Related Experiment Video
Updated: Jun 28, 2025
09:47
Facile Preparation of Internally Self-assembled Lipid Particles Stabilized by Carbon Nanotubes
Published on: February 19, 2016
9.7K
Switchable CO2-Responsive Janus Nanoparticle for Lipase Catalysis in Pickering Emulsion
Wei Wang1,2,3, Ruoyu Zhou1,2,3, Simiao Di1,2,3
1State Key Laboratory of Marine Food Processing and Safety Control, College of Food Science and Engineering, Ocean University of China, Qingdao 266404, China.
Journal of Agricultural and Food Chemistry
|April 19, 2024
Summary
This study introduces CO2-responsive switchable Janus nanoparticles for stabilizing enzymes in Pickering emulsions, significantly reducing enzyme leakage and maintaining catalytic activity through 10 reaction cycles.
Area of Science:
- Biocatalysis
- Materials Science
- Chemical Engineering
Background:
- Enzyme immobilization in Pickering emulsions is vital for biphasic catalysis.
- Mechanical stress during reactions causes enzyme leakage, reducing stability.
- Need for robust enzyme carriers in switchable catalytic systems.
Purpose of the Study:
- To develop a CO2-responsive switchable Janus nanoparticle (CrSJ NP) for enzyme immobilization.
- To create a stable Pickering emulsion catalytic system for biphasic reactions.
- To enhance enzyme stability and reduce leakage during catalytic conversions.
Main Methods:
- Synthesized silica-based Janus nanoparticles with distinct surface functionalities.
- Covalently immobilized lipase onto the CrSJ NPs.
- Utilized CO2 to trigger rapid conversion of the Pickering emulsion.
Main Results:
- CrSJ NPs effectively reduced enzyme leakage and improved immobilization stability.
- The Pickering emulsion maintained structural integrity after repeated transformations.
- Immobilized enzyme retained 77.7% (esterification) and 79.5% (hydrolysis) activity after 10 cycles.
- Catalytic efficiency (Vmax) increased compared to free lipase.
Conclusions:
- CO2-responsive CrSJ NPs offer a stable platform for enzyme immobilization in Pickering emulsions.
- Covalent immobilization significantly enhances enzyme stability and reusability.
- This system presents a promising approach for efficient and sustainable biphasic catalysis.
