Characterization of an alkaline lipase from Proteus vulgaris K80 and the DNA sequence of the encoding gene

Authors

  • Hyung-Kwoun Kim,

    1. Applied Microbiology Research Group, Korea Research Institute of Bioscience and Biotechnology P.O. Box 115, Yusung, Taejon 305-600, South Korea
    2. Department of Biological Science, Korea Advanced Institute of Science and Technology Kusung-Dong, Yusung, Taejon 305-701, South Korea
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  • Jung-Kee Lee,

    1. Applied Microbiology Research Group, Korea Research Institute of Bioscience and Biotechnology P.O. Box 115, Yusung, Taejon 305-600, South Korea
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  • Hyoungman Kim,

    1. Department of Biological Science, Korea Advanced Institute of Science and Technology Kusung-Dong, Yusung, Taejon 305-701, South Korea
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  • Tae-Kwang Oh

    Corresponding author
    1. Applied Microbiology Research Group, Korea Research Institute of Bioscience and Biotechnology P.O. Box 115, Yusung, Taejon 305-600, South Korea
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*Corresponding author. Tel.; +82 (42) 860 4370; Fax: +82 (42) 860 4595; E-mail: jkl4050@geri4680.geri.re.kr

Abstract

Abstract A facultatively anaerobic bacterium producing an extracellular alkaline lipase was isolated from the soil collected near a sewage disposal plant in Korea and identified to be a strain of Proteus vulgaris. The molecular mass of the purified lipase K80 was estimated to be 31 kDa by SDS-PAGE. It was found to be an alkaline enzyme having maximum hydrolytid activity at pH 10, while fairly stable in a wide pH range from 5 to 11. The gene for lipase K80 was cloned in Escherichia coli. Sequence analysis showed an open reading frame of 861 bp coding for a polypeptide of 287 amino acid residues. The deduced amino acid sequence of the lipase gene had 46.3% identity to the lipase from Pseudomonas fragi.

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