Characterization of a novel thermostable N-acylhomoserine lactonase from the thermophilic bacterium Thermaerobacter marianensis

Thermaerobacter marianensis is an extremely thermophilic bacterium, which was isolated from the Mariana Trench, with an optimal growth temperature of approximately 75°C. N-Acylhomoserine lactone (AHL) is a quorum-sensing signal molecule used by many gram-negative bacteria. Here, we report the identi...

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Bibliographic Details
Published in:Journal of bioscience and bioengineering 2015-07, Vol.120 (1), p.1-5
Main Authors: Morohoshi, Tomohiro, Tominaga, Yoshiaki, Someya, Nobutaka, Ikeda, Tsukasa
Format: Article
Language:English
Subjects:
4-Butyrolactone - analogs & derivatives
4-Butyrolactone - chemistry
4-Butyrolactone - metabolism
Acylhomoserine lactone
Bacillus - enzymology
Bacillus - genetics
Bacillus cereus
Bacteria, Aerobic - enzymology
Bacteria, Aerobic - genetics
Carboxylic Ester Hydrolases - metabolism
Enzyme Stability
Homoserine - analogs & derivatives
Homoserine - metabolism
Hydrolysis
Lactonase
Lactones - metabolism
Planococcaceae - enzymology
Planococcaceae - genetics
Quorum Sensing
Substrate Specificity
Temperature
Thermaerobacter
Thermostable enzyme
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Summary:Thermaerobacter marianensis is an extremely thermophilic bacterium, which was isolated from the Mariana Trench, with an optimal growth temperature of approximately 75°C. N-Acylhomoserine lactone (AHL) is a quorum-sensing signal molecule used by many gram-negative bacteria. Here, we report the identification of an AHL-degrading gene homolog (designated aiiT) in the genome of T. marianensis JCM 10246. AiiT has 59.7%, 21.2%, and 11.2% identity to AhlS from Solibacillus silvestris, AiiA from Bacillus cereus, and AidC from Chryseobacterium sp., respectively. Homologs of aiiT were also found in Thermaerobacter nagasakiensis, T. composti, and T. subterraneus. A purified AiiT-maltose binding fusion showed high AHL-degrading activity against N-hexanoyl-l-homoserine lactone, N-octanoyl-l-homoserine lactone, and N-decanoyl-l-homoserine lactone at temperatures ranging from 40 to 80°C. HPLC analysis revealed that AiiT functions as an AHL-lactonase that catalyzes AHL ring opening by hydrolyzing lactones. AiiT displayed maximal activity at high temperatures (60–80°C) and showed higher thermostability than other AHL lactonases.
ISSN:1389-1723
1347-4421
DOI:10.1016/j.jbiosc.2014.11.014