An enzymatic process to alpha-ketoglutarate from L-glutamate: the coupled system L-glutamate dehydrogenase/NADH oxidase
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/264191
- author
- Ödman, Peter LU ; Wellborn, WB and Bommarius, AS
- organization
- publishing date
- 2004
- 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
- 2016-04-01 16:45:51
- date last changed
- 2023-09-19 00:36:31
@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}},
doi = {{10.1016/j.tetasy.2004.07.055}},
volume = {{15}},
year = {{2004}},
}