Development of Multilayer Magnetic Janus Sub-Micrometric Particles for Lipase Catalysis in Pickering Emulsion

This study presents a multilayer magnetic Janus sub-micrometric particle (MMJSP) as a nanoreactor for lipase catalysis. The core of the nanoparticle is constructed from a core-shell Fe<sub>3</sub>O<sub>4</sub>@SiO<sub>2</sub> framework, which serves as a precursor for the sequential amino and aldehyde modifications using 3-aminopropyltriethoxysilane and benzaldehyde. Following localized etching and subsequent modification with N,N-dimethyldodecylamine, a Janus nanoparticle with distinct hydrophilic and hydrophobic domains is synthesized. The resulting MMJSP demonstrates a stable attachment to the reaction interface and significantly enhances lipase performance, exhibiting 1.4-fold and 1.6-fold enhancements in activity after immobilization during 1 h hydrolysis and 24 h esterification reactions, respectively. Additionally, the storage stability of the immobilized lipase is improved by 100% over a period of 30 days. Reusability assessments reveal that the immobilized enzyme retains 80.7% activity after 10 cycles of esterification and 80.6% after 50 cycles of hydrolysis, with the magnetic properties allowing for rapid separation and recovery of the immobilized enzyme.

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Publication Details

Journal
Molecules
Published
2025-05-31
DOI
https://doi.org/10.3390/molecules30112429
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
Field-Weighted Citation Impact
0.00

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article

Development of Multilayer Magnetic Janus Sub-Micrometric Particles for Lipase Catalysis in Pickering Emulsion

Jie Luo, Wen‐Can Huang, Xiangyao Chen, Simiao Di et al.
Molecules
Enzyme Catalysis and Immobilization
article

Development of Multilayer Magnetic Janus Sub-Micrometric Particles for Lipase Catalysis in Pickering Emulsion

Jie Luo, Wen‐Can Huang, Xiangyao Chen, Simiao Di, Wei J. Wang
article en

Abstract

This study presents a multilayer magnetic Janus sub-micrometric particle (MMJSP) as a nanoreactor for lipase catalysis. The core of the nanoparticle is constructed from a core-shell Fe<sub>3</sub>O<sub>4</sub>@SiO<sub>2</sub> framework, which serves as a precursor for the sequential amino and aldehyde modifications using 3-aminopropyltriethoxysilane and benzaldehyde. Following localized etching and subsequent modification with N,N-dimethyldodecylamine, a Janus nanoparticle with distinct hydrophilic and hydrophobic domains is synthesized. The resulting MMJSP demonstrates a stable attachment to the reaction interface and significantly enhances lipase performance, exhibiting 1.4-fold and 1.6-fold enhancements in activity after immobilization during 1 h hydrolysis and 24 h esterification reactions, respectively. Additionally, the storage stability of the immobilized lipase is improved by 100% over a period of 30 days. Reusability assessments reveal that the immobilized enzyme retains 80.7% activity after 10 cycles of esterification and 80.6% after 50 cycles of hydrolysis, with the magnetic properties allowing for rapid separation and recovery of the immobilized enzyme.

MoleculesVol. 30(11)
China Light Industry Press (China) (CN), Marine Biology Institute of Shandong Province (CN), Ocean University of China (CN)
National Key Research and Development Program of China
Clean water and sanitation
Openalex Percentile: Top 89%
Enzyme Catalysis and Immobilization
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