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Updated: Jun 22, 2026

Enzymatic Cascade Reactions for the Synthesis of Chiral Amino Alcohols from L-lysine
Published on: February 16, 2018
Transaminase-catalyzed asymmetric synthesis of L-2-aminobutyric acid from achiral reactants
Jong-Shik Shin1, Byung-Gee Kim
1Department of Biotechnology, Yonsei University, Shinchon-Dong 134, Seodaemun-Gu, Seoul, 120-749, South Korea. enzymo@yonsei.ac.kr
Abstract:
Asymmetric synthesis of an unnatural amino acid was demonstrated by omega-transaminase from Vibrio fluvialis JS17. L-2-Aminobutyric acid was synthesized from 2-oxobutyric acid and benzylamine with an enantiomeric excess higher than 99%. The reaction showed severe product inhibition by benzaldehyde, which was overcome by employing a biphasic reaction system to remove the inhibitory product from the aqueous phase. In a typical biphasic reaction (50 mM 2-oxobutyric acid, 70 mM benzylamine and 2.64 U/ml purified enzyme) using hexane as an extractant, conversion of 2-oxobutyric acid reached 96% in 5 h whereas only 39% conversion was obtained without the product extraction.
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