| Autor: |
SEO, Myung-Ji, LEE, Beom-Seon, PYUN, Yu-Ryang, PARK, Hoon |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; September 2011, Vol. 75 Issue: 9 p1789-1795, 7p |
| Abstrakt: |
Geobacillus caldoxylosilyticusYS-8, which was isolated from volcanic soil in Indonesia, was found to degrade various N-acylhomoserine lactones (AHLs) with different lengths and acyl side-chain substitutions over a wide temperature range of 30–70 °C. The purified AHL-degrading enzyme showed a single band of 32 kDa, and its N-terminal amino acid sequence was determined to be ANVIKARPKLYVMDN, tentatively suggesting that the AHL-degrading enzyme was AHL lactonase. The AHL-degrading activity of the purified enzyme was maximized at pH 7.5 and 50 °C, and it retained about 50% of its activity even after a heat treatment at 60 °C for 3 h, exhibiting properties consistent with a thermostable enzyme. The mass spectrometric analysis demonstrated that the AHL-degrading enzyme catalyzed lactone ring opening of N-3-oxohexanoyl-L-homoserine lactone and N-hexanoyl-L-homoserine lactone by hydrolyzing the lactones and working as an AHL lactonase. |
| Databáze: |
Supplemental Index |
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