期刊
ADVANCED SYNTHESIS & CATALYSIS
卷 353, 期 8, 页码 1213-1217出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/adsc.201100132
关键词
alcohols; asymmetric catalysis; cofactor; oxidoreductases; reduction
资金
- National Natural Science Foundation of China [20902023, 31071604]
- Ministry of Science and Technology, P.R. China [2009CB724706, 2009ZX09501-016, 2011CB710803, 2011CB710805]
- China National Special Fund for State Key Laboratory of Bioreactor Engineering [2060204]
- Shanghai Leading Academic Discipline Project [B505]
A beta-ketoacyl-ACP reductase (FabG) gene from Bacillus sp. ECU0013 was heterologously overexpressed in Escherichia coli and the encoded protein was purified to homogeneity. The recombinant reductase could reduce a broad spectrum of prochiral ketones including aromatic ketones and keto esters and showed the highest activity in the asymmetric reduction of ethyl 2-oxo-4-phenylbutyrate (OPBE). Using E. coli cells coexpressing both FabG and glucose dehydrogenase (GDH) genes, as much as 620 g.L-1 of OPBE was almost stoichiometrically converted to ethyl (S)-2-hydroxy-4-phenylbutyrate [(S)-HPBE] with excellent (> 99%) enantiomeric excess. More importantly, the process could be performed smoothly without external addition of an expensive cofactor as usually done and could be scaled up very easily. All these positive features demonstrate the applicability of this reductase for the large-scale production of optically active a-hydroxy acids/esters.
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