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Updated: Jun 23, 2026
Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Enzymatic characterization of 30 kDa lipase from Pseudomonas aeruginosa ATCC 27853
Lidija T Izrael-Zivkovic1, Gordana D Gojgic-Cvijovic, Kristina R Gopcevic
1School of Medicine, Department of Chemistry, University of Belgrade, Belgrade, Serbia.
Abstract:
An extracellular lipase from Pseudomonas aeruginosa ATCC 27853 has been purified and its enzymatic characteristics were determined. According to SDS-PAGE and gel filtration molecular mass estimated to be 30 kDa, what classified the lipase in group I.1. Although 14 lipases from P. aeruginosa with similar molecular mass are referred to date, their basic enzymatic properties have not been reported yet. To address the gap we found: the optimal temperature and pH in water solution being 50 degrees C and 9.3, respectively; the lipase was inhibited with Hg2+ ions and sodium dodecylsulphate (SDS), while non-ionic detergent Triton X-100 activated the enzyme; the lipase hydrolyzed more rapidly middle chain triglycerides and it was not regiospecific; the lipase demonstrated naturally occurring stability in different organic solvents with concentrations ranging from 30 to 70%, including good thermal stability in 30% organic solvent solution. Even though strain P. aeruginosa ATCC 27853 was not isolated from extreme environment it showed activity in organic solvent suggesting that this lipase is suitable for variety of applications, including reactions in water restricted medium and bioremediation of contaminations by organic solvents.
Insights
This study details a purified Pseudomonas aeruginosa lipase, revealing its optimal conditions and stability in organic solvents. This enzyme shows potential for industrial applications, particularly in non-aqueous environments and bioremediation.
Area of Science:
- Microbiology
- Enzymology
- Biochemistry
Background:
- Pseudomonas aeruginosa is known to produce extracellular lipases.
- While several lipases from this bacterium have been identified, their detailed enzymatic properties remain largely uncharacterized.
- This study addresses the gap in knowledge regarding the specific characteristics of a P. aeruginosa lipase.
Purpose of the Study:
- To purify an extracellular lipase from Pseudomonas aeruginosa ATCC 27853.
- To determine the enzymatic characteristics of the purified lipase.
- To assess its stability and potential applications in various environments.
Main Methods:
- Purification of extracellular lipase using standard biochemical techniques.
- Determination of molecular mass via SDS-PAGE and gel filtration.
- Enzymatic characterization including optimal temperature, pH, substrate specificity, and stability assays in organic solvents.
Main Results:
- The purified lipase has a molecular mass of 30 kDa, classifying it in group I.1.
- Optimal activity was observed at 50°C and pH 9.3.
- The enzyme was inhibited by Hg2+ and sodium dodecyl sulfate (SDS) but activated by Triton X-100.
- It efficiently hydrolyzed medium-chain triglycerides without regioselectivity.
- The lipase exhibited remarkable stability in 30-70% organic solvents and good thermal stability in 30% organic solvent solutions.
Conclusions:
- The characterized Pseudomonas aeruginosa lipase possesses unique properties, including stability in organic solvents.
- Despite not originating from an extreme environment, its solvent tolerance suggests broad applicability.
- Potential uses include biocatalysis in low-water environments and bioremediation of organic solvent contamination.
