详细信息
Efficient Reduction of Ethyl 2-Oxo-4-phenylbutyrate at 620 g.L-1 by a Bacterial Reductase with Broad Substrate Spectrum ( SCI-EXPANDED收录)
文献类型:期刊文献
英文题名:Efficient Reduction of Ethyl 2-Oxo-4-phenylbutyrate at 620 g.L-1 by a Bacterial Reductase with Broad Substrate Spectrum
作者:Ni, Yan[1];Li, Chun-Xiu[1];Zhang, Jie[1];Shen, Nai-Dong[1];Bornscheuer, Uwe T.[2];Xu, Jian-He[1]
机构:[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Lab Biocatalysis & Synthet Biotechnol, Shanghai 200237, Peoples R China;[2]Ernst Moritz Arndt Univ Greifswald, Inst Biochem, Dept Biotechnol Enzyme Catalysis, D-17487 Greifswald, Germany
年份:2011
卷号:353
期号:8
起止页码:1213
外文期刊名:ADVANCED SYNTHESIS & CATALYSIS
收录:;WOS:【SCI-EXPANDED(收录号:WOS:000291530800004)】;
基金:This work was financially supported by the National Natural Science Foundation of China (Nos. 20902023 & 31071604), Ministry of Science and Technology, P.R. China (Nos. 2009CB724706, 2009ZX09501-016, 2011CB710803 & 2011CB710805), China National Special Fund for State Key Laboratory of Bioreactor Engineering (No. 2060204) and Shanghai Leading Academic Discipline Project (No. B505).
语种:英文
外文关键词:alcohols; asymmetric catalysis; cofactor; oxidoreductases; reduction
摘要: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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