메뉴 건너뛰기




Volumn 97, Issue 6, 2013, Pages 2443-2454

Characterization of an extracellular lipase and its chaperone from Ralstonia eutropha H16

Author keywords

Chaperone; Emulsification; Lipase; Palm oil; Ralstonia eutropha; Triacylglycerol

Indexed keywords

CHAPERONE; EXTRACELLULAR LIPASE; GENE EXPRESSION ANALYSIS; LONG CARBON CHAINS; OVEREXPRESSION STRAIN; RALSTONIA EUTROPHA; SOLE CARBON SOURCE; TRIACYLGLYCEROLS;

EID: 84878849220     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4115-z     Document Type: Article
Times cited : (56)

References (64)
  • 1
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: Classification and properties
    • 10.1042/0264-6021:3430177 1:CAS:528:DyaK1MXmvVyju7o%3D
    • Arpigny JL, Jaeger KE (1999) Bacterial lipolytic enzymes: classification and properties. Biochem J 343:177-183
    • (1999) Biochem J , vol.343 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 2
    • 71549149350 scopus 로고    scopus 로고
    • Biodiesel production through lipase catalyzed transesterification: An overview
    • 10.1016/j.molcatb.2009.09.018 1:CAS:528:DC%2BD1MXhtlylsbzF
    • Bajaj A, Lohan P, Jha PN, Mehrotra R (2010) Biodiesel production through lipase catalyzed transesterification: an overview. J Mol Catal B: Enzym 62:9-14
    • (2010) J Mol Catal B: Enzym , vol.62 , pp. 9-14
    • Bajaj, A.1    Lohan, P.2    Jha, P.N.3    Mehrotra, R.4
  • 4
    • 0028308705 scopus 로고
    • Horse pancreatic lipase - The crystal structure refined at 2.3 angstrom resolution
    • 10.1006/jmbi.1994.1331 1:CAS:528:DyaK2cXltVaqur0%3D
    • Bourne Y, Martinez C, Kerfelec B, Lombardo D, Chapus C, Cambillau C (1994) Horse pancreatic lipase - the crystal structure refined at 2.3 angstrom resolution. J Mol Bio 238:709-732
    • (1994) J Mol Bio , vol.238 , pp. 709-732
    • Bourne, Y.1    Martinez, C.2    Kerfelec, B.3    Lombardo, D.4    Chapus, C.5    Cambillau, C.6
  • 5
    • 77957842036 scopus 로고    scopus 로고
    • Elucidation of beta-oxidation pathways in Ralstonia eutropha H16 by examination of global gene expression
    • 10.1128/JB.00493-10 1:CAS:528:DC%2BC3cXhsFSns7bE
    • Brigham CJ, Budde CF, Holder JW, Zeng QD, Mahan AE, Rha C, Sinskey AJ (2010) Elucidation of beta-oxidation pathways in Ralstonia eutropha H16 by examination of global gene expression. J Bacteriol 192:5454-5464
    • (2010) J Bacteriol , vol.192 , pp. 5454-5464
    • Brigham, C.J.1    Budde, C.F.2    Holder, J.W.3    Zeng, Q.D.4    Mahan, A.E.5    Rha, C.6    Sinskey, A.J.7
  • 6
    • 79952573772 scopus 로고    scopus 로고
    • Growth and polyhydroxybutyrate production by Ralstonia eutropha in emulsified plant oil medium
    • 10.1007/s00253-011-3102-0 1:CAS:528:DC%2BC3MXhslWltLY%3D
    • Budde CF, Riedel SL, Hubner F, Risch S, Popovic MK, Rha C, Sinskey AJ (2011a) Growth and polyhydroxybutyrate production by Ralstonia eutropha in emulsified plant oil medium. Appl Microbiol Biotechnol 89:1611-1619
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 1611-1619
    • Budde, C.F.1    Riedel, S.L.2    Hubner, F.3    Risch, S.4    Popovic, M.K.5    Rha, C.6    Sinskey, A.J.7
  • 7
    • 79955585460 scopus 로고    scopus 로고
    • Production of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) from plant oil by engineered Ralstonia eutropha strains
    • 10.1128/AEM.02429-10 1:CAS:528:DC%2BC3MXhtVeju7bI
    • Budde CF, Riedel SL, Willis LB, Rha C, Sinskey AJ (2011b) Production of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) from plant oil by engineered Ralstonia eutropha strains. Appl Environ Microbiol 77:2847-2854
    • (2011) Appl Environ Microbiol , vol.77 , pp. 2847-2854
    • Budde, C.F.1    Riedel, S.L.2    Willis, L.B.3    Rha, C.4    Sinskey, A.J.5
  • 8
    • 55449134749 scopus 로고    scopus 로고
    • Evidence of a double-lid movement in Pseudomonas aeruginosa lipase: Insights from molecular dynamics simulations
    • 10.1371/journal.pcbi.0010028 1:CAS:528:DC%2BD2MXhtVaqu7%2FK
    • Cherukuvada SL, Seshasayee ASN, Raghunathan K, Anishetty S, Pennathur G (2005) Evidence of a double-lid movement in Pseudomonas aeruginosa lipase: insights from molecular dynamics simulations. Plos Comput Biol 1:182-189
    • (2005) Plos Comput Biol , vol.1 , pp. 182-189
    • Cherukuvada, S.L.1    Seshasayee, A.S.N.2    Raghunathan, K.3    Anishetty, S.4    Pennathur, G.5
  • 9
    • 79951774269 scopus 로고    scopus 로고
    • Molecular cloning - A laboratory manual, 3rd edition
    • 10.1126/science.1060677 1:CAS:528:DC%2BD3MXjtVentL4%3D
    • Chong L (2001) Molecular cloning - a laboratory manual, 3rd edition. Science 292:446-446
    • (2001) Science , vol.292 , pp. 446-446
    • Chong, L.1
  • 10
    • 0026786234 scopus 로고
    • The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 angstrom resolution
    • 10.1016/0022-2836(92)90225-9 1:CAS:528:DyaK38Xmt12juro%3D
    • Derewenda ZS, Derewenda U, Dodson GG (1992) The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 angstrom resolution. J Mol Biol 227:818-839
    • (1992) J Mol Biol , vol.227 , pp. 818-839
    • Derewenda, Z.S.1    Derewenda, U.2    Dodson, G.G.3
  • 11
    • 0038692116 scopus 로고    scopus 로고
    • Role of the calcium ion and the disulfide bond in the Burkholderia glumae lipase
    • 10.1016/S1381-1177(03)00047-X 1:CAS:528:DC%2BD3sXltVSkt7c%3D
    • El Khattabi M, Van Gelder P, Bitter W, Tommassen J (2003) Role of the calcium ion and the disulfide bond in the Burkholderia glumae lipase. J Mol Catal B: Enzym 22:329-338
    • (2003) J Mol Catal B: Enzym , vol.22 , pp. 329-338
    • El Khattabi, M.1    Van Gelder, P.2    Bitter, W.3    Tommassen, J.4
  • 12
    • 63549102137 scopus 로고    scopus 로고
    • A review of the current state of biodiesel production using enzymatic transesterification
    • 10.1002/bit.22256 1:CAS:528:DC%2BD1MXjtl2ksrg%3D
    • Fjerbaek L, Christensen KV, Norddahl B (2009) A review of the current state of biodiesel production using enzymatic transesterification. Biotechnol Bioeng 102:1298-1315
    • (2009) Biotechnol Bioeng , vol.102 , pp. 1298-1315
    • Fjerbaek, L.1    Christensen, K.V.2    Norddahl, B.3
  • 14
    • 0027220383 scopus 로고
    • An accessory gene, lipB, required for the production of active Pseudomonas glumae lipase
    • 10.1111/j.1365-2958.1993.tb01718.x 1:CAS:528:DyaK2cXhvVSg
    • Frenken LGJ, Bos JW, Visser C, Muller W, Tommassen J, Verrips CT (1993a) An accessory gene, lipB, required for the production of active Pseudomonas glumae lipase. Mol Microbiol 9:579-589
    • (1993) Mol Microbiol , vol.9 , pp. 579-589
    • Frenken, L.G.J.1    Bos, J.W.2    Visser, C.3    Muller, W.4    Tommassen, J.5    Verrips, C.T.6
  • 15
    • 0027182430 scopus 로고
    • Role of the lipB gene-product in the folding of the secreted lipase of Pseudomonas glumae
    • 10.1111/j.1365-2958.1993.tb01719.x 1:CAS:528:DyaK3sXmt1Wgtbo%3D
    • Frenken LGJ, Degroot A, Tommassen J, Verrips CT (1993b) Role of the lipB gene-product in the folding of the secreted lipase of Pseudomonas glumae. Mol Microbiol 9:591-599
    • (1993) Mol Microbiol , vol.9 , pp. 591-599
    • Frenken, L.G.J.1    Degroot, A.2    Tommassen, J.3    Verrips, C.T.4
  • 16
    • 0027641942 scopus 로고
    • Pseudomonas lipases - Biochemical properties and molecular cloning
    • 10.1016/0141-0229(93)90062-7 1:CAS:528:DyaK3sXlvFyisbY%3D
    • Gilbert EJ (1993) Pseudomonas lipases - biochemical properties and molecular cloning. Enzyme Microb Technol 15:634-645
    • (1993) Enzyme Microb Technol , vol.15 , pp. 634-645
    • Gilbert, E.J.1
  • 17
    • 84946653719 scopus 로고
    • Application of lipases for synthesis of new chemicals
    • Godtfredsen SE (1990) Application of lipases for synthesis of new chemicals. Opp Biotransform 1:17-22
    • (1990) Opp Biotransform , vol.1 , pp. 17-22
    • Godtfredsen, S.E.1
  • 18
    • 3142773489 scopus 로고    scopus 로고
    • Bacterial lipases: An overview of production, purification and biochemical properties
    • 10.1007/s00253-004-1568-8 1:CAS:528:DC%2BD2cXktlyku7Y%3D
    • Gupta R, Gupta N, Rathi P (2004) Bacterial lipases: an overview of production, purification and biochemical properties. Appl Microbiol Biotechnol 64:763-781
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 763-781
    • Gupta, R.1    Gupta, N.2    Rathi, P.3
  • 20
    • 0036669425 scopus 로고    scopus 로고
    • Lipases for biotechnology
    • 10.1016/S0958-1669(02)00341-5 1:CAS:528:DC%2BD38XmsFOnsb8%3D
    • Jaeger KE, Eggert T (2002) Lipases for biotechnology. Curr Opin Biotechnol 13:390-397
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 390-397
    • Jaeger, K.E.1    Eggert, T.2
  • 21
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • 10.1016/S0167-7799(98)01195-0 1:CAS:528:DyaK1cXls1Ontrw%3D
    • Jaeger KE, Reetz MT (1998) Microbial lipases form versatile tools for biotechnology. Trends Biotechnol 16:396-403
    • (1998) Trends Biotechnol , vol.16 , pp. 396-403
    • Jaeger, K.E.1    Reetz, M.T.2
  • 22
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • 10.1146/annurev.micro.53.1.315 1:CAS:528:DyaK1MXmvVOnsb4%3D
    • Jaeger KE, Dijkstra BW, Reetz MT (1999) Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu Rev Microbiol 53:315-320
    • (1999) Annu Rev Microbiol , vol.53 , pp. 315-320
    • Jaeger, K.E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 23
    • 77955239068 scopus 로고    scopus 로고
    • Production of biodiesel from palm oil using liquid core lipase encapsulated in kappa-carrageenan
    • 10.1016/j.fuel.2010.03.016 1:CAS:528:DC%2BC3cXmvFyisb0%3D
    • Jegannathan KR, Jun-Yee L, Chan ES, Ravindra P (2010) Production of biodiesel from palm oil using liquid core lipase encapsulated in kappa-carrageenan. Fuel 89:2272-2277
    • (2010) Fuel , vol.89 , pp. 2272-2277
    • Jegannathan, K.R.1    Jun-Yee, L.2    Chan, E.S.3    Ravindra, P.4
  • 24
    • 58149143135 scopus 로고    scopus 로고
    • Cloning and characterization of a new cold-active lipase from a deep-sea sediment metagenome
    • 10.1007/s00253-008-1656-2 1:CAS:528:DC%2BD1cXhsFart7%2FJ
    • Jeon JH, Kim JT, Kim YJ, Kim HK, Lee HS, Kang SG, Kim SJ, Lee JH (2009) Cloning and characterization of a new cold-active lipase from a deep-sea sediment metagenome. Appl Microbiol Biotechnol 81:865-874
    • (2009) Appl Microbiol Biotechnol , vol.81 , pp. 865-874
    • Jeon, J.H.1    Kim, J.T.2    Kim, Y.J.3    Kim, H.K.4    Lee, H.S.5    Kang, S.G.6    Kim, S.J.7    Lee, J.H.8
  • 25
    • 46849092215 scopus 로고    scopus 로고
    • Cold active microbial lipases: Some hot issues and recent developments
    • 10.1016/j.biotechadv.2008.05.003 1:CAS:528:DC%2BD1cXoslWntrw%3D
    • Joseph B, Ramteke PW, Thomas G (2008) Cold active microbial lipases: some hot issues and recent developments. Biotechnol Adv 26:457-470
    • (2008) Biotechnol Adv , vol.26 , pp. 457-470
    • Joseph, B.1    Ramteke, P.W.2    Thomas, G.3
  • 26
    • 1542685462 scopus 로고    scopus 로고
    • High yield production of polyhydroxyalkanoates from soybean oil by Ralstonia eutropha and its recombinant strain
    • 10.1016/S0141-3910(03)00227-1 1:CAS:528:DC%2BD2cXjvVKjtA%3D%3D
    • Kahar P, Tsuge T, Taguchi K, Doi Y (2004) High yield production of polyhydroxyalkanoates from soybean oil by Ralstonia eutropha and its recombinant strain. Polym Degrad Stab 83:79-86
    • (2004) Polym Degrad Stab , vol.83 , pp. 79-86
    • Kahar, P.1    Tsuge, T.2    Taguchi, K.3    Doi, Y.4
  • 27
    • 0035991656 scopus 로고    scopus 로고
    • Production of a Pseudomonas lipase in n-alkane substrate and its isolation using an improved ammonium sulfate precipitation technique
    • 10.1016/S0960-8524(02)00061-5 1:CAS:528:DC%2BD38XktVeiur8%3D
    • Kanwar L, Gogoi BK, Goswami P (2002) Production of a Pseudomonas lipase in n-alkane substrate and its isolation using an improved ammonium sulfate precipitation technique. Bioresour Technol 84:207-211
    • (2002) Bioresour Technol , vol.84 , pp. 207-211
    • Kanwar, L.1    Gogoi, B.K.2    Goswami, P.3
  • 28
    • 10344255607 scopus 로고    scopus 로고
    • Effects of growth rate on the production of Pseudomonas fluorescens lipase during the fed-batch cultivation of Escherichia coli
    • 10.1021/bp960047h 1:CAS:528:DyaK28XlsFCltL8%3D
    • Kim SS, Kim EK, Rhee JS (1996) Effects of growth rate on the production of Pseudomonas fluorescens lipase during the fed-batch cultivation of Escherichia coli. Biotechnol Prog 12:718-722
    • (1996) Biotechnol Prog , vol.12 , pp. 718-722
    • Kim, S.S.1    Kim, E.K.2    Rhee, J.S.3
  • 29
    • 0034811043 scopus 로고    scopus 로고
    • Lipase and its modulator from Pseudomonas sp. strain KFCC 10818: Proline-to-glutamine substitution at position 112 induces formation of enzymatically active lipase in the absence of the modulator
    • 10.1128/JB.183.20.5937-5941.2001 1:CAS:528:DC%2BD3MXntlamsr8%3D
    • Kim EK, Jang WH, Ko JH, Kang JS, Noh MJ, Yoo OJ (2001) Lipase and its modulator from Pseudomonas sp. strain KFCC 10818: proline-to-glutamine substitution at position 112 induces formation of enzymatically active lipase in the absence of the modulator. J Bacteriol 183:5937-5941
    • (2001) J Bacteriol , vol.183 , pp. 5937-5941
    • Kim, E.K.1    Jang, W.H.2    Ko, J.H.3    Kang, J.S.4    Noh, M.J.5    Yoo, O.J.6
  • 30
    • 0029815077 scopus 로고    scopus 로고
    • Physiological factors affecting production of extracellular lipase (LipA) in Acinetobacter calcoaceticus BD413: Fatty acid repression of lipA expression and degradation of LipA
    • 1:CAS:528:DyaK28XmtFOksLc%3D
    • Kok RG, Nudel CB, Gonzalez RH, NugterenRoodzant IM, Hellingwerf KJ (1996) Physiological factors affecting production of extracellular lipase (LipA) in Acinetobacter calcoaceticus BD413: fatty acid repression of lipA expression and degradation of LipA. J Bacteriol 178:6025-6035
    • (1996) J Bacteriol , vol.178 , pp. 6025-6035
    • Kok, R.G.1    Nudel, C.B.2    Gonzalez, R.H.3    Nugterenroodzant, I.M.4    Hellingwerf, K.J.5
  • 31
    • 0032827502 scopus 로고    scopus 로고
    • A novel alkaline, thermostable, protease-free lipase from Pseudomonas sp
    • 10.1023/A:1005591009596 1:CAS:528:DyaK1MXnt1Gls7c%3D
    • Kulkarni N, Gadre RV (1999) A novel alkaline, thermostable, protease-free lipase from Pseudomonas sp. Biotechnol Lett 21:897-899
    • (1999) Biotechnol Lett , vol.21 , pp. 897-899
    • Kulkarni, N.1    Gadre, R.V.2
  • 32
    • 0027279621 scopus 로고
    • Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme
    • 10.1111/j.1432-1033.1993.tb18127.x 1:CAS:528:DyaK3sXlsFCls7s%3D
    • Lesuisse E, Schanck K, Colson C (1993) Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme. Eur J Biochem 216:155-160
    • (1993) Eur J Biochem , vol.216 , pp. 155-160
    • Lesuisse, E.1    Schanck, K.2    Colson, C.3
  • 33
    • 0029126474 scopus 로고
    • Effect of Triton X-100 on alkaline lipase production by Pseudomonas pseudoalcaligenes F-111
    • 10.1007/BF00127434 1:CAS:528:DyaK2MXosVSqt70%3D
    • Lin SF, Chiou CM, Tsai YC (1995) Effect of Triton X-100 on alkaline lipase production by Pseudomonas pseudoalcaligenes F-111. Biotechnol Lett 17:959-962
    • (1995) Biotechnol Lett , vol.17 , pp. 959-962
    • Lin, S.F.1    Chiou, C.M.2    Tsai, Y.C.3
  • 34
    • 0032102789 scopus 로고    scopus 로고
    • Physiological control on the expression and secretion of Candida rugosa lipase
    • 10.1016/S0009-3084(98)00038-3 1:CAS:528:DyaK1cXks1Kru70%3D
    • Lotti M, Monticelli S, Montesinos JL, Brocca S, Valero F, Lafuente J (1998) Physiological control on the expression and secretion of Candida rugosa lipase. Chem Phys Lipids 93:143-148
    • (1998) Chem Phys Lipids , vol.93 , pp. 143-148
    • Lotti, M.1    Monticelli, S.2    Montesinos, J.L.3    Brocca, S.4    Valero, F.5    Lafuente, J.6
  • 35
    • 11744266617 scopus 로고
    • Present and future applications of lipases
    • 1:CAS:528:DyaL28XhsVOjsbs%3D
    • Macrae AR, Hammond RC (1985) Present and future applications of lipases. Biotechnolo Genet Eng Rev 3:193-217
    • (1985) Biotechnolo Genet Eng Rev , vol.3 , pp. 193-217
    • Macrae, A.R.1    Hammond, R.C.2
  • 36
    • 0034094334 scopus 로고    scopus 로고
    • Effects of carbon sources on extracellular lipase production and lipA transcription in Acinetobacter calcoaceticus
    • 10.1038/sj.jim.2900764 1:CAS:528:DC%2BD3cXhtlyhsr8%3D
    • Mahler GF, Kok RG, Cordenons A, Hellingwerf KJ, Nudel BC (2000) Effects of carbon sources on extracellular lipase production and lipA transcription in Acinetobacter calcoaceticus. J Ind Microbiol Biotechnol 24:25-30
    • (2000) J Ind Microbiol Biotechnol , vol.24 , pp. 25-30
    • Mahler, G.F.1    Kok, R.G.2    Cordenons, A.3    Hellingwerf, K.J.4    Nudel, B.C.5
  • 37
    • 33847272054 scopus 로고    scopus 로고
    • Studies on lipolytic isoenzymes from a thermophilic Bacillus sp.: Production, purification and biochemical characterization
    • 10.1016/j.enzmictec.2006.07.006 1:CAS:528:DC%2BD2sXit1Gktro%3D
    • Nawani N, Kaur J (2007) Studies on lipolytic isoenzymes from a thermophilic Bacillus sp.: production, purification and biochemical characterization. Enzyme Microb Technol 40:881-887
    • (2007) Enzyme Microb Technol , vol.40 , pp. 881-887
    • Nawani, N.1    Kaur, J.2
  • 38
    • 77955286960 scopus 로고    scopus 로고
    • Evaluation of jatropha oil to produce poly(3-hydroxybutyrate) by Cupriavidus necator H16
    • 10.1016/j.polymdegradstab.2010.01.021 1:CAS:528:DC%2BC3cXoslamtLc%3D
    • Ng KS, Ooi WY, Goh LK, Shenbagarathai R, Sudesh K (2010) Evaluation of jatropha oil to produce poly(3-hydroxybutyrate) by Cupriavidus necator H16. Polym Degrad Stab 95:1365-1369
    • (2010) Polym Degrad Stab , vol.95 , pp. 1365-1369
    • Ng, K.S.1    Ooi, W.Y.2    Goh, L.K.3    Shenbagarathai, R.4    Sudesh, K.5
  • 39
    • 0027435346 scopus 로고
    • The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate
    • 10.1016/0014-5793(93)80310-Q 1:CAS:528:DyaK2cXjsVGq
    • Noble MEM, Cleasby A, Johnson LN, Egmond MR, Frenken LGJ (1993) The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. FEBS Lett 331:123-128
    • (1993) FEBS Lett , vol.331 , pp. 123-128
    • Noble, M.E.M.1    Cleasby, A.2    Johnson, L.N.3    Egmond, M.R.4    Frenken, L.G.J.5
  • 41
    • 18144424850 scopus 로고    scopus 로고
    • Effects of methanol on the catalytic properties of porcine pancreatic lipase
    • 1:CAS:528:DC%2BD2MXltFShtLo%3D
    • Park H, Lee KS, Chi YM, Jeong SW (2005) Effects of methanol on the catalytic properties of porcine pancreatic lipase. J Microbiol Biotechnol 15:296-301
    • (2005) J Microbiol Biotechnol , vol.15 , pp. 296-301
    • Park, H.1    Lee, K.S.2    Chi, Y.M.3    Jeong, S.W.4
  • 42
    • 0027158657 scopus 로고
    • Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria
    • 10.1016/0378-1119(93)90611-6 1:CAS:528:DyaK3sXktVWqtbo%3D
    • Quandt J, Hynes MF (1993) Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria. Gene 127:15-21
    • (1993) Gene , vol.127 , pp. 15-21
    • Quandt, J.1    Hynes, M.F.2
  • 43
    • 13244290008 scopus 로고    scopus 로고
    • A novel lipase/chaperone pair from Ralstonia sp M1: Analysis of the folding interaction and evidence for gene loss in R. solanacearum
    • 10.1007/s00438-004-1084-7 1:CAS:528:DC%2BD2MXmsVOqtQ%3D%3D
    • Quyen DT, Nguyen TT, Le TTG, Kim HK, Oh TK, Lee JK (2004) A novel lipase/chaperone pair from Ralstonia sp M1: analysis of the folding interaction and evidence for gene loss in R. solanacearum. Mol Genet Genomics 272:538-549
    • (2004) Mol Genet Genomics , vol.272 , pp. 538-549
    • Quyen, D.T.1    Nguyen, T.T.2    Le, T.T.G.3    Kim, H.K.4    Oh, T.K.5    Lee, J.K.6
  • 44
    • 10644239260 scopus 로고    scopus 로고
    • High level heterologous expression and properties of a novel lipase from Ralstonia sp M1
    • 10.1016/j.pep.2004.10.001 1:CAS:528:DC%2BD2cXhtVKltb3N
    • Quyen DT, Le TTG, Nguyen TT, Oh TK, Lee JK (2005) High level heterologous expression and properties of a novel lipase from Ralstonia sp M1. Protein Expression Purif 39:97-106
    • (2005) Protein Expression Purif , vol.39 , pp. 97-106
    • Quyen, D.T.1    Le, T.T.G.2    Nguyen, T.T.3    Oh, T.K.4    Lee, J.K.5
  • 45
    • 0034823470 scopus 로고    scopus 로고
    • A novel alkaline lipase from Burkholderia cepacia for detergent formulation
    • 10.1016/S0032-9592(01)00200-X 1:CAS:528:DC%2BD3MXlsFyksbc%3D
    • Rathi P, Saxena RK, Gupta R (2001) A novel alkaline lipase from Burkholderia cepacia for detergent formulation. Process Biochem 37:187-192
    • (2001) Process Biochem , vol.37 , pp. 187-192
    • Rathi, P.1    Saxena, R.K.2    Gupta, R.3
  • 47
    • 81455154482 scopus 로고    scopus 로고
    • Production of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) by Ralstonia eutropha in high cell density palm oil fermentations
    • 10.1002/bit.23283 1:CAS:528:DC%2BC3MXhsVOitr%2FL
    • Riedel SL, Bader J, Brigham CJ, Budde CF, Yusof ZAM, Rha C, Sinskey AJ (2012) Production of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) by Ralstonia eutropha in high cell density palm oil fermentations. Biotechnol Bioeng 109:74-83
    • (2012) Biotechnol Bioeng , vol.109 , pp. 74-83
    • Riedel, S.L.1    Bader, J.2    Brigham, C.J.3    Budde, C.F.4    Yusof, Z.A.M.5    Rha, C.6    Sinskey, A.J.7
  • 48
    • 0033646651 scopus 로고    scopus 로고
    • Bacterial lipases from Pseudomonas: Regulation of gene expression and mechanisms of secretion
    • 10.1016/S0300-9084(00)01182-2 1:CAS:528:DC%2BD3cXovFagsr8%3D
    • Rosenau F, Jaeger KE (2000) Bacterial lipases from Pseudomonas: regulation of gene expression and mechanisms of secretion. Biochimie 82:1023-1032
    • (2000) Biochimie , vol.82 , pp. 1023-1032
    • Rosenau, F.1    Jaeger, K.E.2
  • 49
    • 0033647281 scopus 로고    scopus 로고
    • Staphylococcal lipases: Biochemical and molecular characterization
    • 10.1016/S0300-9084(00)01180-9 1:CAS:528:DC%2BD3cXovFahu7c%3D
    • Rosenstein R, Gotz F (2000) Staphylococcal lipases: biochemical and molecular characterization. Biochimie 82:1005-1014
    • (2000) Biochimie , vol.82 , pp. 1005-1014
    • Rosenstein, R.1    Gotz, F.2
  • 50
    • 0033546322 scopus 로고    scopus 로고
    • Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest
    • 10.1074/jbc.274.24.16995 1:CAS:528:DyaK1MXjvVGktLY%3D
    • Roussel A, Canaan S, Egloff MP, Riviere M, Dupuis L, Verger R, Cambillau C (1999) Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. J Biol Chem 274:16995-17002
    • (1999) J Biol Chem , vol.274 , pp. 16995-17002
    • Roussel, A.1    Canaan, S.2    Egloff, M.P.3    Riviere, M.4    Dupuis, L.5    Verger, R.6    Cambillau, C.7
  • 51
    • 0037023903 scopus 로고    scopus 로고
    • Engineering of baker's yeasts, E. coli and Bacillus hosts for the production of Bacillus subtilis lipase A
    • 10.1002/bit.10201 1:CAS:528:DC%2BD38XjslSns78%3D
    • Sanchez M, Prim N, Randez-Gil F, Pastor FI, Diaz P (2002) Engineering of baker's yeasts, E. coli and Bacillus hosts for the production of Bacillus subtilis lipase A. Biotechnol Bioeng 78:339-345
    • (2002) Biotechnol Bioeng , vol.78 , pp. 339-345
    • Sanchez, M.1    Prim, N.2    Randez-Gil, F.3    Pastor, F.I.4    Diaz, P.5
  • 52
    • 0030874881 scopus 로고    scopus 로고
    • Lipases and alpha/beta hydrolase fold
    • 10.1016/S0076-6879(97)84006-2 1:CAS:528:DyaK2sXntFamtLc%3D
    • Schrag JD, Cygler M (1997) Lipases and alpha/beta hydrolase fold. Methods Enzymol 284:85-107
    • (1997) Methods Enzymol , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 53
    • 79952534187 scopus 로고    scopus 로고
    • Continuous lipase-catalyzed production of esters from crude high-oleic sunflower oil
    • 10.1016/j.biortech.2011.01.041 1:CAS:528:DC%2BC3MXjtFKqu7s%3D
    • Severac E, Galy O, Turon F, Monsan P, Marty A (2011) Continuous lipase-catalyzed production of esters from crude high-oleic sunflower oil. Bioresour Technol 102:4954-4961
    • (2011) Bioresour Technol , vol.102 , pp. 4954-4961
    • Severac, E.1    Galy, O.2    Turon, F.3    Monsan, P.4    Marty, A.5
  • 54
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic-engineering - Transposon mutagenesis in gram negative bacteria
    • 10.1038/nbt1183-784 1:CAS:528:DyaL2cXotVCqsg%3D%3D
    • Simon R, Priefer U, Puhler A (1983) A broad host range mobilization system for in vivo genetic-engineering - transposon mutagenesis in gram negative bacteria. Bio-Technology 1:784-791
    • (1983) Bio-Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 56
    • 70349754301 scopus 로고    scopus 로고
    • Biodiesel production through the use of different sources and characterization of oils and their esters as the substitute of diesel: A review
    • 10.1016/j.rser.2009.07.017 1:CAS:528:DC%2BD1MXht1eiu7nK
    • Singh SP, Singh D (2010) Biodiesel production through the use of different sources and characterization of oils and their esters as the substitute of diesel: a review. Renewable Sustainable Energy Rev 14:200-216
    • (2010) Renewable Sustainable Energy Rev , vol.14 , pp. 200-216
    • Singh, S.P.1    Singh, D.2
  • 57
    • 0026710269 scopus 로고
    • Surfactant interference on lipase catalyzed-reactions in microemulsions
    • 10.1002/jctb.280540311 1:CAS:528:DyaK38XlsVKnsLw%3D
    • Skagerlind P, Jansson M, Hult K (1992) Surfactant interference on lipase catalyzed-reactions in microemulsions. J Chem Technol Biotechnol 54:277-282
    • (1992) J Chem Technol Biotechnol , vol.54 , pp. 277-282
    • Skagerlind, P.1    Jansson, M.2    Hult, K.3
  • 58
    • 0031923063 scopus 로고    scopus 로고
    • Multiple beta-ketothiolases mediate poly(beta-hydroxyalkanoate) copolymer synthesis in Ralstonia eutropha
    • 1:CAS:528:DyaK1cXisVCgsLw%3D
    • Slater S, Houmiel KL, Tran M, Mitsky TA, Taylor NB, Padgette SR, Gruys KJ (1998) Multiple beta-ketothiolases mediate poly(beta-hydroxyalkanoate) copolymer synthesis in Ralstonia eutropha. J Bacteriol 180:1979-1987
    • (1998) J Bacteriol , vol.180 , pp. 1979-1987
    • Slater, S.1    Houmiel, K.L.2    Tran, M.3    Mitsky, T.A.4    Taylor, N.B.5    Padgette, S.R.6    Gruys, K.J.7
  • 60
    • 0035946913 scopus 로고    scopus 로고
    • The crystal structure of Bacillus subtilis lipase: A minimal alpha/beta hydrolase fold enzyme
    • 10.1006/jmbi.2001.4659
    • van Pouderoyen G, Eggert T, Jaeger KE, Dijkstra BW (2001) The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme. J Mol Biol 309:215-226
    • (2001) J Mol Biol , vol.309 , pp. 215-226
    • Van Pouderoyen, G.1    Eggert, T.2    Jaeger, K.E.3    Dijkstra, B.W.4
  • 61
    • 0019328522 scopus 로고
    • Methylation of histidine 48 in pancreatic phospholipase-A2 - Role of histidine and calcium ion in the catalytic mechanism
    • 10.1021/bi00545a021 1:CAS:528:DyaL3cXhtVKnuro%3D
    • Verheij HM, Volwerk JJ, Jansen EHJM, Puyk WC, Dijkstra BW, Drenth J, Dehaas GH (1980) Methylation of histidine 48 in pancreatic phospholipase-A2 - role of histidine and calcium ion in the catalytic mechanism. Biochemistry 19:743-750
    • (1980) Biochemistry , vol.19 , pp. 743-750
    • Verheij, H.M.1    Volwerk, J.J.2    Jansen, E.3    Puyk, W.C.4    Dijkstra, B.W.5    Drenth, J.6    Dehaas, G.H.7
  • 62
    • 77952768347 scopus 로고    scopus 로고
    • Molecular dynamics studies on T1 lipase: Insight into a double-flap mechanism
    • 10.1021/ci900458u
    • Wang Y, Wei DQ, Wang JF (2007) Molecular dynamics studies on T1 lipase: insight into a double-flap mechanism. J Chem Inf Model 50:875-878
    • (2007) J Chem Inf Model , vol.50 , pp. 875-878
    • Wang, Y.1    Wei, D.Q.2    Wang, J.F.3
  • 64
    • 0035078527 scopus 로고    scopus 로고
    • New insight into the role of the PhaP phasin of Ralstonia eutropha in promoting synthesis of polyhydroxybutyrate
    • 10.1128/JB.183.7.2394-2397.2001 1:CAS:528:DC%2BD3MXitFWrs7w%3D
    • York GM, Stubbe J, Sinskey AJ (2001) New insight into the role of the PhaP phasin of Ralstonia eutropha in promoting synthesis of polyhydroxybutyrate. J Bacteriol 183:2394-2397
    • (2001) J Bacteriol , vol.183 , pp. 2394-2397
    • York, G.M.1    Stubbe, J.2    Sinskey, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.