Abstract
Lactobacillus brevis alcohol dehydrogenase (Lb-ADH) catalyzes reduction of prochiral carbonyl compounds to chiral alcohol and meanwhile consumes its cofactor NADH into NAD+, while the cofactor regeneration can be catalyzed by Candida boidinii formate dehydrogenase (Cb-FDH). This work presents three different Escherichia coli whole-cell biocatalyst systems expressing recombinant ADH/FDH, FDH-LIN1-ADH and FDH-LIN2-ADH, respectively, all of which display very high efficacies of prochiral carbonyl conversion with respect to conversion rates and enantiomeric excess values. ADH/FDH represents co-expression of Lb-ADH and Cb-FDH under different promoters in a single vector. Fusion of Lb-ADH and Cb-FDH by a linker peptide LIN1 (GGGGS)2 or LIN2 (EAAAK)2 generates the two bifunctional enzymes FDH-LIN1-ADH and FDH-LIN2-ADH, which enable efficient asymmetric reduction of prochiral ketones in whole-cell biotransformation.
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