메뉴 건너뛰기




Volumn 6, Issue 8, 2011, Pages

A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA)

Author keywords

[No Author keywords available]

Indexed keywords

FISH OIL; ICOSAPENTAENOIC ACID; LIPBL PROTEIN; OLIVE OIL; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 84856563290     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0023325     Document Type: Article
Times cited : (82)

References (44)
  • 1
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • Jaeger KE, Dijkstra BW, Reetz MT, (1999) Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Ann Rev Microbiol 53: 315-351.
    • (1999) Ann Rev Microbiol , vol.53 , pp. 315-351
    • Jaeger, K.E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 2
    • 0032721432 scopus 로고    scopus 로고
    • A novel lipolytic enzyme located in the outer membrane of Pseudomonas aeruginosa
    • Wilhelm S, Tommassen J, Jaeger KE, (1999) A novel lipolytic enzyme located in the outer membrane of Pseudomonas aeruginosa. J Bacteriol 181: 6977-6986.
    • (1999) J Bacteriol , vol.181 , pp. 6977-6986
    • Wilhelm, S.1    Tommassen, J.2    Jaeger, K.E.3
  • 3
    • 0029007122 scopus 로고
    • A new family of lipolytic enzymes?
    • Upton C, Buckley JT, (1995) A new family of lipolytic enzymes? Trends Biochem Sci 20: 178-179.
    • (1995) Trends Biochem Sci , vol.20 , pp. 178-179
    • Upton, C.1    Buckley, J.T.2
  • 4
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: classification and properties
    • Arpigny JL, Jaeger KE, (1999) Bacterial lipolytic enzymes: classification and properties. Biochem J 34: 177-183.
    • (1999) Biochem J , vol.34 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 5
    • 61649113649 scopus 로고    scopus 로고
    • Lipolytic enzymes from extremophilic microorganisms
    • In: Mellado E, Barredo JL, editors, Kerala, India, Microorganisms for industrial enzymes and biocontrol
    • Mellado E, Martín S, Sánchez-Porro C, Ventosa A, (2005) Lipolytic enzymes from extremophilic microorganisms. In: Mellado E, Barredo JL, editors. Research Signpost Kerala, India pp. 25-43 Microorganisms for industrial enzymes and biocontrol.
    • (2005) Research Signpost , pp. 25-43
    • Mellado, E.1    Martín, S.2    Sánchez-Porro, C.3    Ventosa, A.4
  • 6
    • 34547263402 scopus 로고    scopus 로고
    • Microbial extremophiles at the limits of life
    • Pikuta EV, Hoover RB, Tang J, (2007) Microbial extremophiles at the limits of life. Crit Rev Microbiol 33: 183-209.
    • (2007) Crit Rev Microbiol , vol.33 , pp. 183-209
    • Pikuta, E.V.1    Hoover, R.B.2    Tang, J.3
  • 7
    • 0034342554 scopus 로고    scopus 로고
    • Production of specific-structured triacylglycerols by lipase-catalyzed reactions: a review
    • Xuebing X, (2000) Production of specific-structured triacylglycerols by lipase-catalyzed reactions: a review. Europ J Pharma Biopharma 102: 287-303.
    • (2000) Europ J Pharma Biopharma , vol.102 , pp. 287-303
    • Xuebing, X.1
  • 8
    • 0032137277 scopus 로고    scopus 로고
    • Lipase-assisted concentration of n-3 polyunsaturated fatty acids in acylglicerols from marine oils
    • Wanasundara UN, Shahidi F, (1998) Lipase-assisted concentration of n-3 polyunsaturated fatty acids in acylglicerols from marine oils. J Amer Oil Chem Soc 75: 945-951.
    • (1998) J Amer Oil Chem Soc , vol.75 , pp. 945-951
    • Wanasundara, U.N.1    Shahidi, F.2
  • 9
    • 21644488706 scopus 로고    scopus 로고
    • Proteolytic extraction of salmon oil and PUFA concentration by lipases
    • Linder M, Fanni J, Parmentier M, (2005) Proteolytic extraction of salmon oil and PUFA concentration by lipases. Mar Biotechnol 7: 70-76.
    • (2005) Mar Biotechnol , vol.7 , pp. 70-76
    • Linder, M.1    Fanni, J.2    Parmentier, M.3
  • 10
    • 27944482507 scopus 로고    scopus 로고
    • Concentration of PUFAs in glyceride by hydrolysis of fish oil with lipase
    • Zheng Y, Zheng N, Zhuo J, Ma L, (2005) Concentration of PUFAs in glyceride by hydrolysis of fish oil with lipase. Chin J Appl Environ Biol 11: 571-574.
    • (2005) Chin J Appl Environ Biol , vol.11 , pp. 571-574
    • Zheng, Y.1    Zheng, N.2    Zhuo, J.3    Ma, L.4
  • 11
    • 41749123712 scopus 로고    scopus 로고
    • Production of n-3 polyunsaturated fatty acid concentrate from sardine oil by immobilized Candida rugosa lipase
    • Okada T, Morrissey MT, (2008) Production of n-3 polyunsaturated fatty acid concentrate from sardine oil by immobilized Candida rugosa lipase. J Food Sci 73: 146-150.
    • (2008) J Food Sci , vol.73 , pp. 146-150
    • Okada, T.1    Morrissey, M.T.2
  • 12
    • 0032486523 scopus 로고    scopus 로고
    • A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports
    • Bastida A, Sabuquillo P, Armisen P, Fernández-Lafuente R, Huguet J, et al. (1998) A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports. Biotechnol Bioeng 58: 486-493.
    • (1998) Biotechnol Bioeng , vol.58 , pp. 486-493
    • Bastida, A.1    Sabuquillo, P.2    Armisen, P.3    Fernández-Lafuente, R.4    Huguet, J.5
  • 13
    • 1842763651 scopus 로고    scopus 로고
    • Purification, immobilization, and stabilization of a lipase from Bacillus thermocatenulatus by interfacial adsorption on hydrophobic supports
    • Palomo JM, Segura RL, Fernández-Lorente G, Pernas M, Rua ML, et al. (2004) Purification, immobilization, and stabilization of a lipase from Bacillus thermocatenulatus by interfacial adsorption on hydrophobic supports. Biotechnol Prog 20: 630-635.
    • (2004) Biotechnol Prog , vol.20 , pp. 630-635
    • Palomo, J.M.1    Segura, R.L.2    Fernández-Lorente, G.3    Pernas, M.4    Rua, M.L.5
  • 14
    • 2942720843 scopus 로고    scopus 로고
    • Different properties of the lipases contained in porcine pancreatic lipase extracts as enantioselective biocatalysts
    • Segura RL, Palomo JM, Mateo C, Cortes A, Terreni M, et al. (2004) Different properties of the lipases contained in porcine pancreatic lipase extracts as enantioselective biocatalysts. Biotechnol Prog 20: 825-829.
    • (2004) Biotechnol Prog , vol.20 , pp. 825-829
    • Segura, R.L.1    Palomo, J.M.2    Mateo, C.3    Cortes, A.4    Terreni, M.5
  • 15
    • 0032506270 scopus 로고    scopus 로고
    • Interfacial affinity chromatography' of lipases: separation of different fractions by selective adsorption on supports activated with hydrophobic groups
    • Sabuquillo P, Reina J, Fernández-Lorente G, Guisán JM, Fernández-Lafuente R, (1998) 'Interfacial affinity chromatography' of lipases: separation of different fractions by selective adsorption on supports activated with hydrophobic groups. Biochim Biophys Acta 1388: 337-348.
    • (1998) Biochim Biophys Acta , vol.1388 , pp. 337-348
    • Sabuquillo, P.1    Reina, J.2    Fernández-Lorente, G.3    Guisán, J.M.4    Fernández-Lafuente, R.5
  • 18
    • 0032869128 scopus 로고    scopus 로고
    • Direct fluorescence-based lipase activity assay
    • Díaz P, Prim N, Javier Pastor FI, (1999) Direct fluorescence-based lipase activity assay. Biotechniques 27: 696-698.
    • (1999) Biotechniques , vol.27 , pp. 696-698
    • Díaz, P.1    Prim, N.2    Javier Pastor, F.I.3
  • 19
    • 0019186616 scopus 로고
    • A small cosmid for efficient cloning of large DNA fragments
    • Hohn B, Collins J, (1980) A small cosmid for efficient cloning of large DNA fragments. Gene 11: 291-298.
    • (1980) Gene , vol.11 , pp. 291-298
    • Hohn, B.1    Collins, J.2
  • 21
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schäffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 67049118923 scopus 로고    scopus 로고
    • Accurate and sensitive peptide identification with Mascot Percolator
    • Brosch M, Yu L, Hubbard T, Choudhary J, (2009) Accurate and sensitive peptide identification with Mascot Percolator. J Proteome Res 8: 3176-3181.
    • (2009) J Proteome Res , vol.8 , pp. 3176-3181
    • Brosch, M.1    Yu, L.2    Hubbard, T.3    Choudhary, J.4
  • 25
    • 0023089142 scopus 로고
    • Specific and sensitive plate assay for bacterial lipases
    • Kouker G, Jaeger KE, (1987) Specific and sensitive plate assay for bacterial lipases. Appl Environ Microbiol 53: 211-213.
    • (1987) Appl Environ Microbiol , vol.53 , pp. 211-213
    • Kouker, G.1    Jaeger, K.E.2
  • 26
    • 20644469267 scopus 로고
    • Quantitative analyses of biochemical kinetic resolutions of enantiomers
    • Chen CS, Fujimoto Y, Girdaukas G, (1982) Quantitative analyses of biochemical kinetic resolutions of enantiomers. J Am Chem Soc 104: 7294-7299.
    • (1982) J Am Chem Soc , vol.104 , pp. 7294-7299
    • Chen, C.S.1    Fujimoto, Y.2    Girdaukas, G.3
  • 27
    • 84856581385 scopus 로고    scopus 로고
    • Molecular characterization of the lipase LipM produced by Marinobacter lipolyticus
    • University of Seville, Department of Microbiology and Parasitology
    • Martín S, (2006) Molecular characterization of the lipase LipM produced by Marinobacter lipolyticus. PhD thesis University of Seville, Department of Microbiology and Parasitology.
    • (2006) PhD Thesis
    • Martín, S.1
  • 28
    • 0023976519 scopus 로고
    • The active-site-serine penicillin-recognizing enzymes as a members of the Streptomyces R61 DD-peptidase family
    • Joris B, Ghuysens JM, Dive G, Renard A, Dideberg O, et al. (1988) The active-site-serine penicillin-recognizing enzymes as a members of the Streptomyces R61 DD-peptidase family. J Biochem 250: 313-324.
    • (1988) J Biochem , vol.250 , pp. 313-324
    • Joris, B.1    Ghuysens, J.M.2    Dive, G.3    Renard, A.4    Dideberg, O.5
  • 29
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxyl esterases: classification, properties and application in biocatalysis
    • Review
    • Bornscheuer UT, (2002) Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol Rev 26: 73-81 Review.
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 73-81
    • Bornscheuer, U.T.1
  • 30
    • 0023385987 scopus 로고
    • Rules for optimization of biocatalysis in organic solvents
    • Laane C, Boeren S, Vos K, Veeger C, (1987) Rules for optimization of biocatalysis in organic solvents. Biotechnol Bioeng 30: 81-87.
    • (1987) Biotechnol Bioeng , vol.30 , pp. 81-87
    • Laane, C.1    Boeren, S.2    Vos, K.3    Veeger, C.4
  • 31
    • 34247159537 scopus 로고    scopus 로고
    • Lipases from extremophiles and potential for industrial applications
    • Review
    • Salameh M, Wiegel J, (2007) Lipases from extremophiles and potential for industrial applications. Adv Appl Microbiol 61: 253-283 Review.
    • (2007) Adv Appl Microbiol , vol.61 , pp. 253-283
    • Salameh, M.1    Wiegel, J.2
  • 32
    • 77953700376 scopus 로고    scopus 로고
    • Industrial and environmental applications of halophilic microorganisms
    • Oren A, (2010) Industrial and environmental applications of halophilic microorganisms. Environ Technol 31: 825-834.
    • (2010) Environ Technol , vol.31 , pp. 825-834
    • Oren, A.1
  • 33
    • 28844483422 scopus 로고    scopus 로고
    • Purification of different lipases from Aspergillus niger by using a highly selective adsorption on hydrophobic supports
    • Fernández-Lorente G, Ortiz C, Segura RL, Fernández-Lafuente R, Guisán JM, et al. (2005) Purification of different lipases from Aspergillus niger by using a highly selective adsorption on hydrophobic supports. Biotechnol Bioeng 92: 773-779.
    • (2005) Biotechnol Bioeng , vol.92 , pp. 773-779
    • Fernández-Lorente, G.1    Ortiz, C.2    Segura, R.L.3    Fernández-Lafuente, R.4    Guisán, J.M.5
  • 34
    • 52649136072 scopus 로고    scopus 로고
    • Solid-phase chemical amination of a lipase from Bacillus thermocatenulatus to improve its stabilization via covalent immobilization on highly activated glyoxyl-agarose
    • Fernández-Lorente G, Godoy CA, Mendes AA, López-Gallego F, Grazu V, et al. (2008) Solid-phase chemical amination of a lipase from Bacillus thermocatenulatus to improve its stabilization via covalent immobilization on highly activated glyoxyl-agarose. Biomacromolecules 9: 2253-2261.
    • (2008) Biomacromolecules , vol.9 , pp. 2253-2261
    • Fernández-Lorente, G.1    Godoy, C.A.2    Mendes, A.A.3    López-Gallego, F.4    Grazu, V.5
  • 35
    • 77953110430 scopus 로고    scopus 로고
    • Role of long-chain polyunsaturated fatty acids in neurodevelopment and growth. Nestlé Nutr Inst WorkshopSer
    • Makrides M, Smithers LG, Gibson RA, (2010) Role of long-chain polyunsaturated fatty acids in neurodevelopment and growth. Nestlé Nutr Inst WorkshopSer. Pediatr Program 65: 123-136.
    • (2010) Pediatr Program , vol.65 , pp. 123-136
    • Makrides, M.1    Smithers, L.G.2    Gibson, R.A.3
  • 36
    • 3142753943 scopus 로고    scopus 로고
    • Dietary n-6 and n-3 fatty acid balance and cardiovascular health
    • Wijendran V, Hayes KC, (2004) Dietary n-6 and n-3 fatty acid balance and cardiovascular health. Annu Rev Nutr 24: 597-615.
    • (2004) Annu Rev Nutr , vol.24 , pp. 597-615
    • Wijendran, V.1    Hayes, K.C.2
  • 37
    • 16444363003 scopus 로고    scopus 로고
    • Dietary marine n-3 fatty acids in relation to risk of distal colorectal adenoma in women
    • Oh K, Willett WC, Fuchs CS, Giovannucci E, (2005) Dietary marine n-3 fatty acids in relation to risk of distal colorectal adenoma in women. Can Epid Biomark 14: 835-841.
    • (2005) Can Epid Biomark , vol.14 , pp. 835-841
    • Oh, K.1    Willett, W.C.2    Fuchs, C.S.3    Giovannucci, E.4
  • 38
    • 0036931477 scopus 로고    scopus 로고
    • Omega-3 fatty acids in inflammation and autoimmune diseases
    • Simopoulos AP, (2002) Omega-3 fatty acids in inflammation and autoimmune diseases. J Am Coll Nutr 21: 495-505.
    • (2002) J Am Coll Nutr , vol.21 , pp. 495-505
    • Simopoulos, A.P.1
  • 39
    • 0033886610 scopus 로고    scopus 로고
    • Enrichment of polyunsaturated fatty acids from sardine cannery affluents by enzymatic selective esterification
    • Schmitt-Rozieres M, Deyris V, Comeau LC, (2000) Enrichment of polyunsaturated fatty acids from sardine cannery affluents by enzymatic selective esterification. JAOCS 77: 329-332.
    • (2000) JAOCS , vol.77 , pp. 329-332
    • Schmitt-Rozieres, M.1    Deyris, V.2    Comeau, L.C.3
  • 40
    • 0031767658 scopus 로고    scopus 로고
    • Omega-3 fatty acid concentrates: nutricional aspects and production technologies
    • Shahidi F, Wanasundara UN, (1998) Omega-3 fatty acid concentrates: nutricional aspects and production technologies. Trends Food Sci Technol 9: 230-240.
    • (1998) Trends Food Sci Technol , vol.9 , pp. 230-240
    • Shahidi, F.1    Wanasundara, U.N.2
  • 41
    • 0034914337 scopus 로고    scopus 로고
    • Enzymatic purification of polyunsaturated fatty acids
    • Shimada Y, Sugihara A, Tominaga Y, (2001) Enzymatic purification of polyunsaturated fatty acids. J Biosc Bioeng 91: 529-538.
    • (2001) J Biosc Bioeng , vol.91 , pp. 529-538
    • Shimada, Y.1    Sugihara, A.2    Tominaga, Y.3
  • 42
    • 0000801758 scopus 로고
    • Concentration of docosahexaenoic acid in glyceride by hydrolysis of fish oils with Candida cylindracea lipase
    • Tanaka Y, Hirano J, Funada T, (1992) Concentration of docosahexaenoic acid in glyceride by hydrolysis of fish oils with Candida cylindracea lipase. JAOCS 69: 1210-1214.
    • (1992) JAOCS , vol.69 , pp. 1210-1214
    • Tanaka, Y.1    Hirano, J.2    Funada, T.3
  • 43
    • 0000870996 scopus 로고
    • Selective hydrolysis of fish oil by lipase to concentrate n-3 polyunsaturated fatty acids
    • Hoshino T, Yamane T, Shimidu S, (1990) Selective hydrolysis of fish oil by lipase to concentrate n-3 polyunsaturated fatty acids. Agric Biol Chem 54: 1459-1467.
    • (1990) Agric Biol Chem , vol.54 , pp. 1459-1467
    • Hoshino, T.1    Yamane, T.2    Shimidu, S.3
  • 44
    • 40549120110 scopus 로고    scopus 로고
    • Enrichment of eicosapentaenoic acid from sardine oil with Delta 5-olefinic bond specific lipase from Bacillus licheniformis MTCC 6824
    • Chakraborty K, Paulraj R, (2008) Enrichment of eicosapentaenoic acid from sardine oil with Delta 5-olefinic bond specific lipase from Bacillus licheniformis MTCC 6824. J Agric Food Chem 56: 1428-1433.
    • (2008) J Agric Food Chem , vol.56 , pp. 1428-1433
    • Chakraborty, K.1    Paulraj, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.