Enzymatic synthesis of l-norephedrine by coupling recombinant pyruvate decarboxylase and ω-transaminase

• DOI: 10.1007/s00253-014-5797-1
• Publication Date: 2014-05-12T02:50:44Z
• Authors: Xuri Wu; Mengdan Fei; Yong Chen; Zongqiang Wang; Yijun Chen
• Keywords: Commodity chemicals; Transaminase; Biotransformation

L-Norephedrine, a natural plant alkaloid, possesses similar activity as ephedrine and can be used as a vicinal amino alcohol for the asymmetric synthesis of a variety of optically pure compounds, including pharmaceuticals, fine chemicals, and agrochemicals. Because of the existence of two asymmetric centers, efficient synthesis of L-norephedrine has been challenging. In the present study, an R-selective pyruvate decarboxylase from Saccharomyces cerevisiae and an S-selective ω-transaminase from Vibrio fluvialis JS17 were coupled to develop a sequential process for the stereoselective biosynthesis of L-norephedrine. After systematic optimization of the reaction conditions, a green, economic, and practical biocatalytic method to prepare L-norephedrine was established to achieve de and ee values of greater than 99.5 % and a molar yield over 60 %. The present coupling approach can facilitate the development of sequential reactions by various biocatalysts.