Isolation and Characterization of N-Acylhomoserine Lactonase from the Thermophilic Bacterium, Geobacillus caldoxylosilyticus YS-8

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概要

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• Geobacillus caldoxylosilyticus YS-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.

著者

• PARK Hoon

  Department of Atmospheric Sciences, Global Environmental Laboratory, Yonsei University

• PYUN YU-RYANG

  Department of Biotechnology & Bioproducts Research Center, Yonsei University

• SEO Myung-Ji

  Department of Biotechnology, Yonsei University

• LEE Beom-Seon

  Department of Biotechnology, Yonsei University

• Park Hoon

  Department Of Atmospheric Sciences Global Environmental Laboratory Yonsei University

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• Isolation and Characterization of N-Acylhomoserine Lactonase from the Thermophilic Bacterium, Geobacillus caldoxylosilyticus YS-8
• Isolation and Characterization of N-Acylhomoserine Lactonase from the Thermophilic Bacterium, Geobacillus caldoxylosilyticus YS-8

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