Abstract
A triple mutant of NADP(H)-dependent malate dehydrogenase from thermotolerant Thermococcus kodakarensis has an altered cofactor preference for NAD+, as well as improved malate production compared to wildtype malate dehydrogenase. By combining mutant malate dehydrogenase with glucose dehydrogenase from Sulfolobus solfataricus and NAD+/NADH in a closed reaction environment, gluconate and malate could be produced from pyruvate and glucose. After 3 h, the yield of malate was 15.96 mM. These data demonstrate the feasibility of a closed system capable of cofactor regeneration in the production of platform chemicals.
| Original language | English |
|---|---|
| Article number | 4877 |
| Journal | Applied Sciences |
| Volume | 11 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 26 May 2021 |
Bibliographical note
Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/.
Funding: This research was funded by the Biotechnology and Biological Sciences Research Council (BBSRC) through the Global Challenges Research Fund Project, CAPRI-BIO (BB/P022685/1). R.M. was supported by a BBSRC training grant with Chemoxy Ltd. (BB/M016668/1). The APC was funded by BBSRC.
Keywords
- Enzymatic cascade reaction
- malate production
- malate dehydrogenase
- glucose dehydrogenase
- Malate production
- Glucose dehydrogenase
- Malate dehydrogenase