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An enzymatic process to alpha-ketoglutarate from L-glutamate: the coupled system L-glutamate dehydrogenase/NADH oxidase

Ödman, Peter LU ; Wellborn, WB and Bommarius, AS (2004) In Tetrahedron: Asymmetry 15(18). p.2933-2937
Abstract
alpha-Ketoglutarate, employed to treat mild chronic renal insufficiency, was obtained through enzymatic oxidation of monosodium glutamate (MSG) catalyzed by L-glutamate dehydrogenase (L-gluDH) coupled with NADH oxidase for the regeneration of NADH back to NAD(+). The irreversible reduction of molecular oxygen to water by NADH oxidase is demonstrated to drive oxidation of MSG to alpha-ketoglutarate to completion. L-gluDH was found to be inhibited by all three oxidative deamination products, alpha-ketoglutarate, NADH, and ammonia. As the pH in the current system was balanced by sodium, not ammonia, and NADH was recycled to NAD(+), inhibition of L-gluDH by alpha-ketoglutarate is believed to present the biggest challenge to an efficient... (More)
alpha-Ketoglutarate, employed to treat mild chronic renal insufficiency, was obtained through enzymatic oxidation of monosodium glutamate (MSG) catalyzed by L-glutamate dehydrogenase (L-gluDH) coupled with NADH oxidase for the regeneration of NADH back to NAD(+). The irreversible reduction of molecular oxygen to water by NADH oxidase is demonstrated to drive oxidation of MSG to alpha-ketoglutarate to completion. L-gluDH was found to be inhibited by all three oxidative deamination products, alpha-ketoglutarate, NADH, and ammonia. As the pH in the current system was balanced by sodium, not ammonia, and NADH was recycled to NAD(+), inhibition of L-gluDH by alpha-ketoglutarate is believed to present the biggest challenge to an efficient process. In a batch experiment, we achieved a volumetric productivity of 1 g/(L(.)d). (C) 2004 Elsevier Ltd. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Tetrahedron: Asymmetry
volume
15
issue
18
pages
2933 - 2937
publisher
Elsevier
external identifiers
  • wos:000224333100036
  • scopus:4644257598
ISSN
0957-4166
DOI
10.1016/j.tetasy.2004.07.055
language
English
LU publication?
yes
id
d3287bda-3b8b-4d8e-b168-e8229dfa6447 (old id 264191)
date added to LUP
2007-10-29 10:20:45
date last changed
2017-10-01 04:48:50
@article{d3287bda-3b8b-4d8e-b168-e8229dfa6447,
  abstract     = {alpha-Ketoglutarate, employed to treat mild chronic renal insufficiency, was obtained through enzymatic oxidation of monosodium glutamate (MSG) catalyzed by L-glutamate dehydrogenase (L-gluDH) coupled with NADH oxidase for the regeneration of NADH back to NAD(+). The irreversible reduction of molecular oxygen to water by NADH oxidase is demonstrated to drive oxidation of MSG to alpha-ketoglutarate to completion. L-gluDH was found to be inhibited by all three oxidative deamination products, alpha-ketoglutarate, NADH, and ammonia. As the pH in the current system was balanced by sodium, not ammonia, and NADH was recycled to NAD(+), inhibition of L-gluDH by alpha-ketoglutarate is believed to present the biggest challenge to an efficient process. In a batch experiment, we achieved a volumetric productivity of 1 g/(L(.)d). (C) 2004 Elsevier Ltd. All rights reserved.},
  author       = {Ödman, Peter and Wellborn, WB and Bommarius, AS},
  issn         = {0957-4166},
  language     = {eng},
  number       = {18},
  pages        = {2933--2937},
  publisher    = {Elsevier},
  series       = {Tetrahedron: Asymmetry},
  title        = {An enzymatic process to alpha-ketoglutarate from L-glutamate: the coupled system L-glutamate dehydrogenase/NADH oxidase},
  url          = {http://dx.doi.org/10.1016/j.tetasy.2004.07.055},
  volume       = {15},
  year         = {2004},
}