Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp.

ABSTRACT:

Background

N-acylhomoserine lactones (AHLs) are well-studied signalling molecules produced by some Gram-negative Proteobacteria for bacterial cell-to-cell communication or quorum sensing. We have previously demonstrated the degradation of AHLs by an Antarctic bacterium, Planococcus versutus L10.15^T, at low temperature through the production of an AHL lactonase. In this study, we cloned the AHL lactonase gene and characterized the purified novel enzyme.

Results

Rapid resolution liquid chromatography analysis indicated that purified AidP possesses high AHL-degrading activity on unsubstituted, and 3-oxo substituted homoserine lactones. Liquid chromatography-mass spectrometry analysis confirmed that AidP functions as an AHL lactonase that hydrolyzes the ester bond of

SUBMITTER: See-Too WS 

PROVIDER: S-EPMC6240239 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature