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

**Authors:** Rukiye Boran Gulen, Aysel Ugur, Nurdan Sarac

PMC · DOI: 10.1021/acsomega.5c11317 · 2026-01-23

## 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.

## Key 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
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.

## Linked entities

- **Proteins:** lipase (lipase)
- **Chemicals:** p-NPP (PubChem CID 77949), Ca2+ (PubChem CID 271), Mg2+ (PubChem CID 888), PMSF (PubChem CID 4784), sodium chloride (PubChem CID 5234), poly(ethylene glycol) (PubChem CID 9033)

## Full-text entities

- **Chemicals:** sodium chloride (MESH:D012965), poly-(ethylene glycol) (MESH:D011092), olive oils (MESH:D000069463), AU-153 (-), oil (MESH:D009821), boron compounds (MESH:D001896)
- **Species:** Helianthus annuus (common sunflower, species) [taxon 4232], Streptomyces sp. (species) [taxon 1931]

## Figures

12 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12902849/full.md

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Source: https://tomesphere.com/paper/PMC12902849