RRC ID 40806
著者 Morohoshi T, Tominaga Y, Someya N, Ikeda T.
タイトル Characterization of a novel thermostable N-acylhomoserine lactonase from the thermophilic bacterium Thermaerobacter marianensis.
ジャーナル J Biosci Bioeng
Abstract 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.
巻・号 120(1)
ページ 1-5
公開日 2015-7-1
DOI 10.1016/j.jbiosc.2014.11.014
PII S1389-1723(14)00453-8
PMID 25529553
MeSH 4-Butyrolactone / analogs & derivatives* 4-Butyrolactone / chemistry 4-Butyrolactone / metabolism Bacillus / enzymology Bacillus / genetics Bacillus cereus Bacteria, Aerobic / enzymology* Bacteria, Aerobic / genetics Carboxylic Ester Hydrolases / metabolism* Enzyme Stability Homoserine / analogs & derivatives Homoserine / metabolism Hydrolysis Lactones / metabolism Planococcaceae / enzymology Planococcaceae / genetics Quorum Sensing Substrate Specificity Temperature*
IF 2.366
引用数 13
WOS 分野 FOOD SCIENCE & TECHNOLOGY BIOTECHNOLOGY & APPLIED MICROBIOLOGY
リソース情報
一般微生物 JCM 10246 JCM 11223 JCM 15650