A redox-neutral, two-enzyme cascade for the production of malate and gluconate from pyruvate and glucose

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.

Publication DOI: https://doi.org/10.3390/app11114877
Divisions: College of Health & Life Sciences > School of Biosciences
College of Health & Life Sciences > School of Biosciences > Cellular and Molecular Biomedicine
College of Health & Life Sciences
Additional Information: 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.
Uncontrolled Keywords: Enzymatic cascade reaction,malate production,malate dehydrogenase,glucose dehydrogenase,Malate production,Glucose dehydrogenase,Malate dehydrogenase,General Engineering,Instrumentation,General Materials Science,Fluid Flow and Transfer Processes,Process Chemistry and Technology,Computer Science Applications
Publication ISSN: 2076-3417
Last Modified: 30 Sep 2024 12:44
Date Deposited: 02 Jun 2021 13:32
Full Text Link:
Related URLs: https://www.mdp ... 3417/11/11/4877 (Publisher URL)
http://www.scop ... tnerID=8YFLogxK (Scopus URL)
PURE Output Type: Article
Published Date: 2021-05-26
Accepted Date: 2021-05-24
Authors: Mandair, Ravneet
Karagoz, Pinar
Bill, Roslyn M. (ORCID Profile 0000-0003-1331-0852)

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