Asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate with two co-existing, recombinant Escherichia coli strains.
Two recombinant strains, E. coli M15 (pQE30-alr0307) and E. coli M15 (pQE30-gdh0310), which were constructed to express, respectively, an NADPH-dependent aldehyde reductase gene and a glucose dehydrogenase gene, were mixed in an appropriate ratio and used for the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The former strain acted as catalyst and the latter functioned in NADPH regeneration. The biotransformation was completed effectively without any addition of glucose dehydrogenase or NADP+/NADPH. An optical purity of 99% (ee) was obtained and the product yield reached 90.5% from 28.5 mM: substrate.
Liu
Ying
Y
Department of Chemical Engineering and Bioengineering, Institute of Bioengineering, Zhejiang University, Hangzhou, Zhejiang, 310027, P.R. China.
Xu
Zhinan
Z
Jing
Keju
K
Jiang
Xiaoxia
X
Lin
Jianping
J
Wang
Fang
F
Cen
Peilin
P
D000090:Acetoacetates / Q000737:chemistry / Q000378:metabolism*; D000449:Aldehyde Reductase / Q000235:genetics / Q000378:metabolism; D002087:Butyrates / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005948:Glucose Dehydrogenases / Q000235:genetics / Q000378:metabolism; D007218:Industrial Microbiology / Q000379:methods*; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
D000090:Acetoacetates; D002087:Butyrates; D011994:Recombinant Proteins; C121244:ethyl 4-chloro-3-hydroxybutanoate; D009249:NADP; C111982:ethyl 4-chloro-3-oxobutanoate; D005948:Glucose Dehydrogenases; D000449:Aldehyde Reductase