Characterization of sp. Ab3 Lipase and Its Coexpression with LEA Peptides.

sp. is a yellowish Gram-negative bacterium that is usually characterized by high concentrations of sphingophospholipids as lipid components. As microbial enzymes have been in high demand in industrial fields in the past few decades, this study hopes to provide significant information on lipase activities of sp., since limited studies have been conducted on the sp. lipase. A microbe from one collected Artic soil sample, ARC4, was identified as psychrotolerant sp., and it could grow in temperatures ranging from 0°C to 24°C. The expression of sp. lipase was successfully performed through an efficient approach of utilizing mutated group 3 late embryogenesis abundant (G3LEA) proteins developed from Polypedilum vanderplanki. Purified enzyme was characterized using a few parameters, such as temperature, pH, metal ion cofactors, organic solvents, and detergents. The expressed enzyme is reported to be cold adapted and has the capability to work efficiently under neutral pH (pH 5.0 to 7.0), cofactors like Na ion, and the water-like solvent methanol. Addition of nonionic detergents greatly enhanced the activity of purified enzyme. The mechanism of action of LEA proteins has remained unknown to many; in this study we reveal their presence and improved protein expression due to the molecular shielding effect reported by others. This paper should be regarded as a useful example of using such proteins to influence an existing expression system to produce difficult-to-express proteins.