Bovine Serum Albumin-Trypsin Sponges for Enhanced Enzymatic Stability and Protein Digestion Efficiency.

ABSTRACT: Protein-based materials are emerging as versatile platforms for biocatalysis and biomedical applications due to their structural tunability and intrinsic catalytic capabilities. Here, we present a light-activated strategy for the scalable fabrication of enzymatically active sponges via covalent cross-linking of trypsin within a bovine serum albumin (BSA) matrix. This method leverages photoinitiated Tyr-Tyr coupling, creating a nanoscale enzyme distribution that addresses critical limitations observed in conventional enzyme immobilization methods─namely, instability, autolysis, and restricted reusability. By modulating trypsin concentration and acetic acid (AA) during synthesis, we achieve precise control over cross-link density, enhancing both mechanical flexibility and catalytic accessibi

SUBMITTER: Kaeek M 

PROVIDER: S-EPMC12541704 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature