earticle

영어

Enantiomerically pure amino acids are widely used as building blocks for the synthesis of a number of chiral drugs. Generally, enantiopure amino acids can be accomplished in two ways: (i) asymmetric synthesis of a pro-chiral compound, and (ii) kinetic resolution of racemic amino acid. However, there are disadvantages to be resolved for efficient preparation of enantiopure amino acids in these approaches. First, in case of asymmetric synthesis, pro-chiral compounds are not readily available compared to racemic amino acid. Second, the theoretical yield of kinetic resolution has a limit of 50%. Here, we report an efficient biocatalytic process for deracemization of amino acids, starting with racemic amino acid to obtain enantiopure amino acid, employing a coupled enzyme strategy to overcome the limitation of two approaches as described above. In this study, the deracemization process consist of kinetic resolution of racemic amino acid employing D-amino acid aminotransferase and asymmetric synthesis of L-amino acid employing ω-transaminase. The coupled reaction consisting of D-amino acid aminotransferase and ω-transaminase resulted in 99 % ee of L- homoalanine using 100 mM DL-homoalanine, 70 mM α-ketoglutarate, and 70 mM isopropylamine. This work was supported by the Advanced Biomass R&D Center (ABC-2010-0029737) through the National Research Foundation of Korea funded by the Ministry of Education, Science, and Technology.