POS4-1252
Tunable Pore Architectures in PEGDA Microparticles via Photopolymerization-Induced Phase Separation for Enhanced Biocatalytic Efficiency
Topic
S4. Colloids, Interfaces, and Molecular Assemblies for Functional Soft Materials
When and Where
Oct 1, 2026
08:30 - 09:30
Room 301 (Grand Ballroom)
Session Chairs
Jinkee HONG
Ki Su KIM
Presenter(s)
AN SEUNG HUI (CHONNAM NATIONAL UNIVERS)
Co-Author(s)
Abstract
Designing advanced support materials with high surface area and optimized mass transfer is crucial for high-performance biocatalytic systems. In this study, we developed tunable porous poly(ethylene glycol) diacrylate (PEGDA) microparticles via photopolymerization-induced phase separation (PIPS) for enhanced enzyme immobilization. The porous architecture was precisely engineered by modulating the initial ratio of PEGDA to a sacrificial porogen in the pre-polymer mixture. Under UV irradiation, the rapid crosslinking of PEGDA triggered a controlled phase separation, creating porogen-rich domains within the polymer matrix. Subsequent removal of the sacrificial porogen resulted in a highly interconnected and tunable pore network. Systematic characterization using scanning electron microscopy (SEM) and BET analysis confirmed that the pore size and morphology could be finely adjusted by varying the porogen concentration and irradiation conditions. The resulting porous PEGDA particles were utilized as a scaffold for enzyme immobilization, and their catalytic performance was evaluated in comparison with free enzymes. While free enzymes often suffer from poor stability and lack of recyclability, the immobilized enzymes on porous PEGDA scaffolds exhibited significantly enhanced thermal and pH stability, along with excellent reusability over multiple cycles. The porous framework effectively minimized diffusion limitations, allowing the immobilized enzymes to maintain high catalytic efficiency comparable to their free form while providing the robust protection of the matrix. This PIPS-based strategy offers a versatile and scalable platform for developing high-performance enzyme reactors with tailored structural properties.
