Characterization of Alkaline Lipase from Fusarium Oxysporum and the Effect of Different Surfactants and Detergents on the Enzyme Activity

Nowadays, there is a tendency of use of low temperature in laundry cleaning for both environmental and economical reasons, which makes the use of enzymes in detergent products indispensable. Since lipases are efficient catalyst both in solution and at the water-liquid interface, they are potentially suitable for lipid stain removal applications in industrial laundry and household detergents. The effect of different commercial detergents and surfactants on enzymatic activity of lipase from Fusarium oxysporum was observed through p-nitrophenylpalmitate (pNPP) assay. The enzyme was compatible with various ionic and non-ionic surfactants as well as commercial detergents. Lipase activity was strongly inhibited by Sodium Dodecyl Sulphate (SDS), but not by Triton X-100 and Triton X-114. The best assay conditions observed for this lipase were pH 8.0 and 50oC. The enzyme was stable at alkaline pH and remained 93% of residual activity during 1 h incubation at 60oC. The highest lipase activity was measured with triglycerides of middle and long chain fatty acids (C8-C18). This enzyme showed a variable specifity/hydrolytic activity towards various fats and oils. All these properties and its resistance towards various surfactants and tolerance to commercial detergents make this lipase a potential additive for detergent formulation.