Abstract
In this study, porcine kidney acylase, as N-acyl homoserine lactones (AHLs)-degradation enzyme, was employed for the first time to directly investigate the role of AHLs in the structure stability of aerobic granules. Results clearly showed that inactivation of AHLs by AHLs-acylase could weaken the stability of aerobic granule. In the presence of AHLs-acylase, AHLs were degraded by hydrolyzing the amide linkage, which resulted in aerobic granular attachment potential and activity of AHLs-based quorum sensing significantly reduced. In addition, it was also found that inactivation of AHLs led to reduction of extracellular polysaccharides and protein (PN), especially PN, and induced extracellular polymeric substances matrix damaged, which was hostile to stability of aerobic granules. This study provided direct evidence that AHLs played a key role in improving aerobic granular stability, and a potential way to enhance long-term stability of aerobic granules.
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