AhlX, an <i>N</i>-acylhomoserine Lactonase with Unique Properties
Pengfu Liu,
Yan Chen,
Zongze Shao,
Jianwei Chen,
Jiequn Wu,
Qian Guo,
Jiping Shi,
Hong Wang,
Xiaohe Chu
Affiliations
Pengfu Liu
Collaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, China
Yan Chen
Collaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, China
Zongze Shao
Key Laboratory of Marine Biogenetic Resources, The Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, China
Jianwei Chen
Collaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, China
Jiequn Wu
Collaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, China
Qian Guo
Collaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, China
Jiping Shi
Shanghai Advanced Research Institute, Chinese Academy of Sciences, Pudong, Shanghai 201210, China
Hong Wang
Collaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, China
Xiaohe Chu
Collaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, China
N-Acylhomoserine lactonase degrades the lactone ring of N-acylhomoserine lactones (AHLs) and has been widely suggested as a promising candidate for use in bacterial disease control. While a number of AHL lactonases have been characterized, none of them has been developed as a commercially available enzymatic product for in vitro AHL quenching due to their low stability. In this study, a highly stable AHL lactonase (AhlX) was identified and isolated from the marine bacterium Salinicola salaria MCCC1A01339. AhlX is encoded by a 768-bp gene and has a predicted molecular mass of 29 kDa. The enzyme retained approximately 97% activity after incubating at 25 °C for 12 days and ~100% activity after incubating at 60 °C for 2 h. Furthermore, AhlX exhibited a high salt tolerance, retaining approximately 60% of its activity observed in the presence of 25% NaCl. In addition, an AhlX powder made by an industrial spray-drying process attenuated Erwinia carotovora infection. These results suggest that AhlX has great potential for use as an in vitro preventive and therapeutic agent for bacterial diseases.
