Purification and Characterization of an Alkaline Lipase from Streptomyces sp. AU-153 and Evaluation of Its Detergent Compatibility

High Resolution Image Download MS PowerPoint Slide Detergent-compatible lipases are increasingly valued for their ability to remove stains under low-temperature and environmentally friendly washing conditions. Their industrial applicability depends on achieving high enzyme production, cost-effective purification, and stability within detergent formulations. Here, we report the purification and characterization of a highly active extracellular lipase from Streptomyces sp. AU-153 (1543 U/mL, p -NPP assay). A simplified aqueous two-phase system (ATPS) of poly(ethylene glycol) and sodium chloride achieved 8-fold purification with a recovery of 272.7%. The purified enzyme exhibited optimal activity at pH 8.0 and 40 °C, maintained stability across pH 7–11, and retained substantial activity up to 60 °C. Activity was enhanced by Ca 2+, Mg 2+, and β-mercaptoethanol, whereas PMSF inhibited activity. The lipase remained stable in various commercial detergents and in the presence of surfactants, oxidizing agents, and boron compounds. It also showed affinity toward sunflower and thermally degraded olive oils. Low-temperature washing assays confirmed its effectiveness in oil stain removal. To our knowledge, ATPS-based purification and washing performance of Streptomyces lipases have each been reported only once, and this study is the first to integrate both approaches for the same enzyme. Moreover, Streptomyces sp. AU-153 displayed one of the highest native extracellular lipase activities documented for the genus, while the ATPS protocol achieved one of the highest recoveries reported for microbial lipases. These findings establish strain AU-153 as a promising natural source of detergent-compatible lipases and highlight its potential for enzyme-based washing applications.