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Volumn 100, Issue 3, 2016, Pages 1265-1273

Mutations improving production and secretion of extracellular lipase by Burkholderia glumae PG1

Author keywords

Burkholderia glumae; Enzyme production; Lipase; Secretion

Indexed keywords

BIODEGRADATION; ESCHERICHIA COLI; GENES; PEPTIDES; PHOSPHATASES; PHYSIOLOGY;

EID: 84955181445     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-015-7041-z     Document Type: Article
Times cited : (16)

References (78)
  • 2
    • 2742517966 scopus 로고    scopus 로고
    • Optically active amines via lipase-catalyzed methoxyacetylation
    • Balkenhohl F, Ditrich K, Hauer B, Ladner W (1997) Optically active amines via lipase-catalyzed methoxyacetylation. J Prak Chem-Chem Ztg 339:381–384. doi:10.1002/prac.19973390166
    • (1997) J Prak Chem-Chem Ztg , vol.339 , pp. 381-384
    • Balkenhohl, F.1    Ditrich, K.2    Hauer, B.3    Ladner, W.4
  • 8
    • 33744827981 scopus 로고    scopus 로고
    • Burkholderia cepacia complex species: health hazards and biotechnological potential
    • PID: 16684604
    • Chiarini L, Bevivino A, Dalmastri C, Tabacchioni S, Visca P (2006) Burkholderia cepacia complex species: health hazards and biotechnological potential. Trends Microbiol 14:277–286. doi:10.1016/j.tim.2006.04.006
    • (2006) Trends Microbiol , vol.14 , pp. 277-286
    • Chiarini, L.1    Bevivino, A.2    Dalmastri, C.3    Tabacchioni, S.4    Visca, P.5
  • 9
    • 67649404857 scopus 로고    scopus 로고
    • The quorum sensing-dependent gene katG of Burkholderia glumae is important for protection from visible light
    • PID: 19395481
    • Chun H, Choi O, Goo E, Kim N, Kim H, Kang Y, Kim J, Moon JS, Hwang I (2009) The quorum sensing-dependent gene katG of Burkholderia glumae is important for protection from visible light. J Bacteriol 191:4152–4157. doi:10.1128/Jb.00227-09
    • (2009) J Bacteriol , vol.191 , pp. 4152-4157
    • Chun, H.1    Choi, O.2    Goo, E.3    Kim, N.4    Kim, H.5    Kang, Y.6    Kim, J.7    Moon, J.S.8    Hwang, I.9
  • 11
    • 81255136999 scopus 로고    scopus 로고
    • Characterization of rhamnolipid production by Burkholderia glumae
    • PID: 21933203
    • Costa SGVAO, Deziel E, Lepine F (2011) Characterization of rhamnolipid production by Burkholderia glumae. Lett Appl Microbiol 53:620–627. doi:10.1111/j.1472-765X.2011.03154.x
    • (2011) Lett Appl Microbiol , vol.53 , pp. 620-627
    • Costa, S.G.V.A.O.1    Deziel, E.2    Lepine, F.3
  • 12
    • 34547770722 scopus 로고    scopus 로고
    • Involvement of a quorum-sensing-regulated lipase secreted by a clinical isolate of Burkholderia glumae in severe disease symptoms in rice
    • Devescovi G, Bigirimana J, Degrassi G, Cabrio L, LiPuma JJ, Kim J, Hwang I, Venturi V (2007) Involvement of a quorum-sensing-regulated lipase secreted by a clinical isolate of Burkholderia glumae in severe disease symptoms in rice. Appl Environ Microb 73:4950–4958. doi:10.1128/Aem.00105-07
    • (2007) Appl Environ Microb , vol.73 , pp. 4950-4958
    • Devescovi, G.1    Bigirimana, J.2    Degrassi, G.3    Cabrio, L.4    LiPuma, J.J.5    Kim, J.6    Hwang, I.7    Venturi, V.8
  • 14
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • PID: 18078384
    • Driessen AJ, Nouwen N (2008) Protein translocation across the bacterial cytoplasmic membrane. Annu Rev Biochem 77:643–667. doi:10.1146/annurev.biochem.77.061606.160747
    • (2008) Annu Rev Biochem , vol.77 , pp. 643-667
    • Driessen, A.J.1    Nouwen, N.2
  • 16
    • 0034282656 scopus 로고    scopus 로고
    • Role of the lipase-specific foldase of Burkholderia glumae as a steric chaperone
    • PID: 10859310
    • El Khattabi M, Van Gelder P, Bitter W, Tommassen J (2000) Role of the lipase-specific foldase of Burkholderia glumae as a steric chaperone. J Biol Chem 275:26885–26891. doi:10.1074/jbc.M003258200
    • (2000) J Biol Chem , vol.275 , pp. 26885-26891
    • El Khattabi, M.1    Van Gelder, P.2    Bitter, W.3    Tommassen, J.4
  • 17
    • 8844269404 scopus 로고    scopus 로고
    • The underlying mechanisms of type II protein secretion
    • Filloux A (2004) The underlying mechanisms of type II protein secretion. Bba-Mol Cell Res 1694:163–179. doi:10.1016/j.bbamcr.2004.05.003
    • (2004) Bba-Mol Cell Res , vol.1694 , pp. 163-179
    • Filloux, A.1
  • 18
    • 84955180629 scopus 로고    scopus 로고
    • Methods Mol Biol
    • Springer, New York, NY
    • Filloux A, Ramos (Eds.) JL (2014) Pseudomonas methods and protocols vol 1149. Methods Mol Biol. Springer, New York, NY
    • (2014)
    • Filloux, A.1
  • 19
    • 84955183858 scopus 로고    scopus 로고
    • Freedonia (2014) World Enzymes Market. Accessed July 2014
    • Freedonia (2014) World Enzymes Market. http://www.reportlinker.com/p0747897/World-Enzymes-Industry.html. Accessed July 2014
  • 20
    • 0027220383 scopus 로고
    • An accessory gene, lipB, required for the production of active Pseudomonas glumae lipase
    • PID: 8412704
    • 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. doi:10.1111/j.1365-2958.1993.tb01718.x
    • (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
  • 21
    • 0027182430 scopus 로고
    • Role of the lipB gene-product in the folding of the secreted lipase of Pseudomonas glumae
    • PID: 8412705
    • 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. doi:10.1111/j.1365-2958.1993.tb01719.x
    • (1993) Mol Microbiol , vol.9 , pp. 591-599
    • Frenken, L.G.J.1    Degroot, A.2    Tommassen, J.3    Verrips, C.T.4
  • 24
    • 77954601007 scopus 로고    scopus 로고
    • Proteomic analysis of quorum sensing-dependent proteins in Burkholderia glumae
    • PID: 20408571
    • Goo E, Kang Y, Kim H, Hwang I (2010) Proteomic analysis of quorum sensing-dependent proteins in Burkholderia glumae. J Proteome Res 9:3184–3199. doi:10.1021/Pr100045n
    • (2010) J Proteome Res , vol.9 , pp. 3184-3199
    • Goo, E.1    Kang, Y.2    Kim, H.3    Hwang, I.4
  • 25
    • 0025295967 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants
    • PID: 2162051
    • Grant SGN, Jessee J, Bloom FR, Hanahan D (1990) Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants. Proc Natl Acad Sci U S A 87:4645–4649. doi:10.1073/pnas.87.12.4645
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 4645-4649
    • Grant, S.G.N.1    Jessee, J.2    Bloom, F.R.3    Hanahan, D.4
  • 26
    • 3142773489 scopus 로고    scopus 로고
    • Bacterial lipases: an overview of production, purification and biochemical properties
    • PID: 14966663
    • Gupta R, Gupta N, Rathi P (2004) Bacterial lipases: an overview of production, purification and biochemical properties. Appl Microbiol Biotechnol 64:763–781. doi:10.1007/s00253-004-1568-8
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 763-781
    • Gupta, R.1    Gupta, N.2    Rathi, P.3
  • 27
    • 79953284743 scopus 로고    scopus 로고
    • Burkholderia glumae: next major pathogen of rice?
    • PID: 21453428
    • Ham JH, Melanson RA, Rush MC (2011) Burkholderia glumae: next major pathogen of rice? Mol Plant Pathol 12:329–339. doi:10.1111/j.1364-3703.2010.00676.x
    • (2011) Mol Plant Pathol , vol.12 , pp. 329-339
    • Ham, J.H.1    Melanson, R.A.2    Rush, M.C.3
  • 28
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • PID: 6345791
    • Hanahan D (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166:557–580. doi:10.1016/S0022-2836(83)80284-8
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 29
    • 33747518326 scopus 로고    scopus 로고
    • Industrial applications of microbial lipases
    • Hasan F, Shah AA, Hameed A (2006) Industrial applications of microbial lipases. Enzyme Microb Tech 39:235–251. doi:10.1016/j.enzmictec.2005.10.016
    • (2006) Enzyme Microb Tech , vol.39 , pp. 235-251
    • Hasan, F.1    Shah, A.A.2    Hameed, A.3
  • 30
    • 0023684064 scopus 로고
    • A general-method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions
    • PID: 3045756
    • Higuchi R, Krummel B, Saiki RK (1988) A general-method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res 16:7351–7367. doi:10.1093/nar/16.15.7351
    • (1988) Nucleic Acids Res , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 31
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • PID: 10547694
    • Jaeger K-E, Dijkstra BW, Reetz MT (1999) Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu Rev Microbiol 53:315–351. doi:10.1146/annurev.micro.53.1.315
    • (1999) Annu Rev Microbiol , vol.53 , pp. 315-351
    • Jaeger, K.-E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 32
    • 0036669425 scopus 로고    scopus 로고
    • Lipases for biotechnology
    • PID: 12323363
    • Jaeger K-E, Eggert T (2002) Lipases for biotechnology. Curr Opin Biotechnol 13:390–397. doi:10.1016/S0958-1669(02)00341-5
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 390-397
    • Jaeger, K.-E.1    Eggert, T.2
  • 34
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • PID: 9744114
    • Jaeger K-E, Reetz MT (1998) Microbial lipases form versatile tools for biotechnology. Trends Biotechnol 16:396–403. doi:10.1016/S0167-7799(98)01195-0
    • (1998) Trends Biotechnol , vol.16 , pp. 396-403
    • Jaeger, K.-E.1    Reetz, M.T.2
  • 35
    • 0043126983 scopus 로고    scopus 로고
    • Toxoflavin produced by Burkholderia glumae causing rice grain rot is responsible for inducing bacterial wilt in many field crops
    • Jeong Y, Kim J, Kim S, Kang Y, Nagamatsu T, Hwang I (2003) Toxoflavin produced by Burkholderia glumae causing rice grain rot is responsible for inducing bacterial wilt in many field crops. Plant Dis 87:890–895. doi:10.1094/PDIS.2003.87.8.890
    • (2003) Plant Dis , vol.87 , pp. 890-895
    • Jeong, Y.1    Kim, J.2    Kim, S.3    Kang, Y.4    Nagamatsu, T.5    Hwang, I.6
  • 37
    • 38149077393 scopus 로고    scopus 로고
    • Proteomic analysis of the proteins regulated by HrpB from the plant pathogenic bacterium Burkholderia glumae
    • PID: 18050277
    • Kang Y, Kim J, Kim S, Kim H, Lim JY, Kim M, Kwak J, Moon JS, Hwang I (2008) Proteomic analysis of the proteins regulated by HrpB from the plant pathogenic bacterium Burkholderia glumae. Proteomics 8:106–121. doi:10.1002/pmic.200700244
    • (2008) Proteomics , vol.8 , pp. 106-121
    • Kang, Y.1    Kim, J.2    Kim, S.3    Kim, H.4    Lim, J.Y.5    Kim, M.6    Kwak, J.7    Moon, J.S.8    Hwang, I.9
  • 38
    • 84863232637 scopus 로고    scopus 로고
    • Regulation of universal stress protein genes by quorum sensing and RpoS in Burkholderia glumae
    • PID: 22178971
    • Kim H, Goo E, Kang Y, Kim J, Hwang I (2012) Regulation of universal stress protein genes by quorum sensing and RpoS in Burkholderia glumae. J Bacteriol 194:982–992. doi:10.1128/Jb.06396-11
    • (2012) J Bacteriol , vol.194 , pp. 982-992
    • Kim, H.1    Goo, E.2    Kang, Y.3    Kim, J.4    Hwang, I.5
  • 39
    • 33947260668 scopus 로고    scopus 로고
    • Regulation of polar flagellum genes is mediated by quorum sensing and FlhDC in Burkholderia glumae
    • PID: 17376080
    • Kim J, Kang Y, Choi O, Jeong Y, Jeong JE, Lim JY, Kim M, Moon JS, Suga H, Hwang I (2007) Regulation of polar flagellum genes is mediated by quorum sensing and FlhDC in Burkholderia glumae. Mol Microbiol 64:165–179. doi:10.1111/j.1365-2958.2007.05646.x
    • (2007) Mol Microbiol , vol.64 , pp. 165-179
    • Kim, J.1    Kang, Y.2    Choi, O.3    Jeong, Y.4    Jeong, J.E.5    Lim, J.Y.6    Kim, M.7    Moon, J.S.8    Suga, H.9    Hwang, I.10
  • 40
    • 8544231380 scopus 로고    scopus 로고
    • Quorum sensing and the LysR-type transcriptional activator ToxR regulate toxoflavin biosynthesis and transport in Burkholderia glumae
    • PID: 15522077
    • Kim J, Kim JG, Kang Y, Jang JY, Jog GJ, Lim JY, Kim S, Suga H, Nagamatsu T, Hwang I (2004) Quorum sensing and the LysR-type transcriptional activator ToxR regulate toxoflavin biosynthesis and transport in Burkholderia glumae. Mol Microbiol 54:921–934. doi:10.1111/j.1365-2958.2004.04338.x
    • (2004) Mol Microbiol , vol.54 , pp. 921-934
    • Kim, J.1    Kim, J.G.2    Kang, Y.3    Jang, J.Y.4    Jog, G.J.5    Lim, J.Y.6    Kim, S.7    Suga, H.8    Nagamatsu, T.9    Hwang, I.10
  • 41
    • 84955203239 scopus 로고    scopus 로고
    • Physiologie eines industriellen Produktionsstammes: Proteinsekretion
    • Ph.D. thesis: Heinrich-Heine-University Duesseldorf
    • Knorr J (2010) Physiologie eines industriellen Produktionsstammes: Proteinsekretion, Regulation und Produktion von Biotensiden in Burkholderia glumae. Ph.D. thesis, Heinrich-Heine-University Duesseldorf
    • (2010) Regulation und Produktion von Biotensiden in Burkholderia glumae
    • Knorr, J.1
  • 43
    • 0036827458 scopus 로고    scopus 로고
    • Lipases and lipase-catalyzed esterification reactions in nonaqueous media
    • Krishna SH, Karanth NG (2002) Lipases and lipase-catalyzed esterification reactions in nonaqueous media. Catal Rev 44:499–591. doi:10.1081/Cr-120015481
    • (2002) Catal Rev , vol.44 , pp. 499-591
    • Krishna, S.H.1    Karanth, N.G.2
  • 44
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • PID: 7108955
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105–132. doi:10.1016/0022-2836(82)90515-0
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • PID: 5432063
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685. doi:10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 47
    • 33749180935 scopus 로고    scopus 로고
    • Functional expression of Candida antarctica lipase B in the Escherichia coli cytoplasm—a screening system for a frequently used biocatalyst
    • PID: 16703321
    • Liu D, Schmid RD, Rusnak M (2006) Functional expression of Candida antarctica lipase B in the Escherichia coli cytoplasm—a screening system for a frequently used biocatalyst. Appl Microbiol Biotechnol 72:1024–1032. doi:10.1007/s00253-006-0369-7
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 1024-1032
    • Liu, D.1    Schmid, R.D.2    Rusnak, M.3
  • 49
    • 0025095225 scopus 로고
    • Alkaline phosphatase fusions: sensors of subcellular location
    • PID: 2404939
    • Manoil C, Mekalanos JJ, Beckwith J (1990) Alkaline phosphatase fusions: sensors of subcellular location. J Bacteriol 172:515–518
    • (1990) J Bacteriol , vol.172 , pp. 515-518
    • Manoil, C.1    Mekalanos, J.J.2    Beckwith, J.3
  • 50
    • 84871920865 scopus 로고    scopus 로고
    • New tools for exploring “old friends-microbial lipases
    • Nagarajan S (2012) New tools for exploring “old friends-microbial lipases”. Appl Biochem Biotech 168:1163–1196. doi:10.1007/s12010-012-9849-7
    • (2012) Appl Biochem Biotech , vol.168 , pp. 1163-1196
    • Nagarajan, S.1
  • 51
    • 84874797447 scopus 로고    scopus 로고
    • Biodiesel production by transesterification using immobilized lipase
    • PID: 23247566
    • Narwal SK, Gupta R (2013) Biodiesel production by transesterification using immobilized lipase. Biotechnol Lett 35:479–490. doi:10.1007/s10529-012-1116-z
    • (2013) Biotechnol Lett , vol.35 , pp. 479-490
    • Narwal, S.K.1    Gupta, R.2
  • 52
    • 84871866528 scopus 로고    scopus 로고
    • Engineering signal peptides for enhanced protein secretion from Lactococcus lactis
    • PID: 23124224
    • Ng DT, Sarkar CA (2013) Engineering signal peptides for enhanced protein secretion from Lactococcus lactis. Appl Environ Microbiol 79:347–356. doi:10.1128/AEM.02667-12
    • (2013) Appl Environ Microbiol , vol.79 , pp. 347-356
    • Ng, D.T.1    Sarkar, C.A.2
  • 53
    • 28744445133 scopus 로고    scopus 로고
    • Active lactonizing lipase (LipL) efficiently overproduced by Pseudomonas strains as heterologous expression hosts
    • PID: 16243284
    • Omori K, Isoyama-Tanaka J, Ihara F, Yamada Y, Nihira T (2005) Active lactonizing lipase (LipL) efficiently overproduced by Pseudomonas strains as heterologous expression hosts. J Biosci Bioeng 100:323–330. doi:10.1263/jbb.100.323
    • (2005) J Biosci Bioeng , vol.100 , pp. 323-330
    • Omori, K.1    Isoyama-Tanaka, J.2    Ihara, F.3    Yamada, Y.4    Nihira, T.5
  • 54
    • 81755174137 scopus 로고    scopus 로고
    • Pathogenicity and biotechnological applications of the genus Burkholderia
    • Paganin P, Tabacchioni S, Chiarini L (2011) Pathogenicity and biotechnological applications of the genus Burkholderia. Cent Eur J Biol 6:997–1005. doi:10.2478/s11535-011-0072-2
    • (2011) Cent Eur J Biol , vol.6 , pp. 997-1005
    • Paganin, P.1    Tabacchioni, S.2    Chiarini, L.3
  • 55
    • 84871536584 scopus 로고    scopus 로고
    • Decoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stability
    • Pauwels K, Sanchez Del Pino MM, Feller G, Van Gelder P (2012) Decoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stability. PLoS One 7::e36999. doi:10.1371/journal.pone.0036999
    • (2012) PLoS One , vol.7 , pp. :e36999
    • Pauwels, K.1    Sanchez Del Pino, M.M.2    Feller, G.3    Van Gelder, P.4
  • 56
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson GL (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 83:346–356. doi:10.1016/0003-2697(77)90043-4
    • (1977) Anal Biochem , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 57
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl MW, Horgan GW, Dempfle L (2002) Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res 30:e36. doi: 10.1093/nar/30.9.e36
    • (2002) Nucleic Acids Res , vol.e36 , pp. 30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 58
    • 0033646651 scopus 로고    scopus 로고
    • Bacterial lipases from Pseudomonas: regulation of gene expression and mechanisms of secretion
    • PID: 11099799
    • Rosenau F, Jaeger K-E (2000) Bacterial lipases from Pseudomonas: regulation of gene expression and mechanisms of secretion. Biochimie 82:1023–1032. doi:10.1016/S0300-9084(00)01182-2
    • (2000) Biochimie , vol.82 , pp. 1023-1032
    • Rosenau, F.1    Jaeger, K.-E.2
  • 63
    • 84928791884 scopus 로고    scopus 로고
    • Comparative genome analysis of rice-pathogenic Burkholderia provides insight into capacity to adapt to different environments and hosts
    • PID: 25943361
    • Seo YS, Lim JY, Park J, Kim S, Lee HH, Cheong H, Kim SM, Moon JS, Hwang I (2015) Comparative genome analysis of rice-pathogenic Burkholderia provides insight into capacity to adapt to different environments and hosts. BMC Genomics 16:349. doi:10.1186/s12864-015-1558-5
    • (2015) BMC Genomics , vol.16 , pp. 349
    • Seo, Y.S.1    Lim, J.Y.2    Park, J.3    Kim, S.4    Lee, H.H.5    Cheong, H.6    Kim, S.M.7    Moon, J.S.8    Hwang, I.9
  • 64
    • 84896846308 scopus 로고    scopus 로고
    • Organic solvent tolerant lipases and applications
    • PID: 24672342
    • Sharma S, Kanwar SS (2014) Organic solvent tolerant lipases and applications. TheScientificWorldJOURNAL 2014:625258. doi:10.1155/2014/625258
    • (2014) TheScientificWorldJOURNAL , vol.2014 , pp. 625258
    • Sharma, S.1    Kanwar, S.S.2
  • 65
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic-engineering—transposon mutagenesis in Gram-negative bacteria
    • 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-Technol 1:784–791. doi:10.1038/nbt1183-784
    • (1983) Bio-Technol , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 66
    • 0030158571 scopus 로고    scopus 로고
    • The Staden sequence analysis package
    • PID: 8837029
    • Staden R (1996) The Staden sequence analysis package. Mol Biotechnol 5:233–241
    • (1996) Mol Biotechnol , vol.5 , pp. 233-241
    • Staden, R.1
  • 68
    • 3042826857 scopus 로고    scopus 로고
    • Molecular characterization of the tox operon involved in toxoflavin biosynthesis of Burkholderia glumae
    • Suzuki F, Sawada H, Azegami K, Tsuchiya K (2004) Molecular characterization of the tox operon involved in toxoflavin biosynthesis of Burkholderia glumae. J Gen Plant Pathol 70:97–107. doi:10.1007/s10327-003-0096-1
    • (2004) J Gen Plant Pathol , vol.70 , pp. 97-107
    • Suzuki, F.1    Sawada, H.2    Azegami, K.3    Tsuchiya, K.4
  • 70
    • 35348823779 scopus 로고    scopus 로고
    • Burkholderia diversity and versatility: an inventory of the extracellular products
    • Vial L, Groleau MC, Dekimpe V, Deziel E (2007) Burkholderia diversity and versatility: an inventory of the extracellular products. J Microbiol Biotechn 17:1407–1429
    • (2007) J Microbiol Biotechn , vol.17 , pp. 1407-1429
    • Vial, L.1    Groleau, M.C.2    Dekimpe, V.3    Deziel, E.4
  • 71
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli—partial purification and some properties
    • PID: 13278318
    • Vogel HJ, Bonner DM (1956) Acetylornithinase of Escherichia coli—partial purification and some properties. J Biol Chem 218:97–106
    • (1956) J Biol Chem , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 72
    • 84927514438 scopus 로고    scopus 로고
    • Complete genome sequence of the lipase producing strain Burkholderia glumae PG1
    • PID: 25848987
    • Voget S, Knapp A, Poehlein A, Vollstedt C, Streit WR, Daniel R, Jaeger K-E (2015) Complete genome sequence of the lipase producing strain Burkholderia glumae PG1. J Biotechnol 204:3–4. doi:10.1016/j.jbiotec.2015.03.022
    • (2015) J Biotechnol , vol.204 , pp. 3-4
    • Voget, S.1    Knapp, A.2    Poehlein, A.3    Vollstedt, C.4    Streit, W.R.5    Daniel, R.6    Jaeger, K.-E.7
  • 74
    • 0018399632 scopus 로고
    • Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens
    • PID: 222724
    • Winkler UK, Stuckmann M (1979) Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens. J Bacteriol 138:663–670
    • (1979) J Bacteriol , vol.138 , pp. 663-670
    • Winkler, U.K.1    Stuckmann, M.2
  • 75
    • 0027096070 scopus 로고
    • Proposal of Burkholderia genus and transfer of 7 species of the genus Pseudomonas homology group II to the new genus, with the type species Burkholderia cepacia (Palleroni and Holmes 1981)
    • PID: 1283774
    • Yabuuchi E, Kosako Y, Oyaizu H, Yano I, Hotta H, Hashimoto Y, Ezaki T, Arakawa M (1992) Proposal of Burkholderia genus and transfer of 7 species of the genus Pseudomonas homology group II to the new genus, with the type species Burkholderia cepacia (Palleroni and Holmes 1981). Microbiol Immunol 36:1251–1275. doi:10.1111/j.1348-0421.1992.tb02129.x
    • (1992) Microbiol Immunol , vol.36 , pp. 1251-1275
    • Yabuuchi, E.1    Kosako, Y.2    Oyaizu, H.3    Yano, I.4    Hotta, H.5    Hashimoto, Y.6    Ezaki, T.7    Arakawa, M.8
  • 76
    • 0032215111 scopus 로고    scopus 로고
    • Ester synthesis in lipase-catalyzed reactions
    • Yahya ARM, Anderson WA, Moo-Young M (1998) Ester synthesis in lipase-catalyzed reactions. Enzyme Microb Tech 23:438–450. doi:10.1016/S0141-0229(98)00065-9
    • (1998) Enzyme Microb Tech , vol.23 , pp. 438-450
    • Yahya, A.R.M.1    Anderson, W.A.2    Moo-Young, M.3
  • 77
    • 77952516669 scopus 로고    scopus 로고
    • Secretory production of recombinant proteins in Escherichia coli
    • PID: 20201800
    • Yoon SH, Kim SK, Kim JF (2010) Secretory production of recombinant proteins in Escherichia coli. Recent Patents on Biotechnology 4:23–29. doi:10.2174/187220810790069550
    • (2010) Recent Patents on Biotechnology , vol.4 , pp. 23-29
    • Yoon, S.H.1    Kim, S.K.2    Kim, J.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.