Purification and Characterization of an Alkaline Lipase from Streptomyces sp. AU-153 and Evaluation of Its Detergent Compatibility
Rukiye Boran Gulen, Aysel Ugur, Nurdan Sarac

TL;DR
Scientists purified a highly active lipase from a Streptomyces bacteria and found it works well in detergents for stain removal at low temperatures.
Contribution
This study is the first to combine ATPS purification with detergent compatibility testing for a Streptomyces lipase.
Findings
The lipase from Streptomyces sp. AU-153 showed high activity (1543 U/mL) and stability in detergent conditions.
ATPS purification achieved an 8-fold purification with 272.7% recovery of the enzyme.
The enzyme effectively removed oil stains in low-temperature washing tests.
Abstract
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 Ca2+, Mg2+, and β-mercaptoethanol, whereas PMSF inhibited activity. The lipase remained stable in various commercial…
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Taxonomy
TopicsEnzyme Catalysis and Immobilization · Chemical and Physical Properties in Aqueous Solutions · Microbial Metabolic Engineering and Bioproduction
