Purification and characterization of a novel extracellular, alkaline, thermoactive, and detergent-compatible lipase from Aeromonas caviae LipT51 for application in detergent industry.

Abstract

Lipase producer bacterium isolated from Erzurum was identified as Aeromonas caviae LipT51 (GenBank ID: MN818567.1) by 16S rDNA sequencing and conventional methods. Extracellular lipase was purified by ammonium sulphate precipitation, centrifugal filtration, and anion-exchange chromatography resulting in 6.1-fold purification with 28% final yield. Molecular weight was 31.6 kDa on SDS-PAGE. Lipase was stable over a broad range of pH (6-11) and temperature (25-70 °C), and showed optimum activity at pH 9 and 60 °C. Km and Vmax for pNPP hydrolysis were 0.88 mM and 34.2 U/mg protein, respectively. Ba2+, Ca2+, Co2+, Cu2+, Fe3+, and Mg2+ increased activity, while Mn2+, Mo2+, Ni2+, Zn2+, and other additives partially decreased. Activity and stability increased with laundry detergent and slightly decreased with handwash and dishwashing detergents. Alkaline and thermostable lipase from newly isolated A. caviae has been shown for the first time to be remarkably compatible with laundry detergent and improve washing performance by enhanced oil-stain removal.