|
type |
Journal Article |
authors |
Matsui D, Fuhshuku KI, Nagamori S, Takata M, Asano Y |
title |
Isolation and characterization of racemase from Ensifer sp. 23-3 that acts on α-aminolactams and α-amino acid amides |
journal |
J Ind Microbiol Biotechnol |
Activity |
5.1.1.15 |
Family |
5.1.1.15 |
sel |
selected |
ui |
28929416 |
year |
(2017) |
volume |
44 |
number |
11 |
pages |
1503-1510 |
| |
keywords |
Racemase; Racemization; α-Amino acid amide; α-Amino-ε-caprolactam; α-Aminolactam |
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. |
last changed |
2018/04/03 14:54 |
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