Characterization of a Novel Thermostable Enzyme from < b > < i > Thermus < /i > < /b > sp. 2.9 with Phospholipase and Acyltransferase Activities

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 strainThermus 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 inEscherichia coli and the purified enzyme was characterized biochemically. PLP_2.9 hydrolyzedp-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.J Mol Microbiol Biotechnol 2018;28:99 –106
Source: Journal of Molecular Microbiology and Biotechnology - Category: Microbiology Source Type: research