Electroanalysis of D-Amino Acid Oxidase and Its Interaction with Hydrogen Peroxide

Zhou, Nandi; Shao, Zhenyu; Huang, Yongmei; Zhu, Tongyang; Li, Genxi

doi:10.1080/00032710802119376

Cited by 2 publications

(2 citation statements)

References 22 publications

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“…The effect of pH on the color development in ninhydrin method was previously studied [13] for a variety of amino acid concentrations and in a restricted pH range (5.3-8.05), while in the present study was specifically analyzed for amino acid lysine and in a large pH range (2)(3)(4)(5)(6)(7)(8)(9)(10)(11). Apart from this, the ratio of Lys to Nin was also investigated and identified as the most important parameter affecting the reaction.…”

Section: Introductionmentioning

confidence: 89%

“…There is a growing demand for amino acids as value-added substances since they have many potential applications in the food, clinical, pharmaceutical and cosmetic industries, among others [1][2][3][4][5][6][7]. Amino acids have also an essential role in regulating neural activities in vivo [7] and have a great importance in all basic biological processes in the cell [8]. They are also used in the synthesis of certain biomaterials such as silk fibroin-magnetite for wounds healing [9].…”

Section: Introductionmentioning

confidence: 99%

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A New Approach on the Amino Acid Lysine Quantification by UV-Visible Spectrophotometry

Bouzid¹,

Filho²,

Marques³

et al. 2020

Rev. Chim.

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The methodology of the amino acid lysine (Lys) analysis using ninhydrin (Nin) reagent by spectrophotometric method was in-depth studied and improved. The optimization of time, Lys to Nin volume ratio and temperature were explicitly investigated. A specific wavelength of 479 nm was set according to the peak of the absorbance spectrum. The reaction time between Lys and Nin, in aqueous solution, occurs during 50 min. The Lys/Nin ratio 1.67 appeared most effective for this reaction. Moreover, the absorbance increased with temperature until a stable value was achieved nearly at 85�C. It was also found that the reaction is more efficient at initial pH 6 corresponding to formation of high amount of coloured product. Furthermore, the pH of post-reaction mixture was around 4 for different concentrations of lysine and initial pH range 3�10. For lysine solution contaminated with potassium (a representative interfering species) and after variation of the reaction conditions, the maximum wavelength (479 nm) was not affected. Mastering the use of these parameters leads to a good usage of this analytical technique which is simple, fast, accurate, less expensive and especially less harmful towards the environment and human health.

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Section: Introductionmentioning

confidence: 89%

Section: Introductionmentioning

confidence: 99%

A New Approach on the Amino Acid Lysine Quantification by UV-Visible Spectrophotometry

Bouzid¹,

Filho²,

Marques³

et al. 2020

Rev. Chim.

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Spectrophotometric assay of d-isoleucine using an artificially created d-amino acid dehydrogenase

et al. 2014

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D-isoleucine (D-Ile) can be assayed using chiral chromatography but the availability of that method is limited by the necessity for special expertise and expensive equipment. We therefore developed a simple and specific colorimetric assay system for D-Ile determination using an artificially created NADP(+)-dependent D-amino acid dehydrogenase (DAADH). The system consists of two reaction steps: the first is the quantitative conversion of D-Ile to (3R)-2-oxo-3-methyl valerate by DAADH in which NADP(+) is converted to NADPH, while the second is chemical conversion of NADPH to reduced water-soluble Tetrazolium-3 via a redox mediator. D-Ile was determined from 1 to 50 µM, and the assay was unaffected by the presence of any of three other isomers (100 µM), alcohol and organic acids.

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Electroanalysis of D-Amino Acid Oxidase and Its Interaction with Hydrogen Peroxide

Cited by 2 publications

References 22 publications

A New Approach on the Amino Acid Lysine Quantification by UV-Visible Spectrophotometry

A New Approach on the Amino Acid Lysine Quantification by UV-Visible Spectrophotometry

Spectrophotometric assay of d-isoleucine using an artificially created d-amino acid dehydrogenase

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