메뉴 건너뛰기




Volumn 16, Issue 10, 2009, Pages 1172-1180

Cold-adapted esterases and lipases: From fundamentals to Application

Author keywords

hydrolase; Pseudoalteromonas haloplanktis tac125; Psychrophilic bacterial strain

Indexed keywords

BACTERIAL PROTEIN; ESTERASE; TRIACYLGLYCEROL LIPASE;

EID: 69549097399     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609789071270     Document Type: Article
Times cited : (52)

References (53)
  • 2
    • 33749074755 scopus 로고    scopus 로고
    • Bacterial incorporation of leucine into protein down to -20 degrees C with evidence for potential activity in sub-eutectic saline ice formations
    • Junge, K.; Eicken, H.; Swanson, B.D.; Deming, J.W. Bacterial incorporation of leucine into protein down to -20 degrees C with evidence for potential activity in sub-eutectic saline ice formations. Cryobiology, 2006, 52(3), 417-429.
    • (2006) Cryobiology , vol.52 , Issue.3 , pp. 417-429
    • Junge, K.1    Eicken, H.2    Swanson, B.D.3    Deming, J.W.4
  • 3
    • 0033619225 scopus 로고    scopus 로고
    • Evolution of an antifreeze glycoprotein
    • Cheng, C.-H. C.; Chen, L. Evolution of an antifreeze glycoprotein. Nature 1999, 40(6752), 443-444.
    • (1999) Nature , vol.40 , Issue.6752 , pp. 443-444
    • Cheng, C.-H.C.1    Chen, L.2
  • 4
    • 34447503551 scopus 로고    scopus 로고
    • An ice-binding protein from an Antarctic sea ice bacterium
    • Raymond, J.A.; Fritsen, C.; Shen, K. An ice-binding protein from an Antarctic sea ice bacterium. FEMS Microbiol. Ecol., 2007, 61(2), 214-221.
    • (2007) FEMS Microbiol. Ecol. , vol.61 , Issue.2 , pp. 214-221
    • Raymond, J.A.1    Fritsen, C.2    Shen, K.3
  • 5
    • 6944228892 scopus 로고    scopus 로고
    • Production of two types of ice crystal-controlling proteins in Antarctic bacterium
    • Kawahara, H.; Nakano, Y.; Omiya, K.; Muryoi, N.; Nishikawa, J.; Obata, H. Production of two types of ice crystal-controlling proteins in Antarctic bacterium. J. Biosci. Bioeng., 2004, 98(3), 220-223.
    • (2004) J. Biosci. Bioeng. , vol.98 , Issue.3 , pp. 220-223
    • Kawahara, H.1    Nakano, Y.2    Omiya, K.3    Muryoi, N.4    Nishikawa, J.5    Obata, H.6
  • 6
    • 33645498972 scopus 로고    scopus 로고
    • Psychrophilic microorganisms: Challenges for life
    • D'Amico, S.; Collins, T.; Marx, J.C.; Feller, G.; Gerday C. Psychrophilic microorganisms: challenges for life. EMBO Rep., 2006, 7(4), 385-389.
    • (2006) EMBO Rep. , vol.7 , Issue.4 , pp. 385-389
    • D'Amico, S.1    Collins, T.2    Marx, J.C.3    Feller, G.4    Gerday, C.5
  • 9
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • Jaeger, K-E.; Reetz MT. Microbial lipases form versatile tools for biotechnology. Trends Biotech., 1998, 16(9), 396-403.
    • (1998) Trends Biotech. , vol.16 , Issue.9 , pp. 396-403
    • Jaeger, K.-E.1    Reetz, M.T.2
  • 10
    • 33749240934 scopus 로고    scopus 로고
    • Purification and characterization of an alkaline lipase from Pseudomonas aeruginosa isolated from putrid mineral cutting oil as component of metalworking fluid
    • Karadzic, I.; Masui, A.; Zivkovic, L.I.; Fujiwara, N. Purification and characterization of an alkaline lipase from Pseudomonas aeruginosa isolated from putrid mineral cutting oil as component of metalworking fluid. J. Biosci. Bioeng., 2006, 102(2), 82-89.
    • (2006) J. Biosci. Bioeng. , vol.102 , Issue.2 , pp. 82-89
    • Karadzic, I.1    Masui, A.2    Zivkovic, L.I.3    Fujiwara, N.4
  • 12
    • 0028773288 scopus 로고
    • The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
    • Erratum in: Structure, 1994, 15(5), 453-454.
    • Uppenberg, J.; Hansen, M.T.; Patkar, S.; Jones, T.A. The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure, 1994, 15(4), 293-308. Erratum in: Structure, 1994, 15(5), 453-454.
    • (1994) Structure , vol.15 , Issue.4 , pp. 293-308
    • Uppenberg, J.1    Hansen, M.T.2    Patkar, S.3    Jones, T.A.4
  • 13
    • 0028279834 scopus 로고
    • Evidence for a pancreatic lipase subfamily with new kinetic properties
    • Thirstrup, K.; Verger, R.; Carriére, F. Evidence for a pancreatic lipase subfamily with new kinetic properties. Biochemistry, 1994, 15(10), 2748-2756.
    • (1994) Biochemistry , vol.15 , Issue.10 , pp. 2748-2756
    • Thirstrup, K.1    Verger, R.2    Carriére, F.3
  • 14
    • 35748968219 scopus 로고    scopus 로고
    • A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens
    • Meier, R.; Drepper, T.; Svensson, V.; Jaeger, K.E.; Baumann U. A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens. J. Biol. Chem., 2007, 282(43), 31477-31483.
    • (2007) J. Biol. Chem. , vol.282 , Issue.43 , pp. 31477-31483
    • Meier, R.1    Drepper, T.2    Svensson, V.3    Jaeger, K.E.4    Baumann, U.5
  • 15
    • 0025773328 scopus 로고
    • Cloning and expression in Escherichia coli of three lipase-encoding genes from the psychrotrophic antarctic strain Moraxella TA144
    • Feller, G.; Thiry, M.; Arpigny, JL; Gerday, C. Cloning and expression in Escherichia coli of three lipase-encoding genes from the psychrotrophic antarctic strain Moraxella TA144. Gene, 1991, 102(1),111-115.
    • (1991) Gene , vol.102 , Issue.1 , pp. 111-115
    • Feller, G.1    Thiry, M.2    Arpigny, J.L.3    Gerday, C.4
  • 16
    • 0027476253 scopus 로고
    • Cloning, sequence and structural features of a lipase from the antarctic facultative psychrophile Psychrobacter immobilis B10
    • Erratum in: Biochim. Biophys. Acta, 1995, 1263(1), 103.
    • Arpigny, JL.; Feller, G.; Gerday C. Cloning, sequence and structural features of a lipase from the antarctic facultative psychrophile Psychrobacter immobilis B10. Biochim. Biophys. Acta, 1993, 171(3), 331-333. Erratum in: Biochim. Biophys. Acta, 1995, 1263(1), 103.
    • (1993) Biochim. Biophys. Acta , vol.171 , Issue.3 , pp. 331-333
    • Arpigny, J.L.1    Feller, G.2    Gerday, C.3
  • 18
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: Classification and properties
    • Arpigny, J.L.; Jaeger, K.E. Bacterial lipolytic enzymes: classification and properties. Biochem. J., 1999, 343(1), 177-183.
    • (1999) Biochem. J. , vol.343 , Issue.1 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 19
    • 5644247368 scopus 로고    scopus 로고
    • Protein engineering and applications of Candida rugosa lipase isoforms
    • Akoh, C.C.; Lee, G.C.; Shaw JF. Protein engineering and applications of Candida rugosa lipase isoforms. Lipids, 2004, 39(6), 513-526.
    • (2004) Lipids , vol.39 , Issue.6 , pp. 513-526
    • Akoh, C.C.1    Lee, G.C.2    Shaw, J.F.3
  • 20
    • 0041568635 scopus 로고    scopus 로고
    • Cloning, heterologous expression, renaturation, and characterization of a cold-adapted esterase with unique primary structure from a psychrotroph Pseudomonas sp. strain B11-1
    • Suzuki, T.; Nakayama, T.; Choo, D.W.; Hirano, Y.; Kurihara, T.; Nishino, T.; Esaki N. 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., 2003, 30(2), 171-178.
    • (2003) Protein Expr. Purif. , vol.30 , Issue.2 , pp. 171-178
    • Suzuki, T.1    Nakayama, T.2    Choo, D.W.3    Hirano, Y.4    Kurihara, T.5    Nishino, T.6    Esaki, N.7
  • 21
    • 1242284208 scopus 로고    scopus 로고
    • Cold-active esterase from Psychrobacter sp. Ant300: Gene cloning, characterization, and the effects of Gly-->Pro substitution near the active site on its catalytic activity and stability
    • Kulakova, L.; Galkin, A.; Nakayama, T.; Nishino, T.; Esaki, N. Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly-->Pro substitution near the active site on its catalytic activity and stability. Biochim. Biophys. Acta, 2004, 1696(1), 59-65.
    • (2004) Biochim. Biophys. Acta , vol.1696 , Issue.1 , pp. 59-65
    • Kulakova, L.1    Galkin, A.2    Nakayama, T.3    Nishino, T.4    Esaki, N.5
  • 22
    • 0036301647 scopus 로고    scopus 로고
    • The cold-active lipase of Pseudomonas fragi. Heterologous expression, biochemical characterization and molecular modeling
    • Alquati, C.; De Gioia, L.; Santarossa, G.; Alberghina, L.; Fantucci, P.; Lotti M. The cold-active lipase of Pseudomonas fragi. Heterologous expression, biochemical characterization and molecular modeling. Eur. J. Biochem., 2002, 26(13), 3321-3328.
    • (2002) Eur. J. Biochem. , vol.26 , Issue.13 , pp. 3321-3328
    • Alquati, C.1    De Gioia, L.2    Santarossa, G.3    Alberghina, L.4    Fantucci, P.5    Lotti, M.6
  • 23
    • 0031889267 scopus 로고    scopus 로고
    • A coldadapted lipase of an Alaskan psychrotroph, Pseudomonas sp. strain B11-1: Gene cloning and enzyme purification and characterization
    • Choo, D.W.; Kurihara, T.; Suzuki, T.; Soda, K.; Esaki, N. A coldadapted lipase of an Alaskan psychrotroph, Pseudomonas sp. strain B11-1: gene cloning and enzyme purification and characterization. Appl. Environ. Microbiol., 1998, 64(2), 486-491.
    • (1998) Appl. Environ. Microbiol. , vol.64 , Issue.2 , pp. 486-491
    • Choo, D.W.1    Kurihara, T.2    Suzuki, T.3    Soda, K.4    Esaki, N.5
  • 24
    • 24244454762 scopus 로고
    • Purification of a thermostable, non-specific lipase from Candida and its use in transesterification
    • WO Patent 8802775
    • Michiyo, M. Purification of a thermostable, non-specific lipase from Candida and its use in transesterification. WO Patent 8802775, Chem. Abstr., 1989, 110, 20529.
    • (1989) Chem. Abstr. , vol.110 , pp. 20529
    • Michiyo, M.1
  • 25
    • 38049012808 scopus 로고    scopus 로고
    • X-ray structure of Candida antarctica lipase A shows a novel lid structure and a likely mode of interfacial activation
    • Ericsson, D.J.; Kasrayan, A.; Johansson, P.; Bergfors, T.; Sandstrüm, A.G.; Bäckvall, J.E.; Mowbray, SL. X-ray structure of Candida antarctica lipase A shows a novel lid structure and a likely mode of interfacial activation. J. Mol. Biol., 2008, 376(1), 109-119.
    • (2008) J. Mol. Biol. , vol.376 , Issue.1 , pp. 109-119
    • Ericsson, D.J.1    Kasrayan, A.2    Johansson, P.3    Bergfors, T.4    Sandstrüm, A.G.5    Bäckvall, J.E.6    Mowbray, S.L.7
  • 26
    • 0032479388 scopus 로고    scopus 로고
    • Lipases: Interfacial Enzymes with Attractive Applications
    • Schmid, R. D.; Verger, R. Lipases: Interfacial Enzymes with Attractive Applications. Angew. Chem., Int. Ed. Engl. 1998, 37(12), 1609-1633.
    • (1998) Angew. Chem., Int. Ed. Engl. , vol.37 , Issue.12 , pp. 1609-1633
    • Schmid, R.D.1    Verger, R.2
  • 28
    • 33749183101 scopus 로고    scopus 로고
    • High yield expression of lipase A from Candida antarctica in the methylotrophic yeast Pichia pastoris and its purification and characterisation
    • Pfeffer, J.; Richter, S.; Nieveler, J.; Hansen, C-E.; Rhlid, R. B.; Schmid, R.D.; Rusnak, M. High yield expression of lipase A from Candida antarctica in the methylotrophic yeast Pichia pastoris and its purification and characterisation. Appl Microbiol. Biotechnol., 2006, 72(5), 931-938.
    • (2006) Appl Microbiol. Biotechnol. , vol.72 , Issue.5 , pp. 931-938
    • Pfeffer, J.1    Richter, S.2    Nieveler, J.3    Hansen, C.-E.4    Rhlid, R.B.5    Schmid, R.D.6    Rusnak, M.7
  • 29
    • 0037206784 scopus 로고    scopus 로고
    • Candida antarctica lipase A. - A powerful catalyst for the resolution of heteroaro- matic β-amino esters
    • Solymár, M.; Fülüp, F.; Kanerva, LT. Candida antarctica lipase A. - a powerful catalyst for the resolution of heteroaro- matic β-amino esters. Tetrahedron Asym., 2002, 13, 2383.
    • (2002) Tetrahedron Asym. , vol.13 , pp. 2383
    • Solymár, M.1    Fülüp, F.2    Kanerva, L.T.3
  • 31
    • 34250879694 scopus 로고    scopus 로고
    • The psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125 possesses a gene coding for a cold- adapted feruloyl esterase activity that shares homology with esterase enzymes from gammaproteobacteria and yeast
    • Aurilia, V.; Parracino, A.; Saviano, M.; Rossi, M.; D'Auria, S. The psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125 possesses a gene coding for a cold- adapted feruloyl esterase activity that shares homology with esterase enzymes from gammaproteobacteria and yeast. Gene, 2007, 397(1-2), 51-57.
    • (2007) Gene , vol.397 , Issue.1-2 , pp. 51-57
    • Aurilia, V.1    Parracino, A.2    Saviano, M.3    Rossi, M.4    D'auria, S.5
  • 32
    • 41549117559 scopus 로고    scopus 로고
    • Heterologous protein expression in psychrophilic hosts
    • (Margesin, R.; Schinner, F.; Marx, J.-C.; Gerday, C. Eds.) . Springer-Verlag Berlin Heidelberg.
    • Parrilli, E. Duilio, A.; Tutino, ML. Heterologous protein expression in psychrophilic hosts in Psychrophiles: from Biodiversity to Biotechnology, (Margesin, R.; Schinner, F.; Marx, J.-C.; Gerday, C. Eds.). 2008, pp. 365-379. Springer-Verlag Berlin Heidelberg.
    • (2008) Psychrophiles: From Biodiversity to Biotechnology , pp. 365-379
    • Parrilli, E.1    Duilio, A.2    Tutino, M.L.3
  • 33
    • 43049159561 scopus 로고    scopus 로고
    • The cold-active Lip1 lipase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 is a member of a new bacterial lipolytic enzyme family
    • de Pascale, D.; Cusano, A.M.; Autore, F.; Parrilli, E.; di Prisco, G.; Marino, G.; Tutino, ML. The cold-active Lip1 lipase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 is a member of a new bacterial lipolytic enzyme family. Extremophiles, 2008, 12(3), 311-323.
    • (2008) Extremophiles , vol.12 , Issue.3 , pp. 311-323
    • De Pascale, D.1    Cusano, A.M.2    Autore, F.3    Parrilli, E.4    Di Prisco, G.5    Marino, G.6    Tutino, M.L.7
  • 34
    • 0032784276 scopus 로고    scopus 로고
    • Alpha/beta hydrolase fold enzymes: The family keeps growing
    • Nardini, M.; Dijkstra, B.W. Alpha/beta hydrolase fold enzymes: the family keeps growing. Curr. Opin. Struct. Biol., 1999, 9(6), 732-737.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , Issue.6 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 35
    • 0027200087 scopus 로고
    • Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography
    • van Tilbeurgh, H.; Egloff, M.P.; Martinez, C.; Rugani, N.; Verger, R.; Cambillau, C. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature, 1993, 362(6423), 814-820.
    • (1993) Nature , vol.362 , Issue.6423 , pp. 814-820
    • Van Tilbeurgh, H.1    Egloff, M.P.2    Martinez, C.3    Rugani, N.4    Verger, R.5    Cambillau, C.6
  • 36
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the gramnegative bacterial outer membrane
    • Bos, M.P.; Robert, V.; Tommassen, J. Biogenesis of the gramnegative bacterial outer membrane. Annu. Rev. Microbiol., 2007, 61, 191-214.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 37
    • 0034170458 scopus 로고    scopus 로고
    • Toward a molecular understanding of cold activity of enzymes from psychrophiles
    • Russell, N.J. Toward a molecular understanding of cold activity of enzymes from psychrophiles. Extremophiles, 2000, 4(2), 83-90.
    • (2000) Extremophiles , vol.4 , Issue.2 , pp. 83-90
    • Russell, N.J.1
  • 38
    • 0035461361 scopus 로고    scopus 로고
    • Lowtemperature lipase from psychrotrophic Pseudomonas sp. strain KB700A
    • Rashid, N.; Shimada, Y.; Ezaki, S.; Atomi, H.; Imanaka, T. Lowtemperature lipase from psychrotrophic Pseudomonas sp. strain KB700A. Appl. Environ. Microbiol., 2001, 67(9), 4064-4069.
    • (2001) Appl. Environ. Microbiol. , vol.67 , Issue.9 , pp. 4064-4069
    • Rashid, N.1    Shimada, Y.2    Ezaki, S.3    Atomi, H.4    Imanaka, T.5
  • 39
    • 34247126769 scopus 로고    scopus 로고
    • A novel psychrophilic lipase from Pseudomonas fluorescens with unique property in chiral resolution and biodiesel production via transesterification
    • Luo, Y.; Zheng, Y.; Jiang, Z.; Ma, Y.; Wei, D. A novel psychrophilic lipase from Pseudomonas fluorescens with unique property in chiral resolution and biodiesel production via transesterification. Appl. Microbiol. Biotechnol., 2006, 73(2), 349-355.
    • (2006) Appl. Microbiol. Biotechnol. , vol.73 , Issue.2 , pp. 349-355
    • Luo, Y.1    Zheng, Y.2    Jiang, Z.3    Ma, Y.4    Wei, D.5
  • 40
    • 0344465273 scopus 로고    scopus 로고
    • Psychrobacter okhotskensis sp. nov., a lipaseproducing facultative psychrophile isolated from the coast of the Okhotsk Sea
    • Yumoto, I.; Hirota, K.; Sogabe, Y.; Nodasaka, Y.; Yokota, Y.; Hoshino, T. Psychrobacter okhotskensis sp. nov., a lipaseproducing facultative psychrophile isolated from the coast of the Okhotsk Sea. Int. J. Syst. Evol. Microbiol., 2003, 53(6), 1985-1989.
    • (2003) Int. J. Syst. Evol. Microbiol. , vol.53 , Issue.6 , pp. 1985-1989
    • Yumoto, I.1    Hirota, K.2    Sogabe, Y.3    Nodasaka, Y.4    Yokota, Y.5    Hoshino, T.6
  • 41
    • 34248352272 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a cold-adapted lipase gene from an antarctic deep-sea psychrotrophic bacterium, Psychrobacter sp 7195
    • Zhang, J.; Lin, S.; Zeng, R. Cloning, expression, and characterization of a cold-adapted lipase gene from an antarctic deep-sea psychrotrophic bacterium, Psychrobacter sp 7195. J. Microbiol Biotechnol., 2007, 17(4), 604-610.
    • (2007) J. Microbiol Biotechnol. , vol.17 , Issue.4 , pp. 604-610
    • Zhang, J.1    Lin, S.2    Zeng, R.3
  • 42
    • 38049105877 scopus 로고    scopus 로고
    • Cloning and expression of lipP, a gene encoding a cold-adapted lipase from Moritella sp.2-5-10-1
    • Yang, X.; Lin, X.; Fan, T.; Bian, J.; Huang X. Cloning and expression of lipP, a gene encoding a cold-adapted lipase from Moritella sp.2-5-10-1. Curr. Microbiol., 2008, 56(2),194-198.
    • (2008) Curr. Microbiol. , vol.56 , Issue.2 , pp. 194-198
    • Yang, X.1    Lin, X.2    Fan, T.3    Bian, J.4    Huang, X.5
  • 43
    • 33747518326 scopus 로고    scopus 로고
    • Industrial applications of microbial lipases
    • Hasan, F.; Shah, AA.; Hameed A. Industrial applications of microbial lipases. Enzyme Microb. Tech., 2006, 39(2), 235-251.
    • (2006) Enzyme Microb. Tech. , vol.39 , Issue.2 , pp. 235-251
    • Hasan, F.1    Shah, A.A.2    Hameed, A.3
  • 44
    • 34548297679 scopus 로고    scopus 로고
    • Alpine microorganisms: Useful tools for lowtemperature bioremediation
    • Margesin, R. Alpine microorganisms: useful tools for lowtemperature bioremediation. J. Microbiol., 2007, 45(4), 281-285.
    • (2007) J. Microbiol. , vol.45 , Issue.4 , pp. 281-285
    • Margesin, R.1
  • 45
    • 18144385855 scopus 로고    scopus 로고
    • Dependence of biodiesel fuel properties on the structure of fatty acid alkyl esters
    • Knothe, G. Dependence of biodiesel fuel properties on the structure of fatty acid alkyl esters. Fuel Process Technol., 2005, 86(10), 1059-1070.
    • (2005) Fuel Process Technol. , vol.86 , Issue.10 , pp. 1059-1070
    • Knothe, G.1
  • 46
    • 27944503485 scopus 로고    scopus 로고
    • Study on acyl migration in immobilized lipozyme TL-catalyzed transesterification of soybean oil for biodiesel production
    • Du, W.; Xu, Y.Y.; Liu, D.H.; Li, Z.B. Study on acyl migration in immobilized lipozyme TL-catalyzed transesterification of soybean oil for biodiesel production. J. Mol. Catal. B: Enzym., 2005, 37(1-6), 68-71.
    • (2005) J. Mol. Catal. B: Enzym. , vol.37 , Issue.1-6 , pp. 68-71
    • Du, W.1    Xu, Y.Y.2    Liu, D.H.3    Li, Z.B.4
  • 47
    • 14844293851 scopus 로고    scopus 로고
    • Lipase-catalyzed production of biodiesel from rice bran oil
    • Lai, C.C.; Zullaikah, S.; Vali, R.R.; Ju, Y.H. Lipase-catalyzed production of biodiesel from rice bran oil. J. Chem. Technol. Biot., 2005, 80, 331-337.
    • (2005) J. Chem. Technol. Biot. , vol.80 , pp. 331-337
    • Lai, C.C.1    Zullaikah, S.2    Vali, R.R.3    Ju, Y.H.4
  • 48
    • 33644513058 scopus 로고    scopus 로고
    • Enzymatic transesterification of sunflower oil in an aqueous- oil biphasic system
    • Oliveira, A.C.; Rosa, M.F. Enzymatic transesterification of sunflower oil in an aqueous- oil biphasic system. J. Am. Oil Chem. Soc., 2006, 83, 21-25.
    • (2006) J. Am. Oil Chem. Soc. , vol.83 , pp. 21-25
    • Oliveira, A.C.1    Rosa, M.F.2
  • 49
    • 0037036126 scopus 로고    scopus 로고
    • Enzymatic alcoholysis for biodiesel fuel production and application of the reaction to oil processing
    • Shimada, Y.; Watanabe, Y.; Sugihara, A.; Tominaga, Y. Enzymatic alcoholysis for biodiesel fuel production and application of the reaction to oil processing. J. Mol. Catal. B: Enzym., 2002, 17(3-5), 133-142.
    • (2002) J. Mol. Catal. B: Enzym. , vol.17 , Issue.3-5 , pp. 133-142
    • Shimada, Y.1    Watanabe, Y.2    Sugihara, A.3    Tominaga, Y.4
  • 51
    • 10944220573 scopus 로고    scopus 로고
    • Immobilized Pseudomonas cepacia lipase for biodiesel fuel production from soybean oil
    • Noureddini, H.; Gao, X.; Philkana, R.S. Immobilized Pseudomonas cepacia lipase for biodiesel fuel production from soybean oil. Bioresource Technol., 2005, 96(7), 769-777.
    • (2005) Bioresource Technol. , vol.96 , Issue.7 , pp. 769-777
    • Noureddini, H.1    Gao, X.2    Philkana, R.S.3
  • 52
    • 0033369696 scopus 로고    scopus 로고
    • Stepwise ethanolysis of tuna oil using immobilized Candida antarctica lipase
    • Watanabe, Y.; Shimada, Y.; Sugihara, A.; Tominaga, Y. Stepwise ethanolysis of tuna oil using immobilized Candida antarctica lipase. J. Biosci. Bioeng., 1999 88(6), 622-626.
    • (1999) J. Biosci. Bioeng. , vol.88 , Issue.6 , pp. 622-626
    • Watanabe, Y.1    Shimada, Y.2    Sugihara, A.3    Tominaga, Y.4
  • 53
    • 0034596254 scopus 로고    scopus 로고
    • A rolling-circle plasmid from Psychrobacter sp. TA144: Evidence for a novel rep subfamily
    • Tutino, ML.; Duilio, A.; Moretti, MA.; Sannia, G.; Marino, G. A rolling-circle plasmid from Psychrobacter sp. TA144: evidence for a novel rep subfamily. Biochem. Biophys. Res. Commun., 2000, 274(2), 488-495.
    • (2000) Biochem. Biophys. Res. Commun. , vol.274 , Issue.2 , pp. 488-495
    • Tutino, M.L.1    Duilio, A.2    Moretti, M.A.3    Sannia, G.4    Marino, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.