Biocatalytic production of (S)-2-aminobutanamide by a novel d-aminopeptidase from Brucella sp. with high activity and enantioselectivity.

Abstract:

:As the important chiral building block of levetiracetam, the synthesis of (S)-2-aminobutanamide has attracted a great deal of attention. The d-aminopeptidase catalyzed kinetic resolution of 2-aminobutanamide was demonstrated as an effective strategy for (S)-2-aminobutanamide production. In this study, a novel d-aminopeptidase from Brucella sp. (Bs-Dap) was screened and systematically characterized. The enzyme exhibited maximum activity at 45°C, pH 8.0 and it showed relatively low Km value toward 2-aminobutanamide, indicating its high affinity to the substrate. Kinetic resolution of 300g/L 2-aminobutanamide by recombinant Escherichia coli whole cells (4g/L wet cell weight) resulted in 50% conversion and >99% e.e. within 80min. The catalytic properties of Bs-Dap demonstrated its great potential for industrial production of (S)-2-aminobutanamide.

journal_name

J Biotechnol

journal_title

Journal of biotechnology

authors

Tang XL,Lu XF,Wu ZM,Zheng RC,Zheng YG

doi

10.1016/j.jbiotec.2017.12.003

subject

Has Abstract

pub_date

2018-01-20 00:00:00

pages

20-26

eissn

0168-1656

issn

1873-4863

pii

S0168-1656(17)31752-2

journal_volume

266

pub_type

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