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Volumn 42, Issue 10, 2015, Pages 1309-1317

Yeast Kluyveromyces lactis as host for expression of the bacterial lipase: cloning and adaptation of the new lipase gene from Serratia sp

Author keywords

de novo synthesis; Kluyveromyces lactis; Lipase; Serratia sp; Whey

Indexed keywords

BACTERIAL ENZYME; POLYGALACTURONASE; SIGNAL PEPTIDE; TRIACYLGLYCEROL LIPASE; TRIOSEPHOSPHATE ISOMERASE; CODON; HYBRID PROTEIN; SOLYSIME;

EID: 84942371382     PISSN: 13675435     EISSN: 14765535     Source Type: Journal    
DOI: 10.1007/s10295-015-1655-0     Document Type: Article
Times cited : (10)

References (35)
  • 2
    • 0034213209 scopus 로고    scopus 로고
    • Heterologous expression of the Kluyveromyces marxianus endopolygalacturonase gene (EPG1) using versatile autonomously replicating vector for a wide range of host
    • COI: 1:CAS:528:DC%2BD3cXktFSjt7c%3D
    • Bartkeviciute D, Siekstele R, Sasnauskas K (2000) Heterologous expression of the Kluyveromyces marxianus endopolygalacturonase gene (EPG1) using versatile autonomously replicating vector for a wide range of host. Enzyme Microb Technol 26:653–656
    • (2000) Enzyme Microb Technol , vol.26 , pp. 653-656
    • Bartkeviciute, D.1    Siekstele, R.2    Sasnauskas, K.3
  • 4
    • 0032176521 scopus 로고    scopus 로고
    • Production of bioingredient from Kluyvervmyces marxianus grown on whey—an alternative
    • COI: 1:CAS:528:DyaK1cXnsVyktrk%3D, PID: 9813735
    • Belem MAF, Lee BH (1998) Production of bioingredient from Kluyvervmyces marxianus grown on whey—an alternative. Crit Rev Food Sci Nutr 38:565–598
    • (1998) Crit Rev Food Sci Nutr , vol.38 , pp. 565-598
    • Belem, M.A.F.1    Lee, B.H.2
  • 5
    • 0036773518 scopus 로고    scopus 로고
    • Optimizing lipases and related enzymes for efficient application
    • COI: 1:CAS:528:DC%2BD38XmvVWmtLg%3D, PID: 12220906
    • Bornscheuer UT, Bessler C, Srinivas R, Krishna SH (2002) Optimizing lipases and related enzymes for efficient application. Trends Biotechnol 20:433–437
    • (2002) Trends Biotechnol , vol.20 , pp. 433-437
    • Bornscheuer, U.T.1    Bessler, C.2    Srinivas, R.3    Krishna, S.H.4
  • 6
    • 84865232198 scopus 로고    scopus 로고
    • Production of recombinant proteins by yeast cells
    • COI: 1:CAS:528:DC%2BC38XhtF2hs7%2FO, PID: 21964262
    • Celik E, Calik P (2012) Production of recombinant proteins by yeast cells. Biotechnol Adv 30:1108–1118
    • (2012) Biotechnol Adv , vol.30 , pp. 1108-1118
    • Celik, E.1    Calik, P.2
  • 7
    • 32044463134 scopus 로고    scopus 로고
    • Kluyvemmyces lactis LAC4 promoter variants thai lack function in bacteria but retain full function in yeast
    • COI: 1:CAS:528:DC%2BD2MXht1ekurrK, PID: 16269745
    • Colussi PA, Taron ChH (2005) Kluyvemmyces lactis LAC4 promoter variants thai lack function in bacteria but retain full function in yeast. Appl Environ Microbiol 71:7092–7098
    • (2005) Appl Environ Microbiol , vol.71 , pp. 7092-7098
    • Colussi, P.A.1    Taron, C.H.2
  • 8
    • 0042694726 scopus 로고    scopus 로고
    • Production of a thermostable extracellular lipase by Kluyveromyces marxianus
    • COI: 1:CAS:528:DC%2BD3sXmtVenu7Y%3D, PID: 14514040
    • Deive FJ, Costas M, Longo MA (2003) Production of a thermostable extracellular lipase by Kluyveromyces marxianus. Biotechnol Lett 25(17):1403–1406
    • (2003) Biotechnol Lett , vol.25 , Issue.17 , pp. 1403-1406
    • Deive, F.J.1    Costas, M.2    Longo, M.A.3
  • 9
    • 21244431641 scopus 로고    scopus 로고
    • Single-step purification of lipase from Burkholderia multivorans using polypropylene matrix
    • COI: 1:CAS:528:DC%2BD2MXkvFSrtLk%3D, PID: 15711795
    • Gupta N, Rathi P, Singh R, Goswami VK, Gupta R (2005) Single-step purification of lipase from Burkholderia multivorans using polypropylene matrix. Appl Microbiol Biotechnol 67:648–653
    • (2005) Appl Microbiol Biotechnol , vol.67 , pp. 648-653
    • Gupta, N.1    Rathi, P.2    Singh, R.3    Goswami, V.K.4    Gupta, R.5
  • 10
    • 3142773489 scopus 로고    scopus 로고
    • Bacterial lipases: an overview of production, purification and biochemical properties
    • COI: 1:CAS:528:DC%2BD2cXktlyku7Y%3D, 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
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 763-781
    • Gupta, R.1    Gupta, N.2    Rathi, P.3
  • 11
    • 3042782585 scopus 로고    scopus 로고
    • Codon bias and heterologous protein expression
    • COI: 1:CAS:528:DC%2BD2cXls1Wktbc%3D, PID: 15245907
    • Gustafsson C, Govindarajan Sh, Minshull J (2004) Codon bias and heterologous protein expression. Trends Biotechnol 22:346–353
    • (2004) Trends Biotechnol , vol.22 , pp. 346-353
    • Gustafsson, C.1    Govindarajan, S.2    Minshull, J.3
  • 12
    • 33747518326 scopus 로고    scopus 로고
    • Industrial applications of microbial lipases
    • COI: 1:CAS:528:DC%2BD28XkslSksbc%3D
    • Hasan F, Shan F, Hameed A (2006) Industrial applications of microbial lipases. Enzyme Microb Tech 39:235–251
    • (2006) Enzyme Microb Tech , vol.39 , pp. 235-251
    • Hasan, F.1    Shan, F.2    Hameed, A.3
  • 13
    • 84975103885 scopus 로고    scopus 로고
    • http://openwetware.org/wiki/Composition_of_Yeast_Nitrogen_Base_(YNB)
  • 14
    • 1842846515 scopus 로고    scopus 로고
    • PCR Cloning protocols
    • Humana Press Inc, New York
    • Huang ShH, Wu HY, Jong AY (2002) PCR Cloning protocols. In: Chen BY, Janes HW (eds) 2nd edn. Humana Press Inc, New York, p 309–314
    • (2002) Chen BY, Janes HW , pp. 309-314
    • Huang, S.H.1    Wu, H.Y.2    Jong, A.Y.3    edn, E.4
  • 15
    • 0242557626 scopus 로고    scopus 로고
    • Production of heterologous microbial lipases by yeasts
    • COI: 1:CAS:528:DC%2BD3sXovVCrtLY%3D
    • Kademi A, Lee B, Houde A (2003) Production of heterologous microbial lipases by yeasts. Indian J Biotechnol 2:346–355
    • (2003) Indian J Biotechnol , vol.2 , pp. 346-355
    • Kademi, A.1    Lee, B.2    Houde, A.3
  • 16
    • 84901625368 scopus 로고    scopus 로고
    • A cleaner approach for biolubricant production using biodiesel as a starting material
    • Kleinaitė E, Jaška V, Tvaska B, Matijošytė I (2014) A cleaner approach for biolubricant production using biodiesel as a starting material. J Clean Prod 75:40–44
    • (2014) J Clean Prod , vol.75 , pp. 40-44
    • Kleinaitė, E.1    Jaška, V.2    Tvaska, B.3    Matijošytė, I.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • COI: 1:CAS:528:DC%2BD3MXlsFags7s%3D, PID: 5432063
    • 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
  • 18
    • 1542268883 scopus 로고    scopus 로고
    • Activity and stability of a crude lipase from Penicillium aurantiogriseum in aqueous media and organic solvents
    • COI: 1:CAS:528:DC%2BD2cXhvVygsLc%3D
    • Lima VMG, Krieger N, Mitchell DA, Fontana JD (2004) Activity and stability of a crude lipase from Penicillium aurantiogriseum in aqueous media and organic solvents. Biochem Eng J 18:65–71
    • (2004) Biochem Eng J , vol.18 , pp. 65-71
    • Lima, V.M.G.1    Krieger, N.2    Mitchell, D.A.3    Fontana, J.D.4
  • 20
    • 84888404570 scopus 로고    scopus 로고
    • Lipases produced by yeasts: powerful biocatalysts for industrial purposes
    • Lock LL, Corbellini AV, Valente P (2007) Lipases produced by yeasts: powerful biocatalysts for industrial purposes. Techno-Logica 11:18–25
    • (2007) Techno-Logica , vol.11 , pp. 18-25
    • Lock, L.L.1    Corbellini, A.V.2    Valente, P.3
  • 22
    • 84911913403 scopus 로고    scopus 로고
    • Comparative expression of lipase CAL-A in the yeasts Saccharomyces cerevisiae, Kluyveromyces lactis and Hansenula polymorpha to investigate a possible host influence
    • COI: 1:CAS:528:DC%2BC2cXhsVOmsrjL, PID: 25172438
    • Morka K, Pietruszka J, Meyer zu Berstenhorsta S (2014) Comparative expression of lipase CAL-A in the yeasts Saccharomyces cerevisiae, Kluyveromyces lactis and Hansenula polymorpha to investigate a possible host influence. J Biotechnol 191:176–186
    • (2014) J Biotechnol , vol.191 , pp. 176-186
    • Morka, K.1    Pietruszka, J.2    Meyer zu Berstenhorsta, S.3
  • 23
    • 0031657285 scopus 로고    scopus 로고
    • Comparison of expression systems in the yeasts Saccharomyces cerevisiae, Hansenula polymorpha, Klyveromyces lactis, Schizosaccharomyces pombe and Yarrowia lipolytica
    • COI: 1:CAS:528:DyaK1cXmslKntbs%3D, PID: 9802206
    • Muller S, Sandal Th, Kamp-Hansen P, Dalboge H (1998) Comparison of expression systems in the yeasts Saccharomyces cerevisiae, Hansenula polymorpha, Klyveromyces lactis, Schizosaccharomyces pombe and Yarrowia lipolytica. Yeast 14:1267–1283
    • (1998) Yeast , vol.14 , pp. 1267-1283
    • Muller, S.1    Sandal, T.2    Kamp-Hansen, P.3    Dalboge, H.4
  • 24
    • 34249857539 scopus 로고    scopus 로고
    • Cobalt: constraint-based alignment tool for multiple protein sequences
    • COI: 1:CAS:528:DC%2BD2sXmtVKqur0%3D, PID: 17332019
    • Papadopoulos JS, Agarwala R (2007) Cobalt: constraint-based alignment tool for multiple protein sequences. Bioinformatics 23:1073–1079
    • (2007) Bioinformatics , vol.23 , pp. 1073-1079
    • Papadopoulos, J.S.1    Agarwala, R.2
  • 26
    • 38449094836 scopus 로고    scopus 로고
    • Purification and characterization of two highly thermophilic alkaline lipases from Thermosyntropha lipolytica
    • COI: 1:CAS:528:DC%2BD2sXhsVeisLrI, PID: 17933930
    • Salameh MA, Wiegel J (2007) Purification and characterization of two highly thermophilic alkaline lipases from Thermosyntropha lipolytica. Appl Environ Microbiol 73:7725–7731
    • (2007) Appl Environ Microbiol , vol.73 , pp. 7725-7731
    • Salameh, M.A.1    Wiegel, J.2
  • 28
    • 84856021987 scopus 로고    scopus 로고
    • Combinatorial reshaping of the Candida antarctica lipase. A substrate pocket for enantioselectivity using an extremely condensed library
    • PID: 22178758
    • Sandström AG, Wikmark Y, Engström K, Nyhlén J, Bäckvall JE (2012) Combinatorial reshaping of the Candida antarctica lipase. A substrate pocket for enantioselectivity using an extremely condensed library. Proc Nat Acad Sci USA 109:78–83
    • (2012) Proc Nat Acad Sci USA , vol.109 , pp. 78-83
    • Sandström, A.G.1    Wikmark, Y.2    Engström, K.3    Nyhlén, J.4    Bäckvall, J.E.5
  • 29
    • 84869132049 scopus 로고    scopus 로고
    • Experimental investigation and optimization of process variables affecting the production of extracellular lipase by Kluyveromyces marxianus IFO 0288
    • COI: 1:CAS:528:DC%2BC38XhsFSgtL%2FL, PID: 22843062
    • Stergiou PY, Foukis A, Sklivaniti H, Zacharaki P, Papagianni M, Papamichael EM (2012) Experimental investigation and optimization of process variables affecting the production of extracellular lipase by Kluyveromyces marxianus IFO 0288. Appl Biochem Biotechnol 168(3):672–680
    • (2012) Appl Biochem Biotechnol , vol.168 , Issue.3 , pp. 672-680
    • Stergiou, P.Y.1    Foukis, A.2    Sklivaniti, H.3    Zacharaki, P.4    Papagianni, M.5    Papamichael, E.M.6
  • 31
    • 32044435832 scopus 로고    scopus 로고
    • Yeast lipases: enzyme purification, biochemical properties and gene cloning
    • COI: 1:CAS:528:DC%2BD28XltVent70%3D
    • Vakhlu J, Kour A (2006) Yeast lipases: enzyme purification, biochemical properties and gene cloning. J Biotechnol 9:69–85
    • (2006) J Biotechnol , vol.9 , pp. 69-85
    • Vakhlu, J.1    Kour, A.2
  • 32
    • 0034467679 scopus 로고    scopus 로고
    • RTX toxin structure and function: a story of numerous anomalies and few analogies in toxin biology
    • COI: 1:CAS:528:DC%2BD3MXjvVyns7c%3D, PID: 11417123
    • Welch RA (2001) RTX toxin structure and function: a story of numerous anomalies and few analogies in toxin biology. Curr Top Microbiol Immunol 257:85–111
    • (2001) Curr Top Microbiol Immunol , vol.257 , pp. 85-111
    • Welch, R.A.1
  • 33
    • 0018399632 scopus 로고
    • Glycogen, hyaluronate, and some other polysaccharides greatly exhance the formation of exolipase by Serratia marcescens
    • COI: 1:CAS:528:DyaE1MXkvVCjtb4%3D, PID: 222724
    • Winkler UK, Stuckmann M (1979) Glycogen, hyaluronate, and some other polysaccharides greatly exhance 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
  • 34
    • 42449114153 scopus 로고    scopus 로고
    • Isolation of a novel lipase gene from Serratia liquefaciens S33 DB-1, functional expression in Pichia pastoris and its properties
    • COI: 1:CAS:528:DC%2BD1cXisFyhurY%3D, PID: 18219590
    • Yao H, Yu S, Zhang L, Zuo K, Ling H, Zhang F, Tang K (2008) Isolation of a novel lipase gene from Serratia liquefaciens S33 DB-1, functional expression in Pichia pastoris and its properties. Mol Biotechnol 38(2):99–107
    • (2008) Mol Biotechnol , vol.38 , Issue.2 , pp. 99-107
    • Yao, H.1    Yu, S.2    Zhang, L.3    Zuo, K.4    Ling, H.5    Zhang, F.6    Tang, K.7
  • 35
    • 84902302687 scopus 로고    scopus 로고
    • Recombinant Kluyveromyces lactis expressing highly pathogenic porcine reproductive and respiratory syndrome virus GP5 elicits mucosal and cell-mediated immune responses in mice
    • PID: 24378591
    • Zhao H, Wang Y, Ma Z, Wang Y, Feng W (2014) Recombinant Kluyveromyces lactis expressing highly pathogenic porcine reproductive and respiratory syndrome virus GP5 elicits mucosal and cell-mediated immune responses in mice. J Vet Sci 15(2):199–208
    • (2014) J Vet Sci , vol.15 , Issue.2 , pp. 199-208
    • Zhao, H.1    Wang, Y.2    Ma, Z.3    Wang, Y.4    Feng, W.5


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