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- Title
Whole-cell biotransformation systems for reduction of prochiral carbonyl compounds to chiral alcohol in Escherichia coli.
- Authors
Bingjuan Li; Yuxia Li; Dongmei Bai; Xin Zhang; Huiying Yang; Jie Wang; Gang Liu; Juejie Yue; Yan Ling; Dongsheng Zhou; Huipeng Chen
- 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.
- Subjects
LACTOBACILLUS brevis; ALCOHOL dehydrogenase; PROCHIRALITY; CARBONYL compounds; ESCHERICHIA coli; CATALYSIS
- Publication
Scientific Reports, 2014, p1
- ISSN
2045-2322
- Publication type
Article
- DOI
10.1038/srep06750