Molecular Cloning, Purification, and Characterization of a Cold-Adapted Esterase from Photobacterium sp. MA1-3 |
Kim, Young-Ok
(Biotechnology Research Division, National Fisheries Research and Development Institute)
Heo, Yu Li (Biotechnology Research Division, National Fisheries Research and Development Institute) Nam, Bo-Hye (Biotechnology Research Division, National Fisheries Research and Development Institute) Kim, Dong-Gyun (Biotechnology Research Division, National Fisheries Research and Development Institute) Jee, Young-Ju (Biotechnology Research Division, National Fisheries Research and Development Institute) Lee, Sang-Jun (Biotechnology Research Division, National Fisheries Research and Development Institute) An, Cheul-Min (Biotechnology Research Division, National Fisheries Research and Development Institute) |
1 | Bornscheuer UT. 2002. Microbial carboxylesterases: classification, properties and applications in biocatalysis. FEMS Microbiol Rev 26, 73-81. http://dx.doi.org/10.1016/S0168-6445(01)00075-4. DOI ScienceOn |
2 | Choo DW, Kurihara T, Suzuki T, Soda K, and Esaki N. 1998. A coldadapted lipase of an alaskan psychrotroph, Pseudomonas sp. strain B11-1: gene cloning and enzyme purification and characterization. Appl Environ Microbiol 64, 486-491. |
3 | Feller G, Thiry M, and Gerday C. 1991. Nucleotide sequence of the lipase gene Lip2 from the antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues. DNA Cell Biol 10, 381-388. DOI ScienceOn |
4 | Feller G, Narinx E, Arpigny JL, Aittaleb M, Baise E, Geniot S and Gerday C. 1996. Enzymes from psychrophilic organisms. FEMS Microbiol Rev 18, 189-202. http://dx.doi.org/10.1016/0168-6445(96)00011-3. DOI ScienceOn |
5 | Grochulski P, Li Y, Schrag JD, Bouthillier F, Smith P, Harrison D, Rubin B and Cygler M. 1993. Insights into interfacial activation from an open structure of Candida rugosa lipase. J Biol Chem 268, 12843-12847. |
6 | Harwood J. 1989. The versatility of lipases for industrial uses. Trends Biochem Sci 14, 125-126. http://dx.doi.org/10.1016/0968-0004(89)90140-0. DOI ScienceOn |
7 | Hasan F, Shah AA and Hameed A. 2006. Industrial applications of microbial lipases. Enzyme Microb Technol 39, 235-251. http://dx.doi.org/10.1016/j.enzmictec.2005.10.016. DOI ScienceOn |
8 | Jaeger KE and Reetz MT. 1998. Microbial lipases from versatile tools for biotechnology, Trends Biotechnol 16, 396-403. http://dx.doi.org/10.1016/S0167-7799(98)01195-0. DOI ScienceOn |
9 | Jaeger KE, Ransac S, Koch HB, Ferrato F and Dijkstra BW. 1993. Topological characterization and modeling of the 3D structure of lipase from Pseudomonas aeruginosa. FEBS Lett 332, 143-149. http://dx.doi.org/10.1016/0014-5793(93)80501-K. DOI ScienceOn |
10 | Jaeger KE, Dijkstra BW and Reetz MT. 1999. Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu Rev Microbiol 53, 315-351. http://dx.doi.org/10.1146/annurev.micro.53.1.315. DOI ScienceOn |
11 | Kim HE and Park KR. 2002. Purification and characterization of an esterase from Acinetobacter lwoffii 16C-1. Curr Microbiol 44, 401-405. http://dx.doi.org/10.1007/s00284-001-0008-6. DOI ScienceOn |
12 | Kim YO, Park IS, Kim HK, Nam BH, Kong HJ, Kim WJ, Kim DG, Kim KK and Lee SJ. 2011. A novel cold-adapted esterase from Salinisphaera sp. P7-4: gene cloning, overexpression, and characterization. J Gen Appl Microbiol 57, 357-364. DOI ScienceOn |
13 | Kim YO, Khosasih V, Nam BH, Lee SJ, Suwanto A, Kim HK. 2012. Gene cloning and catalytic characterization of cold-adapted lipase of Photobacterium sp. MA1-3 isolated from blood clam. J Biosci Bioeng 114, 589-595. DOI ScienceOn |
14 | Kim YO, Park IS, Kim HK, Nam BH, Kong HJ, Kim WJ, Kim DG, Kim BS, Jee YJ, Song JH and Lee SJ. 2013. Shewanella sp. Ke75 esterase with specificity for p-nitrophenyl butyrate: gene cloning and characterization. 56, 55-62. http://dx.doi.org/10.1007/s13765- 012-2089-2. 과학기술학회마을 DOI |
15 | Knothe G. 2005. Dependence of biodiesel fuel properties on the structure of fatty acid alkyl esters. Fuel Process Technol 86, 1059-1070. http://dx.doi.org/10.1016/j.fuproc.2004.11.002. DOI ScienceOn |
16 | Margesin R. 2007. Alpine microorganisms: useful tools for low-temperature bioremediation. J Microbiol 45, 281-285. |
17 |
Kulakova L, Galkin A, Nakayama T. Nishino T and Esaki N. 2004. Cold-active esterase form Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly |
18 | Lee HK, Ahn MJ, Kwak SH, Song WH and Jeong BC. 2003. Purification and characterization of cold active lipase from psychrotrophic Aeromonas sp. LPB4. J Microbiol 41, 22-27. |
19 | Long C. 1971. Biochemists Handbook. Redwood, London, GB, pp 273-274. |
20 | Martinez C, Nicolas A, van Tilbeurgh H, Egloff MP, Cudrey C, Verger R and Cambillau C. 1994. Cutinase, a lipolytic enzyme with a preformed oxyanion hole. Biochemistry 33, 83-89. http://dx.doi.org/10.1021/bi00167a011. DOI ScienceOn |
21 | Pleiss J, Fischer M and Schmid RD. 1998. Anatomy of lipase binding sites: the scissile fatty acid binding site. Chem Phys Lipids 93, 67-80. http://dx.doi.org/10.1016/S0009-3084(98)00030-9. DOI ScienceOn |
22 | Ryu HS, Kim HK, Choi WC, Kim MH, Park SY, Han NS, Oh TK and Lee JK. 2006. New cold-adapted lipase from Photobacterium lipolyticum sp. nov. that is closely related to filamentous fungal lipases. Appl Microbiol Biotechnol 70, 321-326. http://dx.doi.org/10.1007/s00253-005-0058-y. DOI ScienceOn |
23 | Schmid RD and Verger R. 1998. Lipases; interfacial enzymes with attractive applications. Angew Chem Int Ed 37, 1608-1633. http://dx.doi.org/10.1002/(SICI)1521-3773(19980703)37:12<1608::AIDANIE1608>3.3.CO;2-M. DOI ScienceOn |
24 | Suzuki, T, Nakayama T, Choo DW, Hirano Y, Kurihara T, Nishino T and Esaki N. 2003. Cloning, heterologous expression, renaturation, and characterization of a cold-adapted esterase with unique primary structure from a psychrotroph Pseudomonas sp. strain B11-1. Protein Expr Purif 30, 171-178. http://dx.doi.org/10.1016/S1046- 5928(03)00128-1. DOI ScienceOn |
25 | Suzuki T, Nakayama T, Kurihara T, Nishino T and Esaki N. 2001. Coldactive lipolytic activity of psychrotrophic Acinetobacter sp. strain no. 6. J Biosci Bioeng 92, 144-148. http://dx.doi.org/10.1263/jbb.92.144. DOI ScienceOn |
26 | Suzuki T, Nakayama T, Kurihara T, Nishino T, and Esaki N. 2002a. A cold-active esterase with a substrate preference for vinyl esters from a psychrotroph, Acinetobacter sp. strain no. 6: gene cloning, purification, and characterization. J Mol Catal B Enzym 16, 255-263. http://dx.doi.org/10.1016/S1381-1177(01)00070-4. DOI ScienceOn |
27 | Suzuki T, Nakayama T, Kurihara T, Nishino T and Esaki N. 2002b. Primary structure and catalytic properties of a cold-active esterase from a psychrotroph, Acinetobacter sp. strain no. 6 isolated from Siberian soil. Biosci Biotechnol Biochem 66, 1682-1690. http://dx.doi.org/10.1271/bbb.66.1682. DOI ScienceOn |
28 | Thompson JD, Higgins DG and Gibson TJ. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res 22, 4673-4680. http://dx.doi.org/10.1093/nar/22.22.4673. DOI ScienceOn |
29 | Villeneuve P, Muderhwa JM, Graille J and Haas MJ. 2000. Customizing lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches. J. Mol. Catal B: Enzym 9, 113-148. http://dx.doi.org/10.1016/S1381-1177(99)00107-1. DOI ScienceOn |
30 | Wei P, Bai L, Song W and Hao G. 2009. Characterization of two soil metagenome-derived lipases with high specificity for p-nitrophenyl palmitate. Arch Microbiol 191, 233-240. http://dx.doi.org/10.1007/s00203-008-0448-5. DOI |
![]() |