We explored practical applications of PFK amyloid-mediated β-lactam hydrolysis, specifically as a vehicle for antibiotic removal in water (Figure ). In the experiments, we coupled PFK fibrils to commercially available silica beads in a column-filter setup and evaluated the degradation capabilities for water containing dissolved β-lactam antibiotics. Figure illustrates the experimental scheme. To conjugate the PFK amyloid fibrils with the silica beads, we functionalized PFK with levodopa (L-DOPA) via binding to the amine sidechain of Lys-12 (the peptide is denoted PFKDOPA). The catechol ligand of L-DOPA can be anchored onto the silica beads' surface through bidentate coordinative bonds . Importantly, bare PFKDOPA fibrils (not coupled to silica beads) readily formed fibrils which also catalyzed β-lactam hydrolysis (Figure ). The representative scanning electron microscopy (SEM) image of the PFKDOPA/bead in Figure , inset, confirms that bound PFKDOPA fibrils are abundantly displayed on the silica bead surface. The adsorption curve in Figure , calculated through the measurement of the UV-vis absorbance of PFKDOPA in the supernatant, further shows the effective attachment of PFKDOPA fibrils, with saturation of the beads' surface occurring at peptide concentrations higher than 3 mM. Brunauer-Emmett-Teller (BET) analysis indicates a significant increase in the surface area of the PFKDOPA-coated beads, compared to the bare counterparts (Figure ). Following flushing the column with distilled water, most of the embedded nitrocefin was removed (the residual reddish appearance in Figure ,iv indicates bound hydrolyzed nitrocefin).