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August 30, 2026Microbial Cell FactoriesOpen Access

Recombinant thermotolerant alkaline lipase from Lysinibacillus fusiformis for detergent and hard (Ras) cheese applications: cloning, expression, molecular docking, and characterization

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Authors

GEGhada M. El-SayedCairo UniversityHWHala R. WehaidyNational Research CentreAKA. KholifNorth Carolina Agricultural and Technical State University

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Implication

Biochemical study demonstrates high stability and activity of recombinant Lysinibacillus fusiformis lipase, indicating its industrial potential in detergents and accelerated cheese ripening.

Key Points

  • To isolate, clone, and express lipase genes from Lysinibacillus fusiformis to produce a thermostable, alkaline lipase for industrial detergent and food applications.
  • Screened bacterial isolates, sequenced the 16S rRNA gene of Lysinibacillus fusiformis (GenBank PP757498), and cloned three lipase genes (est, est2, lipA) into Escherichia coli BL21 (DE3).
  • Characterized enzyme activity across temperature and pH ranges, performed molecular docking against olive oil fatty acids, and tested applications in fabric stain removal and Ras cheese maturation.
  • Recombinant lipA lipase (rLipase) demonstrated higher activity than the native enzyme (150 U/mL vs 56.2 U/mL), reaching a maximum activity of 320 U/mL at 80 °C and pH 9.
  • Molecular docking identified strong binding affinity for linoleic acid (−8.0 kcal/mol), oleic acid (−7.8 kcal/mol), and palmitic acid (−7.3 kcal/mol), stabilized by hydrophobic bonds and residue VAL250.
  • Supplementation with 0.4% rLipase enhanced oil stain removal from cotton fabric and shortened Ras cheese ripening from 120 to 90 days without compromising quality.

Cite This Study

El-Sayed et al. (2026) studied this question.

synapsesocial.com/papers/6a93f1396c1a8fb52e79dfe9https://doi.org/10.1186/s12934-026-03084-w
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