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Enhanced Enzymatic Transformation of 1-Naphthol in the Presence of Catechol by Peroxidase
Islam, A.K.M. Mydul,Lee, Sung-Eun,Kim, Jang-Eok The Korean Society for Applied Biological Chemistr 2014 Applied Biological Chemistry (Appl Biol Chem) Vol.57 No.2
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 0.1M sodium phosphate buffer (pH 7.0), and 0.3 mM $H_2O_2$ 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.
Enhanced Enzymatic Transformation of 1-Naphthol in the Presence of Catechol by Peroxidase
A. K. M. Mydul Islam,이성은,김장억 한국응용생명화학회 2014 Applied Biological Chemistry (Appl Biol Chem) Vol.57 No.2
Effect of catechol on 1-naphthol transformation byhorse radish peroxidase (HRP) was examined. The impact ofcatechol to 1-naphthol ratio, enzyme activity, pH, and reactiontime in solution were studied. The results obtained indicated that,in the presence of catechol, 1-naphthol transformation byperoxidase shows enhancement greater than that in an equivalentcatechol free system. Only 27% of 1-naphthol (0.3 mM) was ableto transform when catechol was absent in solution, but reached79% in its presence (3.0 mM) in 0.1M sodium phosphate buffer(pH 7.0), and 0.3 mM H2O2 by peroxidase (0.5 unit/mL) after 3 h. The 1-naphthol transformation rate was accelerated by increase ofpH or HRP concentration. High-performance liquid chromatographyanalysis was performed to characterize transformation productsbased on their relative polarities, and molecular weights of productswere identified by mass spectrometry. The transformation productswere 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, tothe best of our knowledge, was used for the first time to elucidatethe product structure at m/z 191. The study shows that 1-naphtholis transformed rapidly by peroxidase when catechol is present,which could be useful information for improving the efficienciesof decontamination techniques.