Purification and characterization of lipase from Acinetobacter haemolyticus TA 106 isolated from human skin

Abstract

Acinetobacter sp. isolated from healthy human skin of a tribal population was tested for lipase production.Medium optimization was achieved to increase the production. Purification was carried out by a one-step purification process using DEAE Sephadex A-50. The molecular weight of the lipase was approximately 60 kDa by SDS-PAGE. The purified lipase showed not only good stability in the presence of detergents and organic solvents but also an enhancement of activity. The lipase was active at pH 9 and displayed good activity at 0, 30 and 37°C. It was inhibited in EDTA, suggesting that it is a metalloenzyme. The cations like Ca2+, Mg2+, and Cu2+ significantly reduced the lipase activity at 5 mM concentration. The lipase converted 67% oleic acid to methyl oleate at 37°C at 72 h. All these features make this lipase an important candidate from an industrial point of view.

Keywords

• Acinetobacter
• human skin
• lipase
• one step purification
• methyl oleate synthesis