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Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities
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
[ver mas...]
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.
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![Thumbnail](/bitstream/handle/20.500.12123/7513/jourmolmicroandbio.jpg?sequence=3&isAllowed=y)
Fuente
Journal of Molecular Microbiology and Biotechnology 28 (3) : 99–106 (2018)
Fecha
2018
Editorial
Karger
ISSN
1464-1801
1660-2412
1660-2412
Formato
pdf
Tipo de documento
artículo
Palabras Claves
Derechos de acceso
Restringido
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