Abstract
Magnetic immobilization of quorum sensing (QS) signal hydrolases provides a convenient solution for quenching QS process that is essential for bacterial biofilm formation and antimicrobial resistance. In the present study, a QS signal hydrolase, AiiA, was fused with a magnetic protein, MagR, and expressed in Escherichia coli. Magnetic immobilization of AiiA was achieved on Fe(3) O(4) -SiO(2) iron beads and was confirmed via SDS-PAGE, zeta potential measurement, FTIR spectrometry, and SEM analysis. The magnetic immobilized AiiA exhibited activity in degrading the quorum sensing signal, C6-HSL. This study opens a new avenue to actively immobilize enzymes via magnetic interaction and quench quorum sensing.