A novel low-temperature resistant alkaline lipase from a soda lake fungus strain Fusarium solani N4-2 for detergent formulation

The effects of temperature, pH, and various components in a detergent on the activity and stability of a lipase produced by a soda lake fungus strain Fusariumsolani N4-2 were studied in a preliminary evaluation for use in detergent formulation. The molecular mass of the lipase was 31.6 kDa by SDS-PAGE after purification using acetone fractionation and Q-sepharose ion exchange technique. In aqueous solutions, the lipase showed maximal activity at pH 9.0 in a glycine–NaOH buffer at 30 °C. At 0 °C and 10 °C, 52.3% and 82.6% of its maximum activities were detained, respectively. Among the metal ions tested, additions of Cu2+, Ca2+, Mg2+, Al3+ and Mn2+ ions were found to enhance the enzyme activity while Zn2+, Ba2+ and Hg2+ ions showed inhibitory effects. Compared with the commercial lipase Lipolase®, the enzyme showed better stability towards selected surfactants, commercial detergents, oxidizing agents and proteases. The remarkable resistance capability of the lipase makes it a potential additive for better detergent formulation.