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Isolation and characterization of racemase from Ensifer sp. 23-3 that acts on α-aminolactams and α-amino acid amides.
- 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.
- Subjects :
- Aminobutyrates metabolism
Caprolactam metabolism
Cloning, Molecular
Escherichia coli genetics
Escherichia coli metabolism
Hydrogen-Ion Concentration
Piperidones metabolism
Racemases and Epimerases genetics
Racemases and Epimerases isolation & purification
Recombinant Proteins genetics
Recombinant Proteins metabolism
Rhizobiaceae enzymology
Sequence Analysis, DNA
Amides metabolism
Amino Acids metabolism
Racemases and Epimerases metabolism
Rhizobiaceae genetics
Subjects
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