De novo construction of multi-enzyme system for one-pot deracemization of (R,S)-1-phenyl-1,2-ethanediol by stereoinversion of (S)-enantiomer to the corresponding counterpart

Publication date: Available online 7 April 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Bin Li, Yao Nie, Xiao Qing Mu, Yan Xu Deracemization via oxidoreductive stereoinversion is one of the most attractive methods for the preparation of enantiomerically pure compounds. However, available enzymatic system is yet limited for efficiently catalyzing deracemization to produce optically pure alcohol in certain configuration. Through evaluation of available stereoselective oxidoreductases on activity, selectivity, and cofactor dependency, the suitable candidates were obtained to construct the enzymatic deracemization system involving cofactor self-recycling. For deracemizing (R,S)-1-phenyl-1,2-ethanediol (PED) to (R)-PED, a facile one-pot system was established by combination of two stereoselective oxidoreductases, the stereospecific carbonyl reductase 1 (SCR1) and the ketoreductase (KRD). To rebalance the activities and catalytic functions of different enzymes involved in the multi-enzyme system, the reaction conditions of SCR1-catalyzed oxidation and KRD-mediated reduction were optimized, respectively. Consequently, the deracemization system involving cofactor self-recycling was built to produce (R)-PED with the optical purity of 95.50%e.e. and the yield of 91.62% from the corresponding racemate (1gL−1), under the optimal reaction conditions including activity ratio of SCR1/KRD 1:4 (SCR1 10UmL−1 and KRD 40UmL−1), molar ratio of NADP+/NADPH 3...
Source: Journal of Molecular Catalysis B: Enzymatic - Category: Biochemistry Source Type: research