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The pathogen  Pseudomonas aeruginosa  uses quorum sensing (QS) to control virulence and biofilm formation. Enzymatic disruption of quorum sensing is a promising anti-infection therapeutic strategy that does not rely on antibiotics. Here, a novel gene ( aii810 ) encoding an  N -acylhomoserine lactonase was isolated from the Mao-tofu metagenome for the first time. Aii810 encoded a protein of 269 amino acids and was expressed in  Escherichia coli  BL21 (DE3) in soluble form. It showed the highest activity at 20°C, and it maintained 76.5% of activity at 0°C and more than 50% activity at 0–40°C. The optimal pH was 8.0. It was stable in both neutral and slightly alkaline conditions and at temperatures below 40°C. The enzyme hydrolyzed several ρ-nitrophenyl esters, but its best substrate was ρ-nitrophenyl acetate. Its  k  cat  and  K m values were 347.7 S -1  and 205.1 μM, respectively. It efficiently degraded  N -butyryl -L- homoserine lactone and  N -(3-oxododecanoyl)- L -homoserine lactone, exceeding hydrolysis rates of 72.3 and 100%, respectively. Moreover, Aii810 strongly attenuated  P. aeruginosa  virulence and biofilm formation. This enzyme with high anti-QS activity was the most cold-adapted  N -acylhomoserine lactonase reported, which makes it an attractive enzyme for use as a therapeutic agent against  P. aeruginosa  infection.

frontiers in microbiology

Aii810, a Novel Cold-Adapted N-Acylhomoserine Lactonase Discovered in a Metagenome, Can Strongly Attenuate Pseudomonas aeruginosa Virulence Factors and Biofilm Formation