Characterization of Detergent-Compatible Lipases from Candida albicans and Acremonium sclerotigenum under Solid-State Fermentation

[Image: see text] The purpose of this study was to compare and explore the potential of two distinct lipases at industrial levels after their production using wheat bran substrate in solid-state fermentation. Lipases from Candida albicans (C. albicans) and Acremonium sclerotigenum (A. sclerotigenum) were characterized to assess their compatibility and suitability for use in laundry detergents. The effects of pH, temperature, metal ions, inhibitors, organic solvents, and various commercially available detergents on these lipases were studied in order to compare their activity and stability profiles and check their stain removal ability. Both lipases remained stable across the wide pH (7–10) and temperature (30–50 °C) ranges. C. albicans lipase exhibited optimum activity (51.66 U/mL) at pH 7.0 and 37 °C, while A. sclerotigenum lipase showed optimum activity (52.12 U/mL) at pH 8.0 and 40 °C. The addition of Ca(2+) and Mg(2+) ions enhanced their activities, while sodium dodecyl sulfate (SDS) and ethylenediamine tetraacetic acid (EDTA) reduced their activities. Lipase from both strains showed tolerance to various organic solvents and considerable stability and compatibility with commercially available laundry detergents (>50%); however, A. sclerotigenum lipase performed slightly better. Characterization of these crude lipases showed nearly 60% relative activity after incubation for 2 h in various detergents, thus suggesting their potential to be employed in the formulation of laundry detergents with easy and efficient enzyme production. The production of thermostable and alkaline lipases from both strains makes them an attractive option for economic gain by lowering the amount of detergent to be used, thus reducing the chemical burden on the environment.