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 30kDa. The optimal pH and temperature were 6.5 and 30 °C, respectively. The maximal reaction rate Vmax was 133.9 Umg-1; the Michaelis-Menten constant K m of LcSDR were 0.345mM for acetophenone (1a), and 0.085mM 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 gl-1 1a was converted to (R)-1b in 2h with a yield of 93.8%, enantiomeric excess of product (e.e.p) above 99% and space-time yield of 562.8 gl-1d-1.
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