Characterization of a New Cold-adapted Lipase from Pseudomonas sp. TK-3

A psychrotrophic Pseudomonas sp. TK-3 was isolated from dirty and cool stream water in Toyama, Japan from which we cloned and characterized the bacterial lipase LipTK-3. The sequenced DNA fragment contains an open reading frame of 1,428 bp that encoded a protein of 476 amino acids with an estimated...

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Veröffentlicht in:Applied biochemistry and biotechnology 2012-09, Vol.168 (2), p.327-338
Hauptverfasser: Tanaka, Daisuke, Yoneda, Satoru, Yamashiro, Yoko, Sakatoku, Akihiro, Kayashima, Takuro, Yamakawa, Kasumi, Nakamura, Shogo
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Sprache:eng
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Zusammenfassung:A psychrotrophic Pseudomonas sp. TK-3 was isolated from dirty and cool stream water in Toyama, Japan from which we cloned and characterized the bacterial lipase LipTK-3. The sequenced DNA fragment contains an open reading frame of 1,428 bp that encoded a protein of 476 amino acids with an estimated molecular mass of 50,132 Da. The lipase showed high sequence similarity to those of subfamily Ι.3 lipase and had a conserved GXSXG motif around the catalytic Ser residue. Its optimal temperature was 20–25 °C, lower than in most other subfamily Ι.3 lipases. The lipase exhibited about 30 % of maximal activity at 5 °C. The optimal pH value was 8.0. The activity was strongly inhibited by EDTA and was highly dependent on Ca 2+ . Tricaprylin and p -nitrophenyl caprylate were the most favorable substrates among the triglycerides and p -nitrophenyl esters, respectively. LipTK-3 also showed high activity towards natural substrates including edible vegetable oils and animal fats. Furthermore, LipTK-3 was very active and stable in the presence of several detergents, metal ions, and organic solvents. This cold-adapted lipase may prove useful for future applications.
ISSN:0273-2289
1559-0291
DOI:10.1007/s12010-012-9776-7