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 Biotechnoljournal_title
Journal of biotechnologyauthors
Tang XL,Lu XF,Wu ZM,Zheng RC,Zheng YGdoi
10.1016/j.jbiotec.2017.12.003subject
Has Abstractpub_date
2018-01-20 00:00:00pages
20-26eissn
0168-1656issn
1873-4863pii
S0168-1656(17)31752-2journal_volume
266pub_type
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