An NADPH-dependent <Emphasis Type="Italic">Lactobacillus composti</Emphasis> short-chain dehydrogenase/reductase: characterization and application to (<Emphasis Type="Italic">R</Emphasis>)-1-phenylethanol synthesis |
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Authors: | Ya-Jun Wang Bin-Bin Ying Min Chen Wei Shen Zhi-Qiang Liu Yu-Guo Zheng |
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Institution: | 1.Key Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering,Zhejiang University of Technology,Hangzhou,People’s Republic of China;2.Engineering Research Center of Bioconversion and Biopurification of the Ministry of Education,Zhejiang University of Technology,Hangzhou,People’s Republic of China |
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Abstract: | A new anti-Prelog short-chain dehydrogenase/reductase (SDR) encoding gene lcsdr was cloned from Lactobacillus composti DSM 18527, and heterologously expressed in Escherichia coli. LcSDR is nicotinamide adenine dinucleotide phosphate (NADPH)-dependent and has a molecular weight of approximately 30 kDa. The optimal pH and temperature were 6.5 and 30?°C, respectively. The maximal reaction rate Vmax was 133.9 U mg?1; the Michaelis–Menten constant K m of LcSDR were 0.345 mM for acetophenone (1a), and 0.085 mM for NADPH. Through introducing an EsGDH-catalyzed NADPH regeneration system, a biocatalytic process for (R)-1-phenylethanol ((R)-1b) was developed with outstanding time–space yield. Under the optimized conditions, 50 g l?1 1a was converted to (R)-1b in 2 h with a yield of 93.8%, enantiomeric excess of product (e.e.p) above 99% and space–time yield of 562.8 g l?1 d?1. |
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