Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities

NAVAS, LAURA EMILCE; FLORIN-CHRISTENSEN, MÓNICA; BENINTENDE, GRACIELA BEATRIZ; ZANDOMENI, RUBÉN ORESTE; BERRETTA, MARCELO FACUNDO

JOURNAL OF MOLECULAR MICROBIOLOGY AND BIOTECHNOLOGY

KARGER

Año: 2018 vol. 28 p. 99 - 106

1464-1801

Phospholipases are classified in different enzyme familiesaccording to the ester bond they cleave within phospholipids.The use of phospholipases in industrial processes hasprompted the search for new enzymes with differentialproperties. A gene encoding a novel phospholipase (PLP_2.9)was identified in the genome of the thermophilic strain Thermussp. 2.9. The analysis of the primary sequence unveiled apatatin-like domain. The alignment of the amino acid sequenceof PLP_2.9 to other bacterial patatin-related proteinsshowed that the four blocks characteristic of this type ofphospholipases and the amino acids representing the catalyticdyad are conserved in this protein. PLP_2.9 was overexpressedin Escherichia coli and the purified enzyme was characterizedbiochemically. 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 displayedphospholipase A and acyltransferase activities on egg yolkphosphatidylcholine. Due to its high thermostability, PLP_2.9has potential applications as a catalyst in several industrialprocesses.