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Volumn 75, Issue 8, 2009, Pages 2326-2332

Heterologous production of methionine-γ-lyase from brevibacterium linens in lactococcus lactis and formation of volatile sulfur compounds

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGICAL APPROACHES; BREVIBACTERIUM LINENS; CELL EXTRACTS; CHEESE RIPENING; DIMETHYL DISULFIDES; FLAVOR DEVELOPMENT; FLAVOR FORMATIONS; GAS CHROMATOGRAPHY - MASS SPECTROMETRIES; HETEROLOGOUS PRODUCTIONS; INDUCIBLE PROMOTERS; L CYSTEINES; L CYSTINES; L METHIONINES; LACTIC ACID BACTERIA; LACTIS STRAINS; LACTOCOCCUS LACTIS; METHANETHIOL; PURIFIED PROTEINS; RECOMBINANT PROTEINS; SULFUR-CONTAINING COMPOUNDS; VOLATILE SULFUR COMPOUNDS; WHOLE CELLS; WILD-TYPE STRAINS;

EID: 64749114679     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02417-08     Document Type: Article
Times cited : (19)

References (44)
  • 1
    • 0028889680 scopus 로고
    • Purification and characterization of cystathionine γ-lyase from Lactococcus lactis subsp. cremoris B78 and its possible role in flavor development in cheese
    • Alting, A. C., W. J. M. Engels, S. van Schalkwijk, and F. A. Exterkate. 1995. Purification and characterization of cystathionine γ-lyase from Lactococcus lactis subsp. cremoris B78 and its possible role in flavor development in cheese. Appl. Environ. Microbiol. 61:4037-4042.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 4037-4042
    • Alting, A.C.1    Engels, W.J.M.2    van Schalkwijk, S.3    Exterkate, F.A.4
  • 2
    • 10444290571 scopus 로고    scopus 로고
    • Identification and functional analysis of the gene encoding methionine-γ-lyase in Brevibacterium linens
    • Amarita, F., M. Yvon, M. Nardi, E. Chambellon, J. Delettre, and P. Bonnarme. 2004. Identification and functional analysis of the gene encoding methionine-γ-lyase in Brevibacterium linens. Appl. Environ. Microbiol. 70: 7348-7354.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 7348-7354
    • Amarita, F.1    Yvon, M.2    Nardi, M.3    Chambellon, E.4    Delettre, J.5    Bonnarme, P.6
  • 3
    • 0034993001 scopus 로고    scopus 로고
    • Lactobacillus casei and Lactobacillus plantarum initiate catabolism of methionine by transamination
    • Amarita, F., T. Requena, G. Taborda, L. Amigo, and C. Pelaez. 2001. Lactobacillus casei and Lactobacillus plantarum initiate catabolism of methionine by transamination. J. Appl. Microbiol. 90:971-978.
    • (2001) J. Appl. Microbiol , vol.90 , pp. 971-978
    • Amarita, F.1    Requena, T.2    Taborda, G.3    Amigo, L.4    Pelaez, C.5
  • 4
    • 33644954958 scopus 로고    scopus 로고
    • Evidence for distinct L-methionine catabolic pathways in the yeast Geotrichum candidum and the bacterium Brevibacterium linens
    • Arfi, K., S. Landaud, and P. Bonnarme. 2006. Evidence for distinct L-methionine catabolic pathways in the yeast Geotrichum candidum and the bacterium Brevibacterium linens. Appl. Environ. Microbiol. 72:2155-2162.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 2155-2162
    • Arfi, K.1    Landaud, S.2    Bonnarme, P.3
  • 5
    • 0036061954 scopus 로고    scopus 로고
    • Isolation of the pat C gene encoding the cystathionine γ-lyase of Lactobacillus delbrueckii subsp. bulgaricus and molecular analysis of inter-strain variability in enzyme biosynthesis
    • Aubel, D., J. E. Germond, C. Gilbert, and D. Atlan. 2002. Isolation of the pat C gene encoding the cystathionine γ-lyase of Lactobacillus delbrueckii subsp. bulgaricus and molecular analysis of inter-strain variability in enzyme biosynthesis. Microbiology 148:2029-2036.
    • (2002) Microbiology , vol.148 , pp. 2029-2036
    • Aubel, D.1    Germond, J.E.2    Gilbert, C.3    Atlan, D.4
  • 6
    • 0033999271 scopus 로고    scopus 로고
    • Overcoming codon bias: A method for high-level overexpression of Plasmodium and other AT-rich parasite genes in Escherichia coli
    • Baca, A. M., and W. G. Hol. 2000. Overcoming codon bias: a method for high-level overexpression of Plasmodium and other AT-rich parasite genes in Escherichia coli. Int. J. Parasitol. 30:113-118.
    • (2000) Int. J. Parasitol , vol.30 , pp. 113-118
    • Baca, A.M.1    Hol, W.G.2
  • 7
    • 0035525372 scopus 로고    scopus 로고
    • L-Methionine degradation potentialities of cheese-ripening microorganisms
    • Bonnarme, P., C. Lapadatescu, M. Yvon, and H. E. Spinnler. 2001. L-Methionine degradation potentialities of cheese-ripening microorganisms. J. Dairy Res. 68:663-674.
    • (2001) J. Dairy Res , vol.68 , pp. 663-674
    • Bonnarme, P.1    Lapadatescu, C.2    Yvon, M.3    Spinnler, H.E.4
  • 8
    • 3042629048 scopus 로고    scopus 로고
    • Methylthioacetaldehyde, a possible intermediate metabolite for the production of volatile sulphur compounds from L-methionine by Lactococcus lactis
    • Bonnarme, P., F. Amarita, E. Chambellon, E. Semon, H. E. Spinnler, and M. Yvon. 2004. Methylthioacetaldehyde, a possible intermediate metabolite for the production of volatile sulphur compounds from L-methionine by Lactococcus lactis. FEMS Microbiol. Lett. 236:85-90.
    • (2004) FEMS Microbiol. Lett , vol.236 , pp. 85-90
    • Bonnarme, P.1    Amarita, F.2    Chambellon, E.3    Semon, E.4    Spinnler, H.E.5    Yvon, M.6
  • 9
    • 0034468974 scopus 로고    scopus 로고
    • Diversity of L-methionine catabolism pathways in cheese-ripening bacteria
    • Bonnarme, P., L. Psoni, and H. E. Spinnler. 2000. Diversity of L-methionine catabolism pathways in cheese-ripening bacteria. Appl. Environ. Microbiol. 66:5514-5517.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 5514-5517
    • Bonnarme, P.1    Psoni, L.2    Spinnler, H.E.3
  • 10
    • 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
  • 11
    • 0030938985 scopus 로고    scopus 로고
    • Purification and characterization of cystathionine γ-lyase from Lactococcus lactis subsp. cremoris SK11: Possible role in flavor compound formation during cheese maturation
    • Bruinenberg, P. G., G. de Roo, and G. K. Y. Limsowtin. 1997. Purification and characterization of cystathionine γ-lyase from Lactococcus lactis subsp. cremoris SK11: possible role in flavor compound formation during cheese maturation. Appl. Environ. Microbiol. 63:561-566.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 561-566
    • Bruinenberg, P.G.1    de Roo, G.2    Limsowtin, G.K.Y.3
  • 12
    • 1542618322 scopus 로고    scopus 로고
    • Codon usage between genomes is constrained by genome-wide mutational processes
    • Chen, S. L., W. Lee, A. K. Hottes, L. Shapiro, and H. H. McAdams. 2004. Codon usage between genomes is constrained by genome-wide mutational processes. Proc. Natl. Acad. Sci. USA 101:3480-3485.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3480-3485
    • Chen, S.L.1    Lee, W.2    Hottes, A.K.3    Shapiro, L.4    McAdams, H.H.5
  • 13
    • 64749095359 scopus 로고    scopus 로고
    • Collins, M. D., D. Jones, R. M. Keddie, and P. H. A. Sneath. 1980. Reclassification of Chromobacterium iodinum (Davis) in a redefined genus Brevi-bacterium (Breed) as Brevibacterium iodinum nom. rev.; comb. nov. J. Gen. Microbiol. 120:1-10.
    • Collins, M. D., D. Jones, R. M. Keddie, and P. H. A. Sneath. 1980. Reclassification of Chromobacterium iodinum (Davis) in a redefined genus Brevi-bacterium (Breed) as Brevibacterium iodinum nom. rev.; comb. nov. J. Gen. Microbiol. 120:1-10.
  • 15
    • 0031687912 scopus 로고    scopus 로고
    • Conversion of methionine to thiols by lactococci, lactobacilli, and brevibacteria
    • Dias, B., and B. Weimer. 1998. Conversion of methionine to thiols by lactococci, lactobacilli, and brevibacteria. Appl. Environ. Microbiol. 64:3320-3326.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 3320-3326
    • Dias, B.1    Weimer, B.2
  • 16
    • 0031662724 scopus 로고    scopus 로고
    • Purification and characterization of L-methionine γ-lyase from Brevibacterium linens BL2
    • Dias, B., and B. Weimer. 1998. Purification and characterization of L-methionine γ-lyase from Brevibacterium linens BL2. Appl. Environ. Microbiol. 64:3327-3331.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 3327-3331
    • Dias, B.1    Weimer, B.2
  • 17
    • 0032707422 scopus 로고    scopus 로고
    • Production of volatile sulphur compounds in Cheddar cheese slurries
    • Dias, B., and B. Weimer. 1999. Production of volatile sulphur compounds in Cheddar cheese slurries. Int. Dairy J. 9:605-611.
    • (1999) Int. Dairy J , vol.9 , pp. 605-611
    • Dias, B.1    Weimer, B.2
  • 18
    • 0033988405 scopus 로고    scopus 로고
    • Identification and characterization of a cystathionine γ/γ-lyase from Lactococcus lactis ssp. cremoris MG1363
    • Dobric, N., G. K. Limsowtin, A. J. Hillier, N. P. Dudman, and B. E. Davidson. 2000. Identification and characterization of a cystathionine γ/γ-lyase from Lactococcus lactis ssp. cremoris MG1363. FEMS Microbiol. Lett. 182: 249-254.
    • (2000) FEMS Microbiol. Lett , vol.182 , pp. 249-254
    • Dobric, N.1    Limsowtin, G.K.2    Hillier, A.J.3    Dudman, N.P.4    Davidson, B.E.5
  • 20
    • 0023081007 scopus 로고
    • L-Methionine-γ-lyase from Pseudomonas putida and Aeromonas
    • Esaki, N., and K. Soda. 1987. L-Methionine-γ-lyase from Pseudomonas putida and Aeromonas. Methods Enzymol. 143:459-465.
    • (1987) Methods Enzymol , vol.143 , pp. 459-465
    • Esaki, N.1    Soda, K.2
  • 21
    • 0021828553 scopus 로고
    • Production of methanethiol from methionine by Brevibacterium linens CNRZ 918
    • Ferchichi, M., D. Hemme, M. Nardi, and N. Pamboukgjian. 1985. Production of methanethiol from methionine by Brevibacterium linens CNRZ 918. J. Gen. Microbiol. 131:715-723.
    • (1985) J. Gen. Microbiol , vol.131 , pp. 715-723
    • Ferchichi, M.1    Hemme, D.2    Nardi, M.3    Pamboukgjian, N.4
  • 23
    • 0031593446 scopus 로고    scopus 로고
    • 13C nuclear magnetic resonance and gas chromatography to examine methionine catabolism by lactococci
    • 13C nuclear magnetic resonance and gas chromatography to examine methionine catabolism by lactococci. Appl. Environ. Microbiol. 64:4670-4675.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 4670-4675
    • Gao, S.1    Mooberry, E.S.2    Steele, J.L.3
  • 24
    • 0020600404 scopus 로고
    • Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-inducing curing
    • Gasson, M. J. 1983. Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-inducing curing. J. Bacteriol. 154:1-9.
    • (1983) J. Bacteriol , vol.154 , pp. 1-9
    • Gasson, M.J.1
  • 25
    • 34250850651 scopus 로고    scopus 로고
    • Kluyveromyces lactis and Saccharomyces cerevisiae, two potent deacidifying and volatile-sulphur-aroma-producing microorganisms of the cheese ecosystem
    • Kagkli, D. M., R. Tache, T. M. Cogan, C. Hill, S. Casaregola, and P. Bonnarme. 2006. Kluyveromyces lactis and Saccharomyces cerevisiae, two potent deacidifying and volatile-sulphur-aroma-producing microorganisms of the cheese ecosystem. Appl. Microbiol. Biotechnol. 73:434-442.
    • (2006) Appl. Microbiol. Biotechnol , vol.73 , pp. 434-442
    • Kagkli, D.M.1    Tache, R.2    Cogan, T.M.3    Hill, C.4    Casaregola, S.5    Bonnarme, P.6
  • 26
    • 0015798572 scopus 로고
    • Isolation and purification of L-methionine-α-deamino-γ-mercaptomethane-lyase (L-methionase) from Clostridium sporogenes
    • Kreis, W., and C. Hession. 1973. Isolation and purification of L-methionine-α-deamino-γ-mercaptomethane-lyase (L-methionase) from Clostridium sporogenes. Cancer Res. 33:1862-1865.
    • (1973) Cancer Res , vol.33 , pp. 1862-1865
    • Kreis, W.1    Hession, C.2
  • 27
    • 34248210545 scopus 로고    scopus 로고
    • Role of cystathionine γ-lyase in catabolism of amino acids to sulfur volatiles by genetic variants of Lactobacillus helveticus CNRZ 32
    • Lee, W.-J., D. S. Banavara, J. E. Hughes, J. K. Christiansen, J. L. Steele, J. R. Broadbent, and S. A. Rankin. 2007. Role of cystathionine γ-lyase in catabolism of amino acids to sulfur volatiles by genetic variants of Lactobacillus helveticus CNRZ 32. Appl. Environ. Microbiol. 73:3034-3039.
    • (2007) Appl. Environ. Microbiol , vol.73 , pp. 3034-3039
    • Lee, W.-J.1    Banavara, D.S.2    Hughes, J.E.3    Christiansen, J.K.4    Steele, J.L.5    Broadbent, J.R.6    Rankin, S.A.7
  • 28
    • 0025947233 scopus 로고
    • Purification and characterization of methionine-γ-lyase from Trichomonas vaginalis
    • Lockwood, B. C., and G. C. Coombs. 1991. Purification and characterization of methionine-γ-lyase from Trichomonas vaginalis. Biochem. J. 279:675-682.
    • (1991) Biochem. J , vol.279 , pp. 675-682
    • Lockwood, B.C.1    Coombs, G.C.2
  • 29
    • 18944395885 scopus 로고    scopus 로고
    • A gene encoding L-methionine γ-lyase is present in Enterobacteriaceae family genomes: Identification and characterization of Citrobacter freundii L-methionine γ-lyase
    • Manukhov, I. V., D. V. Mamaeva, S. M. Rastorguev, N. G. Faleev, E. A. Morozova, T. V. Demidkina, and G. B. Zavilgesky. 2005. A gene encoding L-methionine γ-lyase is present in Enterobacteriaceae family genomes: identification and characterization of Citrobacter freundii L-methionine γ-lyase. J. Bacteriol. 187:3889-3893.
    • (2005) J. Bacteriol , vol.187 , pp. 3889-3893
    • Manukhov, I.V.1    Mamaeva, D.V.2    Rastorguev, S.M.3    Faleev, N.G.4    Morozova, E.A.5    Demidkina, T.V.6    Zavilgesky, G.B.7
  • 32
    • 0642280877 scopus 로고    scopus 로고
    • Expression and delivery of heterologous antigens using lactic acid bacteria
    • Reuter, M. A., S. Hanniffy, and J. M. Wells. 2003. Expression and delivery of heterologous antigens using lactic acid bacteria. Methods Mol. Med. 87:101-104.
    • (2003) Methods Mol. Med , vol.87 , pp. 101-104
    • Reuter, M.A.1    Hanniffy, S.2    Wells, J.M.3
  • 35
    • 15544375677 scopus 로고    scopus 로고
    • Characterization of a novel leucine-rich repeat protein antigen from group B streptococci that elicits protective immunity
    • Seepersaud, R., S. B. Hanniffy, P. Mayne, P. Sizer, R. Le Page, and J. M. Wells. 2005. Characterization of a novel leucine-rich repeat protein antigen from group B streptococci that elicits protective immunity. Infect. Immun. 73:1671-1683.
    • (2005) Infect. Immun , vol.73 , pp. 1671-1683
    • Seepersaud, R.1    Hanniffy, S.B.2    Mayne, P.3    Sizer, P.4    Le Page, R.5    Wells, J.M.6
  • 36
    • 0023066723 scopus 로고
    • Microbial sulfur amino acids: An overview
    • Soda, K. 1987. Microbial sulfur amino acids: an overview. Methods Enzymol. 143:453-459.
    • (1987) Methods Enzymol , vol.143 , pp. 453-459
    • Soda, K.1
  • 37
    • 0142180049 scopus 로고    scopus 로고
    • Identification and characterization of two isoenzymes of methionine-γ-lyase from Entamoeba histolytica
    • Tokoro, M., T. Asai, S. Kobayashi, T. Takeuchi, and T. Nozaki. 2003. Identification and characterization of two isoenzymes of methionine-γ-lyase from Entamoeba histolytica. J. Biol. Chem. 279:42717-42727.
    • (2003) J. Biol. Chem , vol.279 , pp. 42717-42727
    • Tokoro, M.1    Asai, T.2    Kobayashi, S.3    Takeuchi, T.4    Nozaki, T.5
  • 38
    • 58149321458 scopus 로고
    • Contribution of lactic acid bacteria to flavour compound formation in dairy products
    • Urbach, G. 1995. Contribution of lactic acid bacteria to flavour compound formation in dairy products. Int. Dairy J. 5:877-905.
    • (1995) Int. Dairy J , vol.5 , pp. 877-905
    • Urbach, G.1
  • 39
    • 0023066978 scopus 로고
    • Cystathionine γ-lyase from Escherichia coli
    • Uren, J. R. 1987. Cystathionine γ-lyase from Escherichia coli. Methods Enzymol. 143:483-486.
    • (1987) Methods Enzymol , vol.143 , pp. 483-486
    • Uren, J.R.1
  • 41
    • 0032847477 scopus 로고    scopus 로고
    • Sulfur metabolism in bacteria associated with cheese
    • Weimer, B., K. Seefeldt, and B. Dias. 1999. Sulfur metabolism in bacteria associated with cheese. Antonie van Leeuwenhoek 76:247-261.
    • (1999) Antonie van Leeuwenhoek , vol.76 , pp. 247-261
    • Weimer, B.1    Seefeldt, K.2    Dias, B.3
  • 42
    • 0027230871 scopus 로고
    • Improved cloning vectors and transformation procedure for Lactococcus lactis
    • Wells, J. M., P. W. Wilson, and R. W. 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.3
  • 43
    • 0036952884 scopus 로고    scopus 로고
    • Lcd from Streptococcus anginosus encodes a C-S lyase with α,γ-elimination activity that degrades L-cysteine
    • Yoshida, Y., Y. Nakano, A. Amano, M. Yoshimura, H. Fukamachi, T. Oho, and T. Koga. 2002. Lcd from Streptococcus anginosus encodes a C-S lyase with α,γ-elimination activity that degrades L-cysteine. Microbiology 148: 3961-3970.
    • (2002) Microbiology , vol.148 , pp. 3961-3970
    • Yoshida, Y.1    Nakano, Y.2    Amano, A.3    Yoshimura, M.4    Fukamachi, H.5    Oho, T.6    Koga, T.7
  • 44
    • 0029127483 scopus 로고
    • MalY of Escherichia coli is an enzyme with the activity of a γC-S lyase (cystathionase)
    • Zdych, E., R. Peist, J. Reidl, and W. Boos. 1995. MalY of Escherichia coli is an enzyme with the activity of a γC-S lyase (cystathionase). J. Bacteriol. 177:5035-5039.
    • (1995) J. Bacteriol , vol.177 , pp. 5035-5039
    • Zdych, E.1    Peist, R.2    Reidl, J.3    Boos, W.4


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