메뉴 건너뛰기




Volumn 66, Issue 7, 2000, Pages 3113-3116

Screening of environmental DNA libraries for the presence of genes conferring lipolytic activity on Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ESTERASE; TRIACYLGLYCEROL LIPASE; TRIBUTYRIN;

EID: 0033916660     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.7.3113-3116.2000     Document Type: Article
Times cited : (246)

References (26)
  • 1
    • 85046520109 scopus 로고
    • Esterase from the oil-degrading Acinetobacter lwoffii RAG-1: Sequence analysis and over-expression in Escherichia coli
    • Alon, R. N., and D. L. Gutnick. 1993. Esterase from the oil-degrading Acinetobacter lwoffii RAG-1: sequence analysis and over-expression in Escherichia coli. FEMS Microbiol. Lett. 112:275-280.
    • (1993) FEMS Microbiol. Lett. , vol.112 , pp. 275-280
    • Alon, R.N.1    Gutnick, D.L.2
  • 3
    • 0028946084 scopus 로고
    • Phylogenetic identification and in situ detection of individual microbial cells without cultivation
    • Amann, R. I., W. Ludwig, and K. H. Schleifer. 1995. Phylogenetic identification and in situ detection of individual microbial cells without cultivation. Microbiol. Rev. 59:143-169.
    • (1995) Microbiol. Rev. , vol.59 , pp. 143-169
    • Amann, R.I.1    Ludwig, W.2    Schleifer, K.H.3
  • 4
    • 0032189604 scopus 로고    scopus 로고
    • A novel heat-stable lipolytic enzyme from Sulfolobus acidocaldarius DSM 639 displaying similarity to polyhydroxyalkanoate depolymerase
    • Arpigny, J. L., D. Jendrossek, and K.-E. Jäger. 1998. A novel heat-stable lipolytic enzyme from Sulfolobus acidocaldarius DSM 639 displaying similarity to polyhydroxyalkanoate depolymerase. FEMS Microbiol. Lett. 167:69-73.
    • (1998) FEMS Microbiol. Lett. , vol.167 , pp. 69-73
    • Arpigny, J.L.1    Jendrossek, D.2    Jäger, K.-E.3
  • 5
    • 0025712549 scopus 로고
    • More of the catalytic triad
    • Blow, D. 1990. More of the catalytic triad. Nature 351:694-695.
    • (1990) Nature , vol.351 , pp. 694-695
    • Blow, D.1
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 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
  • 8
    • 0031889267 scopus 로고    scopus 로고
    • A cold-adapted lipase of an Alaskan psychrotroph, Pseudomonas sp. strain B11-1: Gene cloning and enzyme purification and characterization
    • Choo, D.-W., T. Kurihara, T. Suzuki, K. Soda, and N. Esaki. 1998. A cold-adapted lipase of an Alaskan psychrotroph, Pseudomonas sp. strain B11-1: gene cloning and enzyme purification and characterization. Appl. Environ. Microbiol. 64:486-491.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 486-491
    • Choo, D.-W.1    Kurihara, T.2    Suzuki, T.3    Soda, K.4    Esaki, N.5
  • 10
    • 0028335828 scopus 로고
    • Sequence of the Streptomyces albus G lipase-encoding gene reveals the presence of a prokaryotic lipase family
    • Cruz, H., C. Perez, E. Wellington, C. Castro, and L. Servin-Gonzalez. 1994. Sequence of the Streptomyces albus G lipase-encoding gene reveals the presence of a prokaryotic lipase family. Gene 144:141-142.
    • (1994) Gene , vol.144 , pp. 141-142
    • Cruz, H.1    Perez, C.2    Wellington, E.3    Castro, C.4    Servin-Gonzalez, L.5
  • 11
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 12
    • 0025088866 scopus 로고
    • Sequence of a lipase gene from the antarctic psychrotroph Moraxella TA144
    • Feller, G., M. Thiry, and C. Gerday. 1990. Sequence of a lipase gene from the antarctic psychrotroph Moraxella TA144. Nucleic Acids Res. 18:6413.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6413
    • Feller, G.1    Thiry, M.2    Gerday, C.3
  • 13
    • 0025773328 scopus 로고
    • Cloning and expression in Escherichia coli of three lipase-encoding genes from the psychrotrophic antarctic strain Moraxella TA144
    • Feller, G., M. Thiry, J. L. Arpigny, and C. Gerday. 1991. Cloning and expression in Escherichia coli of three lipase-encoding genes from the psychrotrophic antarctic strain Moraxella TA144. Gene 102:111-115.
    • (1991) Gene , vol.102 , pp. 111-115
    • Feller, G.1    Thiry, M.2    Arpigny, J.L.3    Gerday, C.4
  • 14
    • 0032863699 scopus 로고    scopus 로고
    • Construction of environmental DNA libraries in Escherichia coli and screening for the presence of genes conferring utilization of 4-hydroxybutyrate
    • Henne, A., R. Daniel, R. A. Schmitz, and G. Gottschalk. 1999. Construction of environmental DNA libraries in Escherichia coli and screening for the presence of genes conferring utilization of 4-hydroxybutyrate. Appl. Environ. Microbiol. 65:3901-3907.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 3901-3907
    • Henne, A.1    Daniel, R.2    Schmitz, R.A.3    Gottschalk, G.4
  • 17
    • 0015425823 scopus 로고
    • Interspecies transformation of Acinetobacter: Genetic evidence for a ubiquitous genus
    • Juni, E. 1972. Interspecies transformation of Acinetobacter: genetic evidence for a ubiquitous genus. J. Bacteriol. 112:917-931.
    • (1972) J. Bacteriol. , vol.112 , pp. 917-931
    • Juni, E.1
  • 18
    • 0023089142 scopus 로고
    • Specific and sensitive plate assay for bacterial lipases
    • Kouker, G., and K.-E. Jaeger. 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
  • 19
    • 0024573670 scopus 로고
    • Cloning and expression in Escherichia coli of an esterase-coding gene from the oil-degrading Acinetobacter lwoffii RAG
    • Reddy, P. G., R. N. Alon, M. Mevarech, S. Mendelovitz, Y. Sato, and D. L. Gutnick. 1989. Cloning and expression in Escherichia coli of an esterase-coding gene from the oil-degrading Acinetobacter lwoffii RAG. Gene 76:145-152.
    • (1989) Gene , vol.76 , pp. 145-152
    • Reddy, P.G.1    Alon, R.N.2    Mevarech, M.3    Mendelovitz, S.4    Sato, Y.5    Gutnick, D.L.6
  • 20
    • 0030035418 scopus 로고    scopus 로고
    • A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomyces coelicolor A3 (2) chromosome
    • Redenbach, M., H. M. Kieser, D. Denapaite, A. Eichner, J. Cullum, H. Kinashi, and D. A. Hopwood. 1996. A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomyces coelicolor A3 (2) chromosome. Mol. Microbiol. 21:77-96.
    • (1996) Mol. Microbiol. , vol.21 , pp. 77-96
    • Redenbach, M.1    Kieser, H.M.2    Denapaite, D.3    Eichner, A.4    Cullum, J.5    Kinashi, H.6    Hopwood, D.A.7
  • 21
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 22
    • 0030690924 scopus 로고    scopus 로고
    • A study of iterative type II polyketide synthases, using bacterial genes cloned from soil DNA: A means to access and use genes from uncultured microorganisms
    • Seow, K.-T., G. Meurer, M. Gerlitz, E. Wendt-Pienkowski, C. R. Hutchinson, and J. Davies. 1997. A study of iterative type II polyketide synthases, using bacterial genes cloned from soil DNA: a means to access and use genes from uncultured microorganisms. J. Bacteriol. 179:7360-7368.
    • (1997) J. Bacteriol. , vol.179 , pp. 7360-7368
    • Seow, K.-T.1    Meurer, G.2    Gerlitz, M.3    Wendt-Pienkowski, E.4    Hutchinson, C.R.5    Davies, J.6
  • 23
    • 0030832083 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a new extracellular lipase from Streptomyces cinnamomeus
    • Sommer, P., C. Bormann, and F. Götz. 1997. Genetic and biochemical characterization of a new extracellular lipase from Streptomyces cinnamomeus. Appl. Environ. Microbiol. 63:3553-3560.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3553-3560
    • Sommer, P.1    Bormann, C.2    Götz, F.3
  • 24
    • 0042705655 scopus 로고    scopus 로고
    • The Streptomyces coelicolor A3 (2) lipAR operon encodes an extracellular lipase and a new type of transcriptional regulator
    • Valdez, F., G. Gonzales-Ceron, H. M. Kieser, and L. Servin-Gonzalez. 1999. The Streptomyces coelicolor A3 (2) lipAR operon encodes an extracellular lipase and a new type of transcriptional regulator. Microbiology 145:2365-2374.
    • (1999) Microbiology , vol.145 , pp. 2365-2374
    • Valdez, F.1    Gonzales-Ceron, G.2    Kieser, H.M.3    Servin-Gonzalez, L.4
  • 25
    • 0031023666 scopus 로고    scopus 로고
    • Interfacial activation of lipases: Facts and artifacts
    • Verger, R. 1997. Interfacial activation of lipases: facts and artifacts. Trends Biotechnol. 15:32-38.
    • (1997) Trends Biotechnol. , vol.15 , pp. 32-38
    • Verger, R.1
  • 26
    • 0018399632 scopus 로고
    • Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens
    • Winkler, U. K., and M. Stuckmann. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.