Related Experiment Video
Updated: Jan 9, 2026

Isolation and Chemical Characterization of Lipid A from Gram-negative Bacteria
Published on: September 16, 2013
Partial purification and characterization acidophilic lipase from Bacillus cereus ALP E1
Nindy Novita Sari1, Nurhasanah2, Titin Haryati3
1Master Program in Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung, Indonesia.
Researchers discovered a novel microbial lipase from Bacillus cereus ALP E1 in seawater. This acidophilic enzyme shows high activity and stability, making it promising for industrial applications.
Area of Science:
- Microbiology
- Enzymology
- Biotechnology
Background:
- Microbial lipases are vital for industrial processes.
- Bacillus cereus is a known lipase producer, but exploration is limited.
- Novel lipases are needed for diverse applications.
Purpose of the Study:
- To isolate and purify lipase from Bacillus cereus ALP E1.
- To characterize the biochemical properties of the enzyme.
- To assess its potential for industrial use.
Main Methods:
- Isolation of Bacillus cereus ALP E1 from seawater.
- Submerged fermentation for lipase production.
- Partial purification using ammonium sulphate fractionation and dialysis.
- Characterization of enzyme activity, pH, temperature, and substrate specificity.
- Analysis using SDS-PAGE.
Main Results:
- Partially purified lipase with 12.31-fold purification and specific activity of 31083.14 U/mg.
- SDS-PAGE indicated a molecular weight of approximately 55 kDa.
- Optimal activity at pH 5 and 40°C, with preference for p-nitrophenyl stearate (C18).
- Enzyme activity influenced by divalent cations (Ba2+, Mg2+), surfactants (Tween 20, Tween 80), and organic solvents (chloroform).
Conclusions:
- Seawater is a valuable source for discovering highly active lipases.
- The characterized lipase from Bacillus cereus ALP E1 exhibits properties suitable for industrial applications.
- Further research can optimize its use in various sectors.
More Related Videos
08:27Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
Published on: January 7, 2019
08:59Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016