Arginine-hydrolyzing enzymes for electrochemical biosensors

Gayda, Galina; Stasyuk, Nataliya; Zakalskiy, Andriy; Gonchar, Mykhailo; Katz, Evgeny

doi:10.1016/j.coelec.2022.100941

Cited by 3 publications

(5 citation statements)

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“…The enzymes metabolizing Arg exhibit high selectivity towards their natural substrate, so they are ideal candidates for biorecognition elements in optical and electrochemical biosensors of Arg [ 23 – 26 ]. Arginase I (ARG, EC 3.5.3.1, L-arginine amidino hydrolase) is an enzyme expressed in the human liver and critical to the urea cycle.…”

Section: Introductionmentioning

confidence: 99%

“…To estimate the level of Arg, the electrochemical BSs which detect the ammonium ions produced during the enzymatic digestion of Arg have been suggested and described in detail in the reviews [ 23 – 25 ] and our previous reports [ 33 – 35 ]. Numerous designs of potentiometric and conductometric BSs based on ammonium-selective electrodes have also been reported [ 23 – 25 , 32 , 36 ].…”

Section: Introductionmentioning

confidence: 99%

“…Despite the popularity of potentiometric BSs, they have a number of disadvantages, namely, the dependence of membrane potential on presence of other ions, temperature, ionic strength of the solution, prolonged response time, and short-term operational stability due to the quick destruction of the polymeric membrane [ 25 ]. Amperometric BSs (ABSs) are more promising for ammonia monitoring due to their higher sensitivity and selectivity as well as easy integration into continuous analytic systems [ 23 – 26 ]. Several ABSs for Arg assay have been developed and described [ 23 – 26 , 37 – 39 ].…”

Section: Introductionmentioning

confidence: 99%

“…Amperometric BSs (ABSs) are more promising for ammonia monitoring due to their higher sensitivity and selectivity as well as easy integration into continuous analytic systems [ 23 – 26 ]. Several ABSs for Arg assay have been developed and described [ 23 – 26 , 37 – 39 ]. Some of them are based on the application of Arg-selective hydrolases, in particular, arginase/urease or ADI co-immobilized with conductive polymers in the bioselective layer [ 21 , 26 , 32 – 35 ].…”

Section: Introductionmentioning

confidence: 99%

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Ammonium nanochelators in conjunction with arginine-specific enzymes in amperometric biosensors for arginine assay

Stasyuk,

Gayda,

Nogala

et al. 2023

Microchim Acta

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Amino acid L-arginine (Arg), usually presented in food products and biological liquids, can serve both as a useful indicator of food quality and an important biomarker in medicine. The biosensors based on Arg-selective enzymes are the most promising devices for Arg assay. In this research, three types of amperometric biosensors have been fabricated. They exploit arginine oxidase (ArgO), recombinant arginase I (ARG)/urease, and arginine deiminase (ADI) coupled with the ammonium-chelating redox-active nanoparticles. Cadmium-copper nanoparticles (nCdCu) as the most effective nanochelators were used for the development of ammonium chemosensors and enzyme-coupled Arg biosensors. The fabricated enzyme/nCdCu-containing bioelectrodes show wide linear ranges (up to 200 µM), satisfactory storage stabilities (14 days), and high sensitivities (A⋅M−1⋅m−2) to Arg: 1650, 1700, and 4500 for ADI-, ArgO- and ARG/urease-based sensors, respectively. All biosensors have been exploited to estimate Arg content in commercial juices. The obtained data correlate well with the values obtained by the reference method. A hypothetic scheme for mechanism of action of ammonium nanochelators in electron transfer reaction on the arginine-sensing electrodes has been proposed. Graphical abstract

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Ammonium nanochelators in conjunction with arginine-specific enzymes in amperometric biosensors for arginine assay

Stasyuk,

Gayda,

Nogala

et al. 2023

Microchim Acta

Self Cite

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“…Enzymes are defined as biologically active proteins [ 2 ], but often they are endowed with a non-protein component known as a cofactor which is responsible for catalytic activity. They are biocompatible and biodegradable, and due to their ease of production and substrate specificity, they are widely used in clinical diagnosis [ 3 ] and the environmental industry [ 4 ]. However, all these remarkable characteristics of enzymes and their widespread use in various fields of application are often hampered by their unstable structure, short lifetime, separation problems and high costs in enzymatic recycling [ 5 , 6 ].…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Comparative Studies of Glucose Oxidase Immobilized on Fe3O4 Magnetic Nanoparticles Using Different Coupling Agents

Rusu¹,

Chiriac²,

Niţă³

et al. 2022

Nanomaterials

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Squaric acid (SA) is a compound with potential to crosslink biomacromolecules. Although SA has become over the last years a well-known crosslinking agent as a result of its good biocompatibility, glutaraldehyde (GA), a compound with proven cytotoxicity is still one of the most used crosslinkers to develop nanomaterials. In this regard, the novelty of the present study consists in determining whether it may be possible to substitute GA with a new bifunctional and biocompatible compound, such as SA, in the process of enzyme immobilization on the surface of magnetic nanoparticles (MNPs). Thus, a direct comparison between SA- and GA-functionalized magnetic nanoparticles was realized in terms of physico-chemical properties and ability to immobilize catalytic enzymes. The optimal conditions of the synthesis of the two types of GOx-immobilized MNPs were described, thus emphasizing the difference between the two reagents. Scanning Electron Microscopy and Dynamic Light Scattering were used for size, shape and colloidal stability characterization of the pristine MNPs and of those coupled with GOx. Binding of GOx to MNPs by using GA or SA was confirmed by FT-IR spectroscopy. The stability of the immobilized and free enzyme was investigated by measuring the enzymatic activity. The study confirmed that the resulting activity of the immobilized enzyme and the optimization of enzyme immobilization depended on the type of reagent used and duration of the process. The catalytic performance of immobilized enzyme was tested, revealing that the long-term colloidal stability of SA-functionalized MNPs was superior to those prepared with GA. In conclusion, the SA-functionalized bioconjugates have a better potential as compared to the GA-modified nanosystems to be regarded as catalytic nanodevices for biomedical purposes such as biosensors.

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Adaptation of Conductometric Monoenzyme Biosensor for Rapid Quantitative Analysis of L-arginine in Dietary Supplements

Saiapina,

Berketa,

Sverstiuk

et al. 2024

Sensors

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The present study reports on the development, adaptation, and optimization of a novel monoenzyme conductometric biosensor based on a recombinant arginine deiminase (ADI) for the determination of arginine in dietary supplements with a high accuracy of results. Aiming for the highly sensitive determination of arginine in real samples, we studied the effect of parameters of the working buffer solution (its pH, buffer capacity, ionic strength, temperature, and protein concentration) on the sensitivity of the biosensor to arginine. Thus, it was determined that the optimal buffer is a 5 mM phosphate buffer solution with pH 6.2, and the optimal temperature is 39.5 °C. The linear functioning range is 2.5–750 µM of L-arginine with a minimal limit of detection of 2 µM. The concentration of arginine in food additive samples was determined using the developed ADI-based biosensor. Based on the obtained results, the most effective method of biosensor analysis using the method of standard additions was chosen. It was also checked how the reproducibility of the biosensor changes during the analysis of pharmaceutical samples. The results of the determination of arginine in real samples using a conductometric biosensor based on ADI clearly correlated with the data obtained using the method of ion-exchange chromatography and enzymatic spectrophotometric analysis. We concluded that the developed biosensor would be effective for the accurate and selective determination of arginine in dietary supplements intended for the prevention and/or elimination of arginine deficiency.

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Arginine-hydrolyzing enzymes for electrochemical biosensors

Cited by 3 publications

References 52 publications

Ammonium nanochelators in conjunction with arginine-specific enzymes in amperometric biosensors for arginine assay

Ammonium nanochelators in conjunction with arginine-specific enzymes in amperometric biosensors for arginine assay

Synthesis and Comparative Studies of Glucose Oxidase Immobilized on Fe3O4 Magnetic Nanoparticles Using Different Coupling Agents

Adaptation of Conductometric Monoenzyme Biosensor for Rapid Quantitative Analysis of L-arginine in Dietary Supplements

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