A Preliminary Study of Cell Membrane Mediated Immobilization of a Recombinant Acyl-homoserine Lactonase AidH

The aim of this work was to inhibit biofilm formation by taking advantages of bacterial surface display technology in combination with cell membrane chromatography. A recombinant protein INP-AidH was constructed by fusing a quorum signal hydrolase AidH to the C-terminus of the ice nucleation protein (INP). Expression of INP-AidH was achieved on E. coli cell surface at an expression level of 30% of total membrane proteins. Activity of INP-AidH on cell membranes was confirmed in degrading the quorum signal C6-HSL as well as inhibiting bacterial biofilm. Immobilization of INP-AidH anchored cell membranes on silica gel particles was facilitated by taking advantages of cell membrane chromatography. The functionalized silica gel particles also exhibit activities in degrading C6-HSL and inhibiting bacterial biofilm. This article presents a new approach to prevent biofilm formation of silica-based materials.