
doi: 10.3390/app11114877
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.
glucose dehydrogenase, Technology, QH301-705.5, T, Physics, QC1-999, malate dehydrogenase, enzymatic cascade reaction, Engineering (General). Civil engineering (General), Chemistry, TA1-2040, Biology (General), malate production, QD1-999
glucose dehydrogenase, Technology, QH301-705.5, T, Physics, QC1-999, malate dehydrogenase, enzymatic cascade reaction, Engineering (General). Civil engineering (General), Chemistry, TA1-2040, Biology (General), malate production, QD1-999
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