Pickering stabilized peptide gel particles as tunable microenvironments for biocatalysis

Area of Science:

• Biomaterials Science
• Nanotechnology
• Biocatalysis

Background:

• Peptide self-assembly creates functional hydrogels with tunable properties.
• Stabilizing delicate biomolecules like proteins requires advanced encapsulation methods.
• Pickering emulsions offer surfactant-free stabilization, crucial for preserving protein activity.

Purpose of the Study:

• To prepare and characterize peptide gel microparticles stabilized by SiO2 nanoparticles.
• To evaluate the performance of immobilized enzymes within these novel microparticles.
• To explore the potential of these systems for protein stabilization and enhanced biocatalysis.

Main Methods:

• Coassembly of aromatic peptide amphiphiles (Fmoc-FF) with functionalized Fmoc-amino acids (S, D, K, Y).
• Emulsification and stabilization of peptide gels using SiO2 nanoparticles (Pickering emulsion).
• Immobilization and activity testing of lipase B enzyme in various Pickering/gel microparticle formulations via transesterification in heptane.

Main Results:

• Successful preparation of peptide gel microparticles stabilized by SiO2 nanoparticles.
• Pickering stabilization enhanced enzyme performance compared to conventional methods.
• Hydrophilic Fmoc-FF/S peptide gels demonstrated superior catalytic activity for immobilized lipase B.
• The gel matrix provided a protective, hydrated environment for the enzyme.

Conclusions:

• Pickering-stabilized peptide gel microparticles offer a robust and surfactant-free platform for enzyme immobilization.
• Tunable chemical environments within the peptide gels significantly improve enzyme activity and stability.
• This technology holds promise for applications in biocatalysis, biosensors, and bioinspired devices.