Radiolysis of 1-naphthol in aqueous solutions

Ngo, Thang Manh; Hoang, Nam Minh; Tran, Tram T. M.

doi:10.1007/s10967-010-0652-z

Cited by 6 publications

(2 citation statements)

References 22 publications

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“…Characterization of the transformation products by HPLC. 1-Naphthol transformation in aqueous solution was analyzed by HPLC at 212 nm, as reported by Ngo et al (2010). The time dependent transformation of 1-naphthol at 3 different reaction times is shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Enhanced enzymatic transformation of 1-naphthol in the presence of catechol by peroxidase

Islam

Lee

Kim

2014

J Korean Soc Appl Biol Chem

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Effect of catechol on 1-naphthol transformation by horse radish peroxidase (HRP) was examined. The impact of catechol to 1-naphthol ratio, enzyme activity, pH, and reaction time in solution were studied. The results obtained indicated that, in the presence of catechol, 1-naphthol transformation by peroxidase shows enhancement greater than that in an equivalent catechol free system. Only 27% of 1-naphthol (0.3 mM) was able to transform when catechol was absent in solution, but reached 79% in its presence (3.0 mM) in 0.1 M sodium phosphate buffer (pH 7.0), and 0.3 mM H 2 O 2 by peroxidase (0.5 unit/mL) after 3 h. The 1-naphthol transformation rate was accelerated by increase of pH or HRP concentration. High-performance liquid chromatography analysis was performed to characterize transformation products based on their relative polarities, and molecular weights of products were identified by mass spectrometry. The transformation products were found to be (hydroxy) naphthoquinones, 1-naphthol: hydroxy-naphthoquinone, and 1-naphthol oligomers (dimer, trimer, tetramer) with the molecular weights (m/z) ranging 100-600. Liquid chromatography-tandem mass spectrometry technique, to the best of our knowledge, was used for the first time to elucidate the product structure at m/z 191. The study shows that 1-naphthol is transformed rapidly by peroxidase when catechol is present, which could be useful information for improving the efficiencies of decontamination techniques.

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Section: Resultsmentioning

confidence: 99%

Enhanced enzymatic transformation of 1-naphthol in the presence of catechol by peroxidase

Islam

Lee

Kim

2014

J Korean Soc Appl Biol Chem

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“…Many articles have been published on removal of naphthols by chemical procedures such as adsorption on polymeric materials,3–5 biochar,6 bentonite,7 radiolysis,8 photolysis,9–11 and biodegradation 12. However, these conventional procedures suffer from high cost, low efficiency, formation or remaining of hazardous by‐products, and applicability to a limit concentration range.…”

Section: Introductionmentioning

confidence: 99%

Use of chitosan for removal of naphthols through tyrosinase‐catalyzed quinone oxidation

Kimura

Kashiwada

Matsuda

et al. 2012

J of Applied Polymer Sci

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In this study, the combined use of chitosan and mushroom tyrosinase was applied to remove 1‐naphthol and 2‐naphthol from aqueous solutions. In particular, the process parameters, such as the pH value, temperature, and enzyme dose, were discussed for tyrosinase‐catalyzed quinone oxidation of 1‐naphthol. The optimum conditions of enzymatic quinone oxidation of 1‐naphthol were determined to be pH 8.0 and 40°C. Under the optimum conditions, quinone oxidation of 1‐naphthol increased with an increase in the enzyme dose. Quinone derivatives enzymatically generated were chemisorbed on chitosan bead sand. The initial velocity of enzymatic quinone oxidation increased with an increase in the amount of added chitosan beads, since unfavorable interactions between quinone derivatives and tyrosinase in the solutions were restrained by quinone adsorption. 1‐Naphthol was completely removed for 8 h by quinone adsorption on chitosan beads (0.10 cm3/cm3) at 20 U/cm3. The removal time was shortened by increasing the enzyme dose or the amount of added chitosan beads. 2‐Naphthol was also completely removed by increasing the enzyme concentration and reaction time, since enzymatic quinone oxidation of 2‐naphthol was much slower than that of 1‐naphthol. The above results reveal that the procedure constructed in this study was an effective technique to remove naphthols. © 2012 Wiley Periodicals, Inc. J Appl Polym Sci, 2012

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Concerted effects of substituents in the reaction of OH with 2-, 3-, and 4-hydroxybiphenyls

Albarrán

Mendoza

2023

Chemical Physics

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Radiolysis of 1-naphthol in aqueous solutions

Cited by 6 publications

References 22 publications

Enhanced enzymatic transformation of 1-naphthol in the presence of catechol by peroxidase

Enhanced enzymatic transformation of 1-naphthol in the presence of catechol by peroxidase

Use of chitosan for removal of naphthols through tyrosinase‐catalyzed quinone oxidation

Concerted effects of substituents in the reaction of OH with 2-, 3-, and 4-hydroxybiphenyls

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