Unknown

Dataset Information

0

AhlX, an N-acylhomoserine Lactonase with Unique Properties.


ABSTRACT: 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.

SUBMITTER: Liu P 

PROVIDER: S-EPMC6669651 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

AhlX, an <i>N</i>-acylhomoserine Lactonase with Unique Properties.

Liu Pengfu P   Chen Yan Y   Shao Zongze Z   Chen Jianwei J   Wu Jiequn J   Guo Qian Q   Shi Jiping J   Wang Hong H   Chu Xiaohe X  

Marine drugs 20190628 7


<i>N</i>-Acylhomoserine lactonase degrades the lactone ring of <i>N</i>-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 <i>in vitro</i> AHL quenching due to their low stability. In this study, a highly stable AHL lactonase (AhlX) was identified and isolated from the marine bacterium  ...[more]

Similar Datasets

| S-EPMC6213412 | biostudies-literature
| S-EPMC6240239 | biostudies-literature
| S-EPMC6881798 | biostudies-literature
| S-EPMC2849219 | biostudies-literature
| S-EPMC7459623 | biostudies-literature
| S-EPMC9327166 | biostudies-literature
| S-EPMC4036043 | biostudies-literature
| S-EPMC2916461 | biostudies-literature
| S-EPMC3485932 | biostudies-literature
| S-EPMC5641347 | biostudies-literature