme Conjugates through Hydrophobic Interaction

A Copper(II) Macrocycle Complex for Sensing Biologically Relevant Organic Anions in a Competitive Fluorescence Assay: Oxalate Sensor or Urate Sensor?

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

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