Purification, characterization, and gene cloning of a novel aminoacylase from Burkholderia sp. strain LP5_18B that efficiently catalyzes the synthesis of N-lauroyl-l-amino acids.
Biosci Biotechnol Biochem
; 83(10): 1964-1973, 2019 Oct.
Article
en En
| MEDLINE
| ID: mdl-31200632
ABSTRACT
An N-lauroyl-l-phenylalanine-producing bacterium, identified as Burkholderia sp. strain LP5_18B, was isolated from a soil sample. The enzyme was purified from the cell-free extract of the strain and shown to catalyze degradation and synthesis activities toward various N-acyl-amino acids. N-lauroyl-l-phenylalanine and N-lauroyl-l-arginine were obtained with especially high yields (51% and 89%, respectively) from lauric acid and l-phenylalanine or l-arginine by the purified enzyme in an aqueous system. The gene encoding the novel aminoacylase was cloned from Burkholderia sp. strain LP5_18B and expressed in Escherichia coli. The gene contains an open reading frame of 1,323 nucleotides. The deduced protein sequence encoded by the gene has approximately 80% amino acid identity to several hydratase of Burkholderia. The addition of zinc sulfate increased the aminoacylase activity of the recombinant E. coli strain.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Burkholderia
/
Amidohidrolasas
/
Aminoácidos
/
Ácidos Láuricos
Idioma:
En
Revista:
Biosci Biotechnol Biochem
Asunto de la revista:
BIOQUIMICA
/
BIOTECNOLOGIA
Año:
2019
Tipo del documento:
Article
País de afiliación:
Japón