Enzymatic L-Arginine and L-Lysine Determination Using a Carbonate Ion Selective Membrane Electrode

Tong, S. L.; Rechnitz, G. A.

doi:10.1080/00032717608059075

Cited by 17 publications

(3 citation statements)

References 9 publications

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“…3.5.1.5) detects the ammonia produced from l ‐arginine by the two coupling reactions: arginase degrades l ‐arginine to urea and l ‐ornithine, and urease produces ammonia from urea 7,8 . The l ‐arginine decarboxylase (EC 4.1.1.19) method detects the carbonate ion, which is produced by the decarboxylation of l ‐arginine, by ion selective membrane electrode 9 . The method using l ‐arginine deiminase (EC 3.5.3.6) and argininosuccinate synthetase (EC 6.3.4.5) measures the pyrophosphate produced from l ‐arginine thorough the two‐step reaction.…”

Section: Introductionmentioning

confidence: 99%

“…19) method detects the carbonate ion, which is produced by the decarboxylation of L-arginine, by ion selective membrane electrode. 9 The method using Larginine deiminase (EC 3.5.3.6) and argininosuccinate synthetase (EC 6.3.4.5) measures the pyrophosphate produced from L-arginine thorough the two-step reaction. Pyrophosphate is a byproduct of the argininosuccinate synthesis from L-citrulline by argininosuccinate synthetase, and L-citrulline is converted from L-arginine by Larginine deiminase.…”

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A new l‐arginine oxidase engineered from l‐glutamate oxidase

et al. 2021

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The alternation of substrate specificity expands the application range of enzymes in industrial, medical, and pharmaceutical fields. l‐Glutamate oxidase (LGOX) from Streptomyces sp. X‐119‐6 catalyzes the oxidative deamination of l‐glutamate to produce 2‐ketoglutarate with ammonia and hydrogen peroxide. LGOX shows strict substrate specificity for l‐glutamate. Previous studies on LGOX revealed that Arg305 in its active site recognizes the side chain of l‐glutamate, and replacement of Arg305 by other amino acids drastically changes the substrate specificity of LGOX. Here we demonstrate that the R305E mutant variant of LGOX exhibits strict specificity for l‐arginine. The oxidative deamination activity of LGOX to l‐arginine is higher than that of l‐arginine oxidase form from Pseudomonas sp. TPU 7192. X‐ray crystal structure analysis revealed that the guanidino group of l‐arginine is recognized not only by Glu305 but also Asp433, Trp564, and Glu617, which interact with Arg305 in wild‐type LGOX. Multiple interactions by these residues provide strict specificity and high activity of LGOX R305E toward l‐arginine. LGOX R305E is a thermostable and pH stable enzyme. The amount of hydrogen peroxide, which is a byproduct of oxidative deamination of l‐arginine by LGOX R305E, is proportional to the concentration of l‐arginine in a range from 0 to 100 μM. The linear relationship is maintained around 1 μM of l‐arginine. Thus, LGOX R305E is suitable for the determination of l‐arginine.

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Section: Introductionmentioning

confidence: 99%

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confidence: 99%

A new l‐arginine oxidase engineered from l‐glutamate oxidase

et al. 2021

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“…2- 4 The use of gas-sensing membrane electrodes have led to the development of better enzyme elect r o d e~~-'~ which are free from ionic and protein interferences. However, the application of such enzyme electrodes in rapid and continuous determination of amino acids is limited by the time consumed to reach the steady state of electrode response.…”

Section: Introductionmentioning

confidence: 99%

An enzyme electrode for specific determination of L‐lysine: A real‐time control sensor

Tran

Romette

Thomas

1983

Biotech & Bioengineering

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Lysine decarboxylase (L-lysine carboxylyase, E.C.4.1.1.18) is immobolized on a carbon dioxide gas-sensing electrode, by copolymerization with gelatin using the bifuncitional agent glutaraldehyde. The enzyme electrodes thus prepared are used in a continuous flow system to measure the concentration of L-lysine in a mixture of amino acids. The measuring time for each sample is about 3 min, including response and rinsing times. The electrode response is linear between 0.01-1 g/L and has a high specificity for L-lysine. The enzyme electrode response to lysine at concentrations below 0.5 g/L is stable on repeated use for at least 500 assays.

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Enzyme electrode for specific determination of L‐lysine

Romette

Yang

Kusakabe

et al. 1983

Biotech & Bioengineering

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L-Lysine alpha-oxidase from Trichoderma viride Y244-2 is immobilized in a gelatin support and fixed on a pO(2) sensor. The enzyme electrode obtained is used in a continuous flow system in order to measure the concentration of L-lysine in a fermentor. The sample oxygen-content dependance of the signal is minimized because of the enzyme support properties. The enzyme electrode response is set for lysine concentration from 0.2mM to 4mM. The specificity of lysine is tested with other amino acids. The enzyme membrane for lysine electrode can be used 3000 times or stored six months with good stability.

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Enzymatic L-Arginine and L-Lysine Determination Using a Carbonate Ion Selective Membrane Electrode

Cited by 17 publications

References 9 publications

A new l‐arginine oxidase engineered from l‐glutamate oxidase

A new l‐arginine oxidase engineered from l‐glutamate oxidase

An enzyme electrode for specific determination of L‐lysine: A real‐time control sensor

Enzyme electrode for specific determination of L‐lysine

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