Transaminase-catalyzed asymmetric synthesis of L-2-aminobutyric acid from achiral reactants

Jong Shik Shin; Byung Gee Kim

doi:10.1007/s10529-009-0057-7

Transaminase-catalyzed asymmetric synthesis of L-2-aminobutyric acid from achiral reactants

Jong Shik Shin, Byung Gee Kim

Research output: Contribution to journal › Article › peer-review

45 Citations (Scopus)

Abstract

Asymmetric synthesis of an unnatural amino acid was demonstrated by ω-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.

Original language	English
Pages (from-to)	1595-1599
Number of pages	5
Journal	Biotechnology Letters
Volume	31
Issue number	10
DOIs	https://doi.org/10.1007/s10529-009-0057-7
Publication status	Published - 2009 Aug

Bibliographical note

Funding Information:
Acknowledgment This work was supported by BK21 program from the Korean Ministry of Education, start-up research funds provided by Yonsei University and Seoul R&BD Program (NT080612, KU080657).

All Science Journal Classification (ASJC) codes

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1007/s10529-009-0057-7

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title = "Transaminase-catalyzed asymmetric synthesis of L-2-aminobutyric acid from achiral reactants",

abstract = "Asymmetric synthesis of an unnatural amino acid was demonstrated by ω-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.",

author = "Shin, {Jong Shik} and Kim, {Byung Gee}",

note = "Funding Information: Acknowledgment This work was supported by BK21 program from the Korean Ministry of Education, start-up research funds provided by Yonsei University and Seoul R&BD Program (NT080612, KU080657).",

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doi = "10.1007/s10529-009-0057-7",

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T1 - Transaminase-catalyzed asymmetric synthesis of L-2-aminobutyric acid from achiral reactants

AU - Shin, Jong Shik

AU - Kim, Byung Gee

N1 - Funding Information: Acknowledgment This work was supported by BK21 program from the Korean Ministry of Education, start-up research funds provided by Yonsei University and Seoul R&BD Program (NT080612, KU080657).

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N2 - Asymmetric synthesis of an unnatural amino acid was demonstrated by ω-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.

AB - Asymmetric synthesis of an unnatural amino acid was demonstrated by ω-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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Transaminase-catalyzed asymmetric synthesis of L-2-aminobutyric acid from achiral reactants

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

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