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N -Acylated homoserine lactone (AHL) lactonases are capable of degrading signal molecules involved in bacterial quorum sensing and therefore represent a new approach to control bacterial infection. Here a gene responsible for the AHL lactonase activity ofBacillus sp. strain AI96, 753 bp in length, was cloned and then expressed inEscherichia coli . The deduced amino acid sequence ofBacillus sp. AI96 AiiA (AiiAAI96 ) is most similar to those of otherBacillus sp. AHL lactonases (∼80% sequence identity) and was consequently categorized as a member of the metallo-β-lactamase superfamily. AiiAAI96 maintains ∼100% of its activity at 10°C to 40°C at pH 8.0, and it is very stable at 70°C at pH 8.0 for at least 1 h; no otherBacillus AHL lactonase has been found to be stable under these conditions. AiiAAI96 resists digestion by proteases and carp intestinal juice, and it has broad-spectrum substrate specificity. The supplementation of AiiAAI96 into fish feed by oral administration significantly attenuatedAeromonas hydrophila infection in zebrafish. This is the first report of the oral administration of an AHL lactonase for the efficient control ofA. hydrophila .

applied and environmental microbiology

Orally Administered Thermostable <i>N</i> -Acyl Homoserine Lactonase from Bacillus sp. Strain AI96 Attenuates Aeromonas hydrophila Infection in Zebrafish

Orally Administered Thermostable N -Acyl Homoserine Lactonase from Bacillus sp. Strain AI96 Attenuates Aeromonas hydrophila Infection in Zebrafish