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

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

<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...

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Main Authors: Pengfu Liu, Yan Chen, Zongze Shao, Jianwei Chen, Jiequn Wu, Qian Guo, Jiping Shi, Hong Wang, Xiaohe Chu
Format: Article
Language:English
Published: MDPI AG 2019-06-01
Series:Marine Drugs
Subjects:
quorum sensing
quorum-quenching
<i>N</i>-acylhomoserine lactonase
marine
thermostable
salt tolerance
Online Access:https://www.mdpi.com/1660-3397/17/7/387
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spelling doaj-ead7413a408a4c939c92a24f99e24fe82020-11-24T21:54:59ZengMDPI AGMarine Drugs1660-33972019-06-0117738710.3390/md17070387md17070387AhlX, an <i>N</i>-acylhomoserine Lactonase with Unique PropertiesPengfu Liu0Yan Chen1Zongze Shao2Jianwei Chen3Jiequn Wu4Qian Guo5Jiping Shi6Hong Wang7Xiaohe Chu8Collaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, ChinaCollaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, ChinaKey Laboratory of Marine Biogenetic Resources, The Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, ChinaCollaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, ChinaCollaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, ChinaCollaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, ChinaShanghai Advanced Research Institute, Chinese Academy of Sciences, Pudong, Shanghai 201210, ChinaCollaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, ChinaCollaborative Innovation Center of Yangtze River DeltaRegion Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, China<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 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 <i>Salinicola salaria</i> 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 &#176;C for 12 days and ~100% activity after incubating at 60 &#176;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 <i>Erwinia carotovora</i> infection. These results suggest that AhlX has great potential for use as an in vitro preventive and therapeutic agent for bacterial diseases.https://www.mdpi.com/1660-3397/17/7/387quorum sensingquorum-quenching<i>N</i>-acylhomoserine lactonasemarinethermostablesalt tolerance
collection DOAJ
language English
format Article
sources DOAJ
author Pengfu Liu
Yan Chen
Zongze Shao
Jianwei Chen
Jiequn Wu
Qian Guo
Jiping Shi
Hong Wang
Xiaohe Chu
spellingShingle Pengfu Liu
Yan Chen
Zongze Shao
Jianwei Chen
Jiequn Wu
Qian Guo
Jiping Shi
Hong Wang
Xiaohe Chu
AhlX, an <i>N</i>-acylhomoserine Lactonase with Unique Properties
Marine Drugs
quorum sensing
quorum-quenching
<i>N</i>-acylhomoserine lactonase
marine
thermostable
salt tolerance
author_facet Pengfu Liu
Yan Chen
Zongze Shao
Jianwei Chen
Jiequn Wu
Qian Guo
Jiping Shi
Hong Wang
Xiaohe Chu
author_sort Pengfu Liu
title AhlX, an <i>N</i>-acylhomoserine Lactonase with Unique Properties
title_short AhlX, an <i>N</i>-acylhomoserine Lactonase with Unique Properties
title_full AhlX, an <i>N</i>-acylhomoserine Lactonase with Unique Properties
title_fullStr AhlX, an <i>N</i>-acylhomoserine Lactonase with Unique Properties
title_full_unstemmed AhlX, an <i>N</i>-acylhomoserine Lactonase with Unique Properties
title_sort ahlx, an <i>n</i>-acylhomoserine lactonase with unique properties
publisher MDPI AG
series Marine Drugs
issn 1660-3397
publishDate 2019-06-01
description <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 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 <i>Salinicola salaria</i> 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 &#176;C for 12 days and ~100% activity after incubating at 60 &#176;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 <i>Erwinia carotovora</i> infection. These results suggest that AhlX has great potential for use as an in vitro preventive and therapeutic agent for bacterial diseases.
topic quorum sensing
quorum-quenching
<i>N</i>-acylhomoserine lactonase
marine
thermostable
salt tolerance
url https://www.mdpi.com/1660-3397/17/7/387
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