• Title/Summary/Keyword: Ketoacids

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FORMATION OF KETOACIDS AND AOC DURING OZONATION IN DRINKING WATER

  • Lee, Kyung-Hyuk
    • Environmental Engineering Research
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    • v.11 no.6
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    • pp.293-302
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    • 2006
  • The reaction of ozone with NOM (Natural Organic Matter) can occur by two different pathways: that involving molecular ozone and by way of reactions with hydroxyl radicals which are produced from the decomposition of molecular ozone. As such, the formation of ketoacids and Assimilable Organic Carbon (AOC) can be controlled by controlling the pathway by which ozone reacts with NOM. The ratios of $[OH{\cdot}]/[O_3]$ ($R_{CT}$ values) were determined under the various ozonation conditions. The $R_{CT}$ values increased with increasing initial ozone concentration. The $R_{CT}$ values (ranges from 10 to $35^{\circ}C$) increased linearly as temperature increased (within the range from 10 to $35^{\circ}C$). However, $R_{CT}$ was independent of hydraulic retention time (HRT). Operational conditions were found to affect the formation of AOC. The conditions where the molecular ozone reaction predominated resulted in an increase in the formation of AOC.

Derivatization of a-ketoacid for the Analysis of Aminotransferase Reaction Using Mass Spectrometry (질량 분석기를 이용한 트렌스아미나제 반응 분석을 위한 케토산 화학 수식법 개발)

  • Lee Chang Soo;Kim Yun Gon;Kim Eun Mi;Kim Byung Gee
    • KSBB Journal
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    • v.19 no.5
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    • pp.394-398
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    • 2004
  • A derivatization method in mass spectrometry for small molecular analysis was developed to solve the problems of volatility of many analytes, difficult ionization of analytes, and undiscriminating isobaric analytes. This derivatization method, oximation of $\alpha$-ketoacid, in the transaminase reaction leads to change of mass difference between amine reactants and ketoacid products. In addition, regardless of the kinds of ketoacid, the linear relationship between the peak intensity and its concentration (from 1 mM to 10 mM) shows that quantitative analysis of the conversion of the reaction can be executed by the analysis of peak intensity of the corresponding oximated ketoacids. Furthermore, this method can be used for identifying transaminase as well as determining its substrate specificity