Identification and characterization of a novel functional acylhomoserine lactone-degrading enzyme for preventing bacterial infection
| Project/Area Number |
24760643
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biofunction/Bioprocess
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| Research Institution | Utsunomiya University |
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Principal Investigator |
MOROHOSHI Tomohiro 宇都宮大学, 工学(系)研究科(研究院), 准教授 (90361360)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | クオラムセンシング / アシル化ホモセリンラクトン / Thermaerobacter / ラクトナーゼ / 分解 / 好熱菌 / 耐熱性酵素 / 分解遺伝子 / 好熱性細菌 |
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| Outline of Final Research Achievements |
Thermaerobacter marianensis is an extremely thermophilic bacterium. N-Acylhomoserine lactone (AHL) is a quorum-sensing signal molecule used by many gram-negative bacteria. We found AHL-degrading gene homologue (designated aiiT) in the genome sequences of T. marianensis JCM 10246. AiiT has 59.7%, 21.2, and 11.2% identities with AhlS from Solibacillus silvestris, AiiA from Bacillus cereus, and AidC from Chryseobacterium sp., respectively. Purified AiiT, as a maltose-binding fusion protein, showed high AHL-degrading activity against all tested AHLs at the temperatures ranging from 40 to 80°C. AiiT displayed its maximal activity at high temperature range, 60 to 80°C, and showed higher thermostability than the other AHL lactonases.
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Report
(4 results)
Research Products
(10 results)
