Characterization of a New Cold-adapted Lipase from Pseudomonas sp. TK-3 |
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Authors: | Daisuke Tanaka Satoru Yoneda Yoko Yamashiro Akihiro Sakatoku Takuro Kayashima Kasumi Yamakawa Shogo Nakamura |
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Affiliation: | 1. Graduate School of Science and Engineering, University of Toyama, 3190 Gofuku, Toyama, 930-8555, Japan
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Abstract: | 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 ??.3 lipase and had a conserved GXSXG motif around the catalytic Ser residue. Its optimal temperature was 20?C25?°C, lower than in most other subfamily ??.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 Ca2+. 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. |
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