Artículo
Characterization of a novel thermostable enzyme from thermus sp. 2.9 with phospholipase and acyltransferase activities
Navas, Laura Emilce
; Jacobsen, Monica Ofelia
; Benintende, Graciela Beatriz; Zandomeni, Rubén Oreste; Berretta, Marcelo Facundo
![Icon](/themes/CONICETDigital/images/conicet.png)
![Icon](/themes/CONICETDigital/images/conicet.png)
![Icon](/themes/CONICETDigital/images/conicet.png)
Fecha de publicación:
01/2019
Editorial:
Karger
Revista:
Journal of Molecular Microbiology and Biotechnology
ISSN:
1464-1801
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
Phospholipases are classified in different enzyme families according to the ester bond they cleave within phospholipids. The use of phospholipases in industrial processes has prompted the search for new enzymes with differential properties. A gene encoding a novel phospholipase (PLP-2.9) was identified in the genome of the thermophilic strain Thermus sp. 2.9. The analysis of the primary sequence unveiled a patatin-like domain. The alignment of the amino acid sequence of PLP-2.9 to other bacterial patatin-related proteins showed that the four blocks characteristic of this type of phospholipases and the amino acids representing the catalytic dyad are conserved in this protein. PLP-2.9 was overexpressed in Escherichia coli and the purified enzyme was characterized biochemically. PLP-2.9 hydrolyzed p-nitrophenyl palmitate at alkaline pH over a wide range of temperatures (55-80°C), showing high thermostability. PLP-2.9 displayed phospholipase A and acyltransferase activities on egg yolk phosphatidylcholine. Due to its high thermostability, PLP-2.9 has potential applications as a catalyst in several industrial processes.
Archivos asociados
Licencia
Identificadores
Colecciones
Articulos(SEDE CENTRAL)
Articulos de SEDE CENTRAL
Articulos de SEDE CENTRAL
Citación
Navas, Laura Emilce; Jacobsen, Monica Ofelia; Benintende, Graciela Beatriz; Zandomeni, Rubén Oreste; Berretta, Marcelo Facundo; Characterization of a novel thermostable enzyme from thermus sp. 2.9 with phospholipase and acyltransferase activities; Karger; Journal of Molecular Microbiology and Biotechnology; 28; 3; 1-2019; 99-106
Compartir
Altmétricas