A Redox-Neutral, Two-Enzyme Cascade for the Production of Malate and Gluconate from Pyruvate and Glucose
Source abstract
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.
Source: crossref · Quality: baseline
Research context
OpenAlex topics: Enzyme Catalysis and Immobilization · Enzyme Structure and Function · Microbial Metabolic Engineering and Bioproduction
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
College of Health and Life Sciences, Aston University, Birmingham B4 7ET, UK
Department of Biochemical Engineering, University College London, Gower Street, London WC1E 6BT, UK
Funding
Biotechnology and Biosciences Research Council
References (19)
Show source-provided references
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