Enhanced Immobilization of Glutaraldehyde Cross-Linked Lipase via Microfluidic Polymerization and Structured Porosity Optimization for Biocatalysis
**Abstract:** This research introduces a novel approach to enzyme immobilization leveraging microfluidic polymerization for precisely controlled, spatially-structured lipase matrices. Combining glutaraldehyde cross-linking with optimized polymer porosity generated through controlled flow rates and monomer ratios, we achieve significantly enhanced enzyme loading, stability, and catalytic activity compared to conventional methods. Our system allows for fine-tuning of matrix architecture to maximize mass transfer and minimize diffusional limitations, leading to a 10-40% improvement in reaction rates and a 2-3x increase in operational stability across multiple biocatalytic applications. This enhanced performance opens avenues for cost-effective and efficient industrial biocatalysis processes.
Institutions
- Freed–Hardeman University (US)
Publication Details
- Journal
- Zenodo (CERN European Organization for Nuclear Research)
- Published
- 2025-10-02
- DOI
- https://doi.org/10.5281/zenodo.17247086
- Primary Topic
- Fluorine in Organic Chemistry
- Type
- article
- Field-Weighted Citation Impact
- 0.00