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Published on: August 31, 2019
Enhanced Biodiesel Production with Eversa Transform 2.0 Lipase on Magnetic Nanoparticles
Kaiany Moreira Dos Santos1, Juliana de França Serpa1, Viviane de Castro Bizerra1
1Instituto de Engenharia e Desenvolvimento Sustentável - IEDS, Campus das Auroras, Universidade da Integração Internacional da Lusofonia Afro-Brasileira - UNILAB, Rua José Franco de Oliveira, s/n - Zona Rural, Redenção 62790-970, CE, Brazil.
Magnetic iron oxide nanoparticles immobilized lipase Eversa Transform 2.0 for efficient biodiesel production. The stable biocatalyst achieved high conversion rates and reusability, demonstrating its potential for sustainable ester synthesis.
Area of Science:
- Biocatalysis
- Nanotechnology
- Renewable Energy
Background:
- Biodiesel production relies on efficient esterification and transesterification processes.
- Lipase immobilization is key to developing stable and reusable biocatalysts.
- Magnetic nanoparticles offer advantages for enzyme recovery and process efficiency.
Purpose of the Study:
- To immobilize lipase Eversa Transform 2.0 (ET 2.0) onto magnetic iron oxide nanoparticles (Fe3O4).
- To evaluate the performance of the immobilized enzyme for ethyl oleate synthesis.
- To assess the stability and reusability of the biocatalyst for sustainable biodiesel production.
Main Methods:
- Magnetic nanoparticles synthesized via coprecipitation, activated with glutaraldehyde, and functionalized with APTES.
- Lipase ET 2.0 immobilization optimized for pH, buffer, enzyme load, and contact time.
- Esterification of oleic acid with ethanol using the immobilized biocatalyst, followed by kinetic and recirculation studies.
- Molecular docking to assess enzyme-substrate binding affinity.
Main Results:
- Optimal immobilization conditions yielded 78% yield and 205.9 U/g activity.
- Immobilized lipase demonstrated superior performance compared to the free enzyme.
- Achieved 88.1% conversion in ethyl oleate synthesis, with ~80% conversion maintained over four cycles.
- Molecular docking indicated a stable enzyme-substrate complex (-5.8 kcal/mol binding affinity).
Conclusions:
- Immobilized lipase ET 2.0 on Fe3O4 nanoparticles is an effective and stable biocatalyst.
- The developed biocatalyst is suitable for sustainable biodiesel production through efficient esterification.
- Magnetic support facilitates easy recovery and reuse, enhancing process economics.
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