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

Content Provider	Springer Nature Link
Author	Tanaka, Daisuke Yoneda, Satoru Yamashiro, Yoko Sakatoku, Akihiro Kayashima, Takuro Yamakawa, Kasumi Nakamura, Shogo
Copyright Year	2012
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 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.
Starting Page	327
Ending Page	338
Page Count	12
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	168
Issue Number	2
e-ISSN	15590291
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-06-30
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Pseudomonas sp. Cold-adapted lipase Characterization Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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