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Isolation and characterization of racemase from Ensifer sp. 23-3 that acts on α-aminolactams and α-amino acid amides.

Authors :
Matsui D
Fuhshuku KI
Nagamori S
Takata M
Asano Y
Source :
Journal of industrial microbiology & biotechnology [J Ind Microbiol Biotechnol] 2017 Nov; Vol. 44 (11), pp. 1503-1510. Date of Electronic Publication: 2017 Sep 19.
Publication Year :
2017

Abstract

Limited information is available on α-amino-ε-caprolactam (ACL) racemase (ACLR), a pyridoxal 5'-phosphate-dependent enzyme that acts on ACL and α-amino acid amides. In the present study, eight bacterial strains with the ability to racemize α-amino-ε-caprolactam were isolated and one of them was identified as Ensifer sp. strain 23-3. The gene for ACLR from Ensifer sp. 23-3 was cloned and expressed in Escherichia coli. The recombinant ACLR was then purified to homogeneity from the E. coli transformant harboring the ACLR gene from Ensifer sp. 23-3, and its properties were characterized. This enzyme acted not only on ACL but also on α-amino-δ-valerolactam, α-amino-ω-octalactam, α-aminobutyric acid amide, and alanine amide.

Details

Language :
English
ISSN :
1476-5535
Volume :
44
Issue :
11
Database :
MEDLINE
Journal :
Journal of industrial microbiology & biotechnology
Publication Type :
Academic Journal
Accession number :
28929416
Full Text :
https://doi.org/10.1007/s10295-017-1981-5