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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제22권 제10호
- 발행연도
- 2012.1
- 수록면
- 1,406 - 1,411 (6page)
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5,5'-Dithiobis(2-nitrobenzoic acid) (DTNB) was selected as an electron transfer mediator and was covalently immobilized onto high porosity carbon cloth to employ as a working electrode in an electrochemical NAD+-regeneration process,which was coupled to an enzymatic reaction. The voltammetric behavior of DTNB attached to carbon cloth resembled that of DTNB in buffered aqueous solution,and the electrocatalytic anodic current grew continuously upon addition of NADH at different concentrations,indicating that DTNB is immobilized to carbon cloth effectively and the immobilized DTNB is active as a soluble one. The bioelectrocatalytic NAD+ regeneration was coupled to the conversion of L-glutamate into α-ketoglutarate by L-glutamate dehydrogenase within the same microreactor.
The conversion at 3 mM monosodium glutamate was very rapid, up to 12 h, to result in 90%, and then slow up to 24 h, showing 94%, followed by slight decrease. Low conversion was shown when substrate concentration exceeding 4 mM was tested, suggesting that L-glutamate dehydrogenase is inhibited by α-ketoglutarate. However,our electrochemical NAD+ regeneration procedure looks advantageous over the enzymatic procedure using NADH oxidase, from the viewpoint of reaction time to completion.
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참고문헌 (21)
참고문헌 신청
Anne, A. / 1999 / Can the combination of electrochemical regeneration of NAD+, selectivity of L-α-amino-acid dehydrogenase, and reductive amination of α-keto-acid be applie
Antiochia, R. / 1999 / Electrocatalytic oxidation of dihydronicotinamide adenine dinucleotide with ferrocene carboxylic acid by diaphorase from Clostridium kluyveri. Remarks
Basso, L. A. / 1993 / The mechanism of substrate and coenzyme binding to clostridial glutamate dehydrogenase during oxidative deamination / Eur. J. Biochem 213 : 935 ~ 945
Brown, A. / 1978 / Effect of ammonia on the glutamate dehydrogenase catalyzed oxidative deamination of L-glutamate: Production of an ammonia-containing intermediate in the “
Brown, A. / 1979 / Effect of ammonia on the glutamate dehydrogenase catalyzed oxidative deamination of L-glutamate. The steady state / Biochemistry 18 : 5924 ~ 5928
Antiochia, R. / 1999 / Electrocatalytic oxidation of dihydronicotinamide adenine dinucleotide with ferrocene carboxylic acid by diaphorase from Clostridium kluyveri. Remarks
Basso, L. A. / 1993 / The mechanism of substrate and coenzyme binding to clostridial glutamate dehydrogenase during oxidative deamination / Eur. J. Biochem 213 : 935 ~ 945
Brown, A. / 1978 / Effect of ammonia on the glutamate dehydrogenase catalyzed oxidative deamination of L-glutamate: Production of an ammonia-containing intermediate in the “
Brown, A. / 1979 / Effect of ammonia on the glutamate dehydrogenase catalyzed oxidative deamination of L-glutamate. The steady state / Biochemistry 18 : 5924 ~ 5928
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