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Volumn 66, Issue 4, 2000, Pages 1360-1368

Cloning, characterization, controlled overexpression, and inactivation of the major tributyrin esterase gene of Lactococcus lactis

Author keywords

[No Author keywords available]

Indexed keywords

ESTERASE; HYDROLASE; LONG CHAIN FATTY ACID; PHOSPHOLIPID DERIVATIVE; SHORT CHAIN FATTY ACID; TRIACYLGLYCEROL LIPASE; TRIBUTYRIN;

EID: 0342369383     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.4.1360-1368.2000     Document Type: Article
Times cited : (83)

References (55)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for quantification 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
  • 3
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban, M. J., and S. N. Cohen. 1980. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138:179-207.
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 4
    • 0027473945 scopus 로고
    • Gene organization, primary structure and RNA processing analysis of a ribosomal RNA operon in Lactococcus lactis
    • Chiaruttini, C., and M. Millet. 1993. Gene organization, primary structure and RNA processing analysis of a ribosomal RNA operon in Lactococcus lactis. J. Mol. Biol. 230:57-76.
    • (1993) J. Mol. Biol. , vol.230 , pp. 57-76
    • Chiaruttini, C.1    Millet, M.2
  • 5
    • 0030952751 scopus 로고    scopus 로고
    • Intracellular esterase from Lactococcus lactis subsp. lactis NCDO 763: Purification and characterization
    • Chich, J. F., K. Marchesseau, and J. C. Gripon. 1997. Intracellular esterase from Lactococcus lactis subsp. lactis NCDO 763: purification and characterization. Int. Dairy J. 7:169-174.
    • (1997) Int. Dairy J. , vol.7 , pp. 169-174
    • Chich, J.F.1    Marchesseau, K.2    Gripon, J.C.3
  • 6
    • 0027181942 scopus 로고
    • Organization and regulation of genes for amino acid biosynthesis in lactic acid bacteria
    • Chopin, A. 1993. Organization and regulation of genes for amino acid biosynthesis in lactic acid bacteria. FEMS Microbiol. Rev. 12:21-38.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 21-38
    • Chopin, A.1
  • 7
    • 0027963099 scopus 로고
    • The diversity of potential cheese ripening characteristics of lactic acid starter bacteria. 2. The levels and subcellular distributions of peptidase and esterase activities
    • Crow, V. L., R. Holland, G. G. Pritchard, and T. Coolbear. 1994. The diversity of potential cheese ripening characteristics of lactic acid starter bacteria. 2. The levels and subcellular distributions of peptidase and esterase activities. Int. Dairy J. 4:723-742.
    • (1994) Int. Dairy J. , vol.4 , pp. 723-742
    • Crow, V.L.1    Holland, R.2    Pritchard, G.G.3    Coolbear, T.4
  • 8
    • 0027535179 scopus 로고
    • Relationship between sequence conservation and three-dimensional structure in a large family of esterases. Lipases, and related proteins
    • Cygler, M., J. D. Schrag, J. L. Sussman, M. Harel, I. Silman, M. K. Gentry, and B. P. Doctor. 1993. Relationship between sequence conservation and three-dimensional structure in a large family of esterases. lipases, and related proteins. Protein Sci. 2:366-382.
    • (1993) Protein Sci. , vol.2 , pp. 366-382
    • Cygler, M.1    Schrag, J.D.2    Sussman, J.L.3    Harel, M.4    Silman, I.5    Gentry, M.K.6    Doctor, B.P.7
  • 9
    • 0032809574 scopus 로고    scopus 로고
    • Purification and properties of an esterase from the yeast .Saccharomyces cerevisiae and identification of the encoding gene
    • Degrassi, G., L. Uotila, R. Klima, and V. Venturi. 1999. Purification and properties of an esterase from the yeast .Saccharomyces cerevisiae and identification of the encoding gene. Appl. Environ. Microbiol. 65:3470-3472.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 3470-3472
    • Degrassi, G.1    Uotila, L.2    Klima, R.3    Venturi, V.4
  • 10
  • 11
    • 0028223392 scopus 로고
    • Structure and function of lipases
    • Derewenda, Z. S. 1994. Structure and function of lipases. Adv. Protein Chem. 45:1-52.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 1-52
    • Derewenda, Z.S.1
  • 12
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • de Ruyter, P. G. G. A., O. P. Kuipers, and W. M. de Vos. 1996. Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl. Environ. Microbiol. 62:3662-3667.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3662-3667
    • De Ruyter, P.G.G.A.1    Kuipers, O.P.2    De Vos, W.M.3
  • 14
    • 0002978298 scopus 로고
    • Gene cloning and expression systems in lactococci
    • M. J. Gasson and W. M de Vos (ed.), Blackie Academic and Professional, Glasgow. United Kingdom
    • de Vos, W. M., and G. Simons. 1994. Gene cloning and expression systems in lactococci, p. 52-105. In M. J. Gasson and W. M de Vos (ed.), Genetics and biotechnology of lactic acid bacteria. Blackie Academic and Professional, Glasgow. United Kingdom.
    • (1994) Genetics and Biotechnology of Lactic Acid Bacteria , pp. 52-105
    • De Vos, W.M.1    Simons, G.2
  • 15
    • 0022894910 scopus 로고
    • Identity of the polymorphisms for esterase D and S-formylglutathione hydrolase in red blood cells
    • Eiberg, H., and J. Mohr, 1986. Identity of the polymorphisms for esterase D and S-formylglutathione hydrolase in red blood cells. Hum. Genet. 74:174-175.
    • (1986) Hum. Genet. , vol.74 , pp. 174-175
    • Eiberg, H.1    Mohr, J.2
  • 16
    • 0023084055 scopus 로고
    • Progressive sequence alignment as a prerequisite to correct phylogenetic trees
    • Feng, D. F., and R. F. Doolittle. 1987. Progressive sequence alignment as a prerequisite to correct phylogenetic trees. J. Mol. Evol. 25:351-360.
    • (1987) J. Mol. Evol. , vol.25 , pp. 351-360
    • Feng, D.F.1    Doolittle, R.F.2
  • 17
    • 0020600404 scopus 로고
    • Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing
    • Gasson, M. J. 1983. Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing. J. Bacteriol. 154:1-9.
    • (1983) J. Bacteriol. , vol.154 , pp. 1-9
    • Gasson, M.J.1
  • 18
    • 0026468164 scopus 로고
    • Divergence of genomic sequences between Lactococcus lactis subsp. lactis and Lactococcus lactis subsp. cremoris
    • Goddon, J. J., C. Delorme, S. D. Ehrlich, and P. Renault. 1992. Divergence of genomic sequences between Lactococcus lactis subsp. lactis and Lactococcus lactis subsp. cremoris. Appl. Environ. Microbiol. 58:4045-4047.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 4045-4047
    • Goddon, J.J.1    Delorme, C.2    Ehrlich, S.D.3    Renault, P.4
  • 19
    • 0006377528 scopus 로고
    • Lipases for industrial use
    • Godfrey, A. 1995. Lipases for industrial use. Lipid Technol. 7:58-61.
    • (1995) Lipid Technol. , vol.7 , pp. 58-61
    • Godfrey, A.1
  • 20
    • 0024094694 scopus 로고
    • Purification of Clostridium thermocellum xylanase Z expressed in Escherichia coli and identification of the corresponding product in the culture medium of C. thermocellum
    • Grépinet, O., M. C. Chebrou, and P. Béguin. 1988. Purification of Clostridium thermocellum xylanase Z expressed in Escherichia coli and identification of the corresponding product in the culture medium of C. thermocellum. J. Bacteriol. 170:4576-4581.
    • (1988) J. Bacteriol. , vol.170 , pp. 4576-4581
    • Grépinet, O.1    Chebrou, M.C.2    Béguin, P.3
  • 21
    • 0024095009 scopus 로고
    • Nucleotide sequence and deletion analysis of the xylanase gene (xynZ) of Clostridium thermocellum
    • Grépinet, O., M. C. Chebrou, and P. Béguin. 1988. Nucleotide sequence and deletion analysis of the xylanase gene (xynZ) of Clostridium thermocellum. J. Bacteriol. 170:4582-4588.
    • (1988) J. Bacteriol. , vol.170 , pp. 4582-4588
    • Grépinet, O.1    Chebrou, M.C.2    Béguin, P.3
  • 23
    • 0029967019 scopus 로고    scopus 로고
    • S-Formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: A universal pathway for formaldehyde detoxification?
    • Harms, N., J. Ras, W. N. M. Reijnders, R. J. M. van Spanning, and A. H. Stouthamer. 1996. S-Formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification? J. Bacteriol. 178:6296-6299.
    • (1996) J. Bacteriol. , vol.178 , pp. 6296-6299
    • Harms, N.1    Ras, J.2    Reijnders, W.N.M.3    Van Spanning, R.J.M.4    Stouthamer, A.H.5
  • 24
    • 0030087916 scopus 로고    scopus 로고
    • Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris
    • Holland, R., and T. Coolbear. 1996. Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris. J. Dairy Res. 63:131-140.
    • (1996) J. Dairy Res. , vol.63 , pp. 131-140
    • Holland, R.1    Coolbear, T.2
  • 25
    • 0026774359 scopus 로고
    • Cloning and nucleotide sequence of the cspl gene encoding PS1, one of the two major secreted proteins of Corynebacterium glutamicum: The deduced N-terminal region of PS1 is similar to the Mycobacterium antigen 85 complex
    • Joliff, G., L. Mathieu, V. Hahn, N. Bayan, F. Duchiron, M. Renaud, E. Shechter, and G. Leblon. 1992 Cloning and nucleotide sequence of the cspl gene encoding PS1, one of the two major secreted proteins of Corynebacterium glutamicum: the deduced N-terminal region of PS1 is similar to the Mycobacterium antigen 85 complex. Mol. Microbiol. 6:2349-2362.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2349-2362
    • Joliff, G.1    Mathieu, L.2    Hahn, V.3    Bayan, N.4    Duchiron, F.5    Renaud, M.6    Shechter, E.7    Leblon, G.8
  • 26
    • 0017016139 scopus 로고
    • Enzymes of Penicillium roquefortii Involved in the biosynthesis of cheese flavor
    • Kinsella, J. E., and D. H. Hwang. 1976. Enzymes of Penicillium roquefortii Involved in the biosynthesis of cheese flavor. Crit. Rev. Food Sci. Nutr. 8: 191-228.
    • (1976) Crit. Rev. Food Sci. Nutr. , vol.8 , pp. 191-228
    • Kinsella, J.E.1    Hwang, D.H.2
  • 27
    • 0025740912 scopus 로고
    • Improved site-directed mutagenesis method using PCR
    • Kuipers, O. P., H. J. Boot, and W. M. de Vos. 1991. Improved site-directed mutagenesis method using PCR. Nucleic Acids Res. 19:4558.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4558
    • Kuipers, O.P.1    Boot, H.J.2    De Vos, W.M.3
  • 28
    • 0027162304 scopus 로고
    • Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis: Requirement of expression of the nisA and nisI genes for development of immunity
    • Kuipers, O. P., M. M. Beerthuyzen, R. J. Siezen, and W. M. de Vos. 1993. Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis: requirement of expression of the nisA and nisI genes for development of immunity. Eur. J. Biochem. 216:281-291.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 281-291
    • Kuipers, O.P.1    Beerthuyzen, M.M.2    Siezen, R.J.3    De Vos, W.M.4
  • 31
    • 0023001208 scopus 로고
    • Molecular cloning of the human esterase D gene, a genetic marker of retinoblastoma
    • Lee, E. Y. H., and W. H. Lee. 1986. Molecular cloning of the human esterase D gene, a genetic marker of retinoblastoma. Proc. Natl. Acad. Sci. USA 83: 6337-6341.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6337-6341
    • Lee, E.Y.H.1    Lee, W.H.2
  • 33
    • 0032383294 scopus 로고    scopus 로고
    • Regulation of the carbohydrate metabolism in Lactococcus lactis and other lactic acid bacteria
    • Luesink, E. J., O. P. Kuipers, and W. M de Vos. 1998. Regulation of the carbohydrate metabolism in Lactococcus lactis and other lactic acid bacteria. Lait 78:69-76.
    • (1998) Lait , vol.78 , pp. 69-76
    • Luesink, E.J.1    Kuipers, O.P.2    De Vos, W.M.3
  • 34
    • 0025237055 scopus 로고
    • Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile "Caldocellum saccharolyticum."
    • Lüthi, E., D. R. Love, J. McAnulty, C. Wallace, P. A. Caughey, D. Saul, and P. L. Bergquist. 1990. Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile "Caldocellum saccharolyticum." Appl. Environ. Microbiol. 56:1017-1024.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 1017-1024
    • Lüthi, E.1    Love, D.R.2    McAnulty, J.3    Wallace, C.4    Caughey, P.A.5    Saul, D.6    Bergquist, P.L.7
  • 35
    • 0030027865 scopus 로고    scopus 로고
    • Efficient insertional mutagenesis in lactococci and other gram-positive bacteria
    • Maguin, E., H. Prévost, S. D. Ehrlich, and A. Gruss. 1996. Efficient insertional mutagenesis in lactococci and other gram-positive bacteria. J. Bacteriol. 178:931-935.
    • (1996) J. Bacteriol. , vol.178 , pp. 931-935
    • Maguin, E.1    Prévost, H.2    Ehrlich, S.D.3    Gruss, A.4
  • 36
    • 0013438872 scopus 로고
    • A method for the quantification of individual free fatty acids in cheese: Application to ripening of cheddar-type cheeses
    • McNeill, G. P., and J. F. Connolly. 1989. A method for the quantification of individual free fatty acids in cheese: application to ripening of cheddar-type cheeses. Irish J. Food Sci. Technol. 13:119-128.
    • (1989) Irish J. Food Sci. Technol. , vol.13 , pp. 119-128
    • McNeill, G.P.1    Connolly, J.F.2
  • 37
    • 0030267827 scopus 로고    scopus 로고
    • Lipase production by lactic acid bacteria and activity on butter oil
    • Meyers, S. A., S. L. Cuppett, and R. W. Hutkins. 1996. Lipase production by lactic acid bacteria and activity on butter oil. Food Microbiol. 13:383-389.
    • (1996) Food Microbiol. , vol.13 , pp. 383-389
    • Meyers, S.A.1    Cuppett, S.L.2    Hutkins, R.W.3
  • 38
    • 0027415633 scopus 로고
    • Cloning and sequencing of the gene for the α antigen from Mycobacterium avium and mapping of B-cell epitopes
    • Ohara, N., K. Matsuo, R. Yamaguchi, A. Yamazaki, H. Tasaka, and T. Yamada. 1993. Cloning and sequencing of the gene for the α antigen from Mycobacterium avium and mapping of B-cell epitopes. Infect. Immun. 61: 1173-1179.
    • (1993) Infect. Immun. , vol.61 , pp. 1173-1179
    • Ohara, N.1    Matsuo, K.2    Yamaguchi, R.3    Yamazaki, A.4    Tasaka, H.5    Yamada, T.6
  • 39
    • 0023989064 scopus 로고
    • Improved tools for biological sequence analysis
    • Pearson, W, R., and D. J. Lipman. 1988. Improved tools for biological sequence analysis. Proc. Natl. Acad. Sci. USA 85:2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 40
    • 0027305708 scopus 로고    scopus 로고
    • The Mycobacterium leprae antigen 85 complex gene family: Identification of the genes for the 85A, 85C, and related MPT51 proteins
    • Rinke de Wit, T. F., S. Bekelie, A. Osland, B. Wieles, A. A. M. Janson, and J. E. R. Thole. 3993. The Mycobacterium leprae antigen 85 complex gene family: identification of the genes for the 85A, 85C, and related MPT51 proteins. Infect. Immun. 61:3642-3647.
    • (3993) Infect. Immun. , vol.61 , pp. 3642-3647
    • Rinke De Wit, T.F.1    Bekelie, S.2    Osland, A.3    Wieles, B.4    Janson, A.A.M.5    Thole, J.E.R.6
  • 41
    • 0031029049 scopus 로고    scopus 로고
    • Antitermination of transcription of catabolic operons
    • Rutberg, B. 1997. Antitermination of transcription of catabolic operons. Mol. Microbiol. 23:413-421.
    • (1997) Mol. Microbiol. , vol.23 , pp. 413-421
    • Rutberg, B.1
  • 44
    • 0009939749 scopus 로고    scopus 로고
    • Cloning and sequencing of a S-formylglutathione hydrolase (FGH) gene from the cyanobacterium Anabaena azollae (accession no AF035558) (PGR98-024)
    • Shaw, W. H., T. Arioli, and J. Plazinski. 1998. Cloning and sequencing of a S-formylglutathione hydrolase (FGH) gene from the cyanobacterium Anabaena azollae (accession no AF035558) (PGR98-024). Plant Physiol. 116:868.
    • (1998) Plant Physiol. , vol.116 , pp. 868
    • Shaw, W.H.1    Arioli, T.2    Plazinski, J.3
  • 45
    • 0002773288 scopus 로고
    • Fat hydrolysis by lactic acid bacteria in cheese
    • Stadhouders, J., and H. A. Veringa. 1973. Fat hydrolysis by lactic acid bacteria in cheese. Neth. Milk Dairy J. 27:77-91.
    • (1973) Neth. Milk Dairy J. , vol.27 , pp. 77-91
    • Stadhouders, J.1    Veringa, H.A.2
  • 46
    • 0027930111 scopus 로고
    • Cloning, sequencing and expression in Escherichia coli of the gene for α antigen from Mycobacterium scrofulaceum
    • Takano, M., N. Ohara, A. Mizuno, and T. Yamada. 1994. Cloning, sequencing and expression in Escherichia coli of the gene for α antigen from Mycobacterium scrofulaceum. Scand. J. Immunol 40:165-170.
    • (1994) Scand. J. Immunol , vol.40 , pp. 165-170
    • Takano, M.1    Ohara, N.2    Mizuno, A.3    Yamada, T.4
  • 48
    • 21144478865 scopus 로고
    • Purification and partial characterization of an esterase from Lactococcus lactis ssp. lactis strain ACA-DC 127
    • Tsakalidou, E., and G. Kalantzopoulos. 1992. Purification and partial characterization of an esterase from Lactococcus lactis ssp. lactis strain ACA-DC 127. Lait 72:533-543.
    • (1992) Lait , vol.72 , pp. 533-543
    • Tsakalidou, E.1    Kalantzopoulos, G.2
  • 49
    • 0018174192 scopus 로고
    • Lipolysis by intracellular lipase of Streptococcus lactis against its neutral lipids obtained by growth at low temperature
    • Umemoto, Y., and Y. Sato. 1978. Lipolysis by intracellular lipase of Streptococcus lactis against its neutral lipids obtained by growth at low temperature. Agric. Biol. Chem. 42:221-225.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 221-225
    • Umemoto, Y.1    Sato, Y.2
  • 50
    • 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
  • 52
    • 0024538493 scopus 로고
    • A maturation protein is essential for the production of active forms of Lactococcus lactis SK11 serine proteinase located in or secreted from the cell envelope
    • Vos, P., M. van Asseldonk, F. van Jeveren, R. J. Siezen, G. Simons, and W. M. de Vos. 1989. A maturation protein is essential for the production of active forms of Lactococcus lactis SK11 serine proteinase located in or secreted from the cell envelope. J. Bacteriol. 171:2795-2802.
    • (1989) J. Bacteriol. , vol.171 , pp. 2795-2802
    • Vos, P.1    Van Asseldonk, M.2    Van Jeveren, F.3    Siezen, R.J.4    Simons, G.5    De Vos, W.M.6
  • 53
    • 0027230871 scopus 로고
    • Improved cloning vectors and transformation procedure for Lactococcus lactis
    • Wells, J. M., P. W. Wilson, and R. W. F. Le Page. 1993. Improved cloning vectors and transformation procedure for Lactococcus lactis. J. Appl. Bacteriol. 74:629-636.
    • (1993) J. Appl. Bacteriol. , vol.74 , pp. 629-636
    • Wells, J.M.1    Wilson, P.W.2    Le Page, R.W.F.3
  • 54
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 55
    • 0023779952 scopus 로고
    • Human esterase D gene: Complete cDNA sequence, genomic structure, and application in the genetic diagnosis of human retinoblastoma
    • Young, L. J. S., E. Y. H. P. Lee, H. To, R. Bookstein, J. Y. Shew, L. A. Donoso, T. Sery, M, Giblin, J. A. Shields, and W. H. Lee. 1988. Human esterase D gene: complete cDNA sequence, genomic structure, and application in the genetic diagnosis of human retinoblastoma. Hum. Genet. 79:137-141.
    • (1988) Hum. Genet. , vol.79 , pp. 137-141
    • Young, L.J.S.1    Lee, E.Y.H.P.2    To, H.3    Bookstein, R.4    Shew, J.Y.5    Donoso, L.A.6    Sery, T.7    Giblin, M.8    Shields, J.A.9    Lee, W.H.10


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