Mandair, Ravneet;
Karagoz, Pinar;
Bill, Roslyn M;
(2021)
A Redox-Neutral, Two-Enzyme Cascade for the Production of Malate and Gluconate from Pyruvate and Glucose.
Applied Sciences
, 11
(11)
, Article 4877. 10.3390/app11114877.
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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.
Type: | Article |
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Title: | A Redox-Neutral, Two-Enzyme Cascade for the Production of Malate and Gluconate from Pyruvate and Glucose |
Open access status: | An open access version is available from UCL Discovery |
DOI: | 10.3390/app11114877 |
Publisher version: | https://doi.org/10.3390/app11114877 |
Language: | English |
Additional information: | This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
Keywords: | enzymatic cascade reaction; malate production; malate dehydrogenase; glucose dehydrogenase |
UCL classification: | UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Engineering Science UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Engineering Science > Dept of Biochemical Engineering UCL > Provost and Vice Provost Offices > UCL BEAMS UCL |
URI: | https://discovery.ucl.ac.uk/id/eprint/10149760 |
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