메뉴 건너뛰기




Volumn 51, Issue 7, 2011, Pages 691-703

Biogenic amines in dairy products

Author keywords

Biochemistry; Biogenic amines; Dairy products; Detection; Genetics; Microbiology; Regulation; Toxicology

Indexed keywords

BIOGENIC AMINES; BIOSYNTHETIC PATHWAY; ENVIRONMENTAL CONDITIONS; GENETIC ORGANIZATION; GENETICS; HIGH CONCENTRATION; NITROGENOUS COMPOUNDS; REGULATION; TOXICOLOGY;

EID: 79960852239     PISSN: 10408398     EISSN: 15497852     Source Type: Journal    
DOI: 10.1080/10408398.2011.582813     Document Type: Article
Times cited : (318)

References (107)
  • 1
    • 44849124780 scopus 로고    scopus 로고
    • Factors affecting the production of putrescine from agmatine by Lactobacillus hilgardii X1B isolated from wine
    • Arena, M.E., Landete, J.M., Manca de Nadra, M.C., Pardo, I., and Ferrer, S. (2008). Factors affecting the production of putrescine from agmatine by Lactobacillus hilgardii X1B isolated from wine. J. Appl. Microbiol. 105: 158-165.
    • (2008) J. Appl. Microbiol. , vol.105 , pp. 158-165
    • Arena, M.E.1    Landete, J.M.2    Manca de Nadra, M.C.3    Pardo, I.4    Ferrer, S.5
  • 2
    • 0035134087 scopus 로고    scopus 로고
    • Biogenic amine production by Lactobacillus
    • Arena, M.E. and Manca de Nadra, M. C. (2001). Biogenic amine production by Lactobacillus. J. Appl. Microbiol. 90: 158-162.
    • (2001) J. Appl. Microbiol. , vol.90 , pp. 158-162
    • Arena, M.E.1    Manca de Nadra, M.C.2
  • 3
    • 84856311258 scopus 로고    scopus 로고
    • Role of biogenic amines-summing up or what is it we do not know?
    • European Community, Ed
    • Bardócz, S. (1999). Role of biogenic amines-summing up or what is it we do not know? In: Biogenically Active Amines in Food, Vol. III. pp 1-4. European Community, Ed.
    • (1999) Biogenically Active Amines in Food , vol.3 , pp. 1-4
    • Bardócz, S.1
  • 4
    • 0032788357 scopus 로고    scopus 로고
    • Biogenic amines in foods: Histamine and food processing
    • Bodmer, S., Imark, C., and Kneubúhl, M. (1999). Biogenic amines in foods: Histamine and food processing. Inflam. Research. 48: 296-300.
    • (1999) Inflam. Research. , vol.48 , pp. 296-300
    • Bodmer, S.1    Imark, C.2    Kneubúhl, M.3
  • 5
    • 0024968602 scopus 로고
    • Purification and characterization of tyrosine decarboxylase and aromatic- L-amino acid decarboxylase
    • Børrensen, T., Klausen, N.K., Larsen, L.M., and Sørensen, H. (1989). Purification and characterization of tyrosine decarboxylase and aromatic- L-amino acid decarboxylase. Biochim. Biophys. Acta. 993: 108-115.
    • (1989) Biochim. Biophys. Acta. , vol.993 , pp. 108-115
    • Børrensen, T.1    Klausen, N.K.2    Larsen, L.M.3    Sørensen, H.4
  • 7
    • 0033408543 scopus 로고    scopus 로고
    • Improved screening procedure for biogenic amine production by lactic acid bacteria
    • Bover-Cid, S. and Holzapfel, W.H. (1999). Improved screening procedure for biogenic amine production by lactic acid bacteria. Int. J Food Microbiol. 53: 33-41.
    • (1999) Int. J Food Microbiol. , vol.53 , pp. 33-41
    • Bover-Cid, S.1    Holzapfel, W.H.2
  • 8
    • 35448967978 scopus 로고    scopus 로고
    • Biogenic amine-forming microbial communities in cheese
    • Burdychova, R. and Komprda, T. (2007). Biogenic amine-forming microbial communities in cheese. FEMS Microbiol. Lett. 276: 149-155.
    • (2007) FEMS Microbiol. Lett. , vol.276 , pp. 149-155
    • Burdychova, R.1    Komprda, T.2
  • 9
    • 0036300809 scopus 로고    scopus 로고
    • Identification of the Enterococcus faecalis tyrosine decarboxylase operon involved in tyramine production
    • Connil, N., Breton, Y.L., Dousset, X., Auffray, Y., Rincé, A., and Prévost, H (2002). Identification of the Enterococcus faecalis tyrosine decarboxylase operon involved in tyramine production. Appl. Environ. Microbiol. 68: 3537- 3544.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3537-3544
    • Connil, N.1    Breton, Y.L.2    Dousset, X.3    Auffray, Y.4    Rincé, A.5    Prévost, H.6
  • 10
    • 0024834141 scopus 로고
    • The molecular cloning, sequence and expression of the hdcB gene from Lactobacillus 30A
    • Copeland, W.C., Domena, J.D., and Robertus, J.D. (1989). The molecular cloning, sequence and expression of the hdcB gene from Lactobacillus 30A. Gene. 85: 259-265.
    • (1989) Gene , vol.85 , pp. 259-265
    • Copeland, W.C.1    Domena, J.D.2    Robertus, J.D.3
  • 11
    • 27744546509 scopus 로고    scopus 로고
    • Multiplex PCR for colony direct detection of Gram-positive histamine- and tyramine-producing bacteria
    • Coton, E. and Coton, M. (2005). Multiplex PCR for colony direct detection of Gram-positive histamine- and tyramine-producing bacteria. J. Microbiol. Methods. 63: 296-304.
    • (2005) J. Microbiol. Methods. , vol.63 , pp. 296-304
    • Coton, E.1    Coton, M.2
  • 12
    • 33750503418 scopus 로고    scopus 로고
    • PCR detection of foodborne bacteria producing the biogenic amines histamine, tyramine, putrescine, and cadaverine
    • de las Rivas, B., Marcobal, A., Carrascosa, A.V., and Muñoz, R. (2006). PCR detection of foodborne bacteria producing the biogenic amines histamine, tyramine, putrescine, and cadaverine. J. Food Prot. 69: 2509-2514.
    • (2006) J. Food Prot. , vol.69 , pp. 2509-2514
    • de las Rivas, B.1    Marcobal, A.2    Carrascosa, A.V.3    Muñoz, R.4
  • 13
    • 0023793137 scopus 로고
    • Transport of diamines by Enterococcus faecalis is mediated by an agmatine-putrescine antiporter
    • Driessen, A.J., Smid, E.J., and Konings, W.N. (1988). Transport of diamines by Enterococcus faecalis is mediated by an agmatine-putrescine antiporter. J. Bacteriol. 170: 4522-4527.
    • (1988) J. Bacteriol. , vol.170 , pp. 4522-4527
    • Driessen, A.J.1    Smid, E.J.2    Konings, W.N.3
  • 14
    • 35348813614 scopus 로고    scopus 로고
    • HPLC quantification of biogenic amines in cheeses: Correlation with PCR-detection of tyramine-producing microorganisms
    • Fernández, M., Linares, D.M., del Río, B., Ladero, V., and Alvarez, M.A. (2007a). HPLC quantification of biogenic amines in cheeses: correlation with PCR-detection of tyramine-producing microorganisms. J. Dairy Res. 74: 276-282.
    • (2007) J. Dairy Res. , vol.74 , pp. 276-282
    • Fernández, M.1    Linares, D.M.2    del Río, B.3    Ladero, V.4    Alvarez, M.A.5
  • 16
    • 33746458379 scopus 로고    scopus 로고
    • Early PCR detection of tyramine-producing bacteria during cheese production
    • Fernández, M., Flórez, A.B., Linares, D.M., Mayo, B., and Alvarez, M.A. (2006a). Early PCR detection of tyramine-producing bacteria during cheese production J. Dairy Res. 73: 318-321.
    • (2006) J. Dairy Res. , vol.73 , pp. 318-321
    • Fernández, M.1    Flórez, A.B.2    Linares, D.M.3    Mayo, B.4    Alvarez, M.A.5
  • 17
    • 33749407158 scopus 로고    scopus 로고
    • Real-time polymerase chain reaction for quantitative detection of histamine-producing bacteria: Use in cheese production
    • Fernández, M., del Río, B., Linares, D.M., Martín, M.C., and Alvarez, M.A. (2006b). Real-time polymerase chain reaction for quantitative detection of histamine-producing bacteria: use in cheese production. J. Dairy Sci. 89: 3763-3769.
    • (2006) J. Dairy Sci. , vol.89 , pp. 3763-3769
    • Fernández, M.1    del Río, B.2    Linares, D.M.3    Martín, M.C.4    Alvarez, M.A.5
  • 18
    • 7944235085 scopus 로고    scopus 로고
    • Sequencing of the tyrosine decarboxylase cluster of Lactococcus lactis IPLA 655 and the development of a PCR method for detecting tyrosine decarboxylating lactic acid bacteria
    • Fernández, M., Linares, D.M., and Alvarez, M.A. (2004). Sequencing of the tyrosine decarboxylase cluster of Lactococcus lactis IPLA 655 and the development of a PCR method for detecting tyrosine decarboxylating lactic acid bacteria J. Food Prot. 67: 2521-2529.
    • (2004) J. Food Prot. , vol.67 , pp. 2521-2529
    • Fernández, M.1    Linares, D.M.2    Alvarez, M.A.3
  • 19
    • 33747084425 scopus 로고    scopus 로고
    • Amino acid catabolic pathways in lactic acid bacteria
    • Fernández, M. and Zuñiga, M. (2006). Amino acid catabolic pathways in lactic acid bacteria. Crit. Rev. Microbiol. 32: 155-183.
    • (2006) Crit. Rev. Microbiol. , vol.32 , pp. 155-183
    • Fernández, M.1
  • 20
    • 0033761929 scopus 로고    scopus 로고
    • Formation of biogenic amines in raw milk Hispanico cheese manufactured with proteinases and different levels of starter culture
    • Fernández-García, E., Tomillo, J., and Nuñez, M. (2000) Formation of biogenic amines in raw milk Hispanico cheese manufactured with proteinases and different levels of starter culture. J. Food Prot. 63: 1551-1555.
    • (2000) J. Food Prot. , vol.63 , pp. 1551-1555
    • Fernández-García, E.1    Tomillo, J.2    Nuñez, M.3
  • 24
    • 0035961658 scopus 로고    scopus 로고
    • Effects of pH, temperature and NaCl concentration on the growth kinetics, proteolytic activity and biogenic amine production of Enterococcus faecalsi
    • Gardini, F., Martuscelli, M., Caruso, M.C., Galgano, F., Crudele, M.A., Favati, F., Guerzoni, M.E., and. Suzzi, G. (2001). Effects of pH, temperature and NaCl concentration on the growth kinetics, proteolytic activity and biogenic amine production of Enterococcus faecalsi. Int. J. Food. Microbiol. 64: 105- 117.
    • (2001) Int. J. Food. Microbiol. , vol.64 , pp. 105-117
    • Gardini, F.1    Martuscelli, M.2    Caruso, M.C.3    Galgano, F.4    Crudele, M.A.5    Favati, F.6    Guerzoni, M.E.7    Suzzi, G.8
  • 25
    • 7144253136 scopus 로고    scopus 로고
    • Biogenic amine production by wild lactococcal and leuconostoc strains
    • González de Llano, D., Cuesta, P., and Rodríguez, A. (1998). Biogenic amine production by wild lactococcal and leuconostoc strains. Lett. Appl.Microbiol. 26: 270-274.
    • (1998) Lett Appl.Microbiol , vol.26 , pp. 270-274
    • de González, L.D.1    Cuesta, P.2    Rodríguez, A.3
  • 27
    • 0019411584 scopus 로고
    • Crystallization and subunit structure of histidinedecarboxylase from Lactobacillus-30A
    • Hackert, M.L., Meador, W.E., Oliver, R.M., Salmon, J.B., Recsei, P.A., and Snell, E.E. (1981). Crystallization and subunit structure of histidinedecarboxylase from Lactobacillus-30A. J. Biol. Chem. 256: 687-690.
    • (1981) J. Biol. Chem. , vol.256 , pp. 687-690
    • Hackert, M.L.1    Meador, W.E.2    Oliver, R.M.3    Salmon, J.B.4    Recsei, P.A.5    Snell, E.E.6
  • 28
    • 0034806849 scopus 로고    scopus 로고
    • Genome of the bacterium Streptococcus pneumoniae strain R6
    • Hoskins, J., Alborn, W.E., Arnold, J., et al. (2001). Genome of the bacterium Streptococcus pneumoniae strain R6. J. Bacteriol. 183: 5709-5717.
    • (2001) J. Bacteriol. , vol.183 , pp. 5709-5717
    • Hoskins, J.1    Alborn, W.E.2    Arnold, J.3
  • 30
    • 0035002972 scopus 로고    scopus 로고
    • Polyamine uptake systems in Escherichia coli
    • Igarashi, K., Ito, K., and Kashiwagi, K. (2001). Polyamine uptake systems in Escherichia coli. Res. Microbiol. 152: 271-278.
    • (2001) Res. Microbiol. , vol.152 , pp. 271-278
    • Igarashi, K.1    Ito, K.2    Kashiwagi, K.3
  • 31
    • 0036715280 scopus 로고    scopus 로고
    • Formation of biogenic amines in a typical semihard Italian cheese
    • Innocente, N. and D'Agostin, P. (2002). Formation of biogenic amines in a typical semihard Italian cheese. J. Food Prot. 65: 1498-1501.
    • (2002) J. Food Prot. , vol.65 , pp. 1498-1501
    • Innocente, N.1    D'Agostin, P.2
  • 32
    • 0033886562 scopus 로고    scopus 로고
    • The amino acid/polyamine/ organocation (APC) superfamily of transporters specific for amino acids, polyamines and organocations
    • Jack, D.L., Paulsen, I.T., and Saier, M.H. (2000). The amino acid/polyamine/ organocation (APC) superfamily of transporters specific for amino acids, polyamines and organocations. Microbiol. 146: 1797-1814.
    • (2000) Microbiol , vol.146 , pp. 1797-1814
    • Jack, D.L.1    Paulsen, I.T.2    Saier, M.H.3
  • 33
    • 0000013051 scopus 로고
    • Conditions allowing the formation of biogenic amines in cheese 2.Decarboxylative properties of some non starter bacteria.
    • Joosten, H.M.L.J. and Northolt, M.D. (1987).Conditions allowing the formation of biogenic amines in cheese 2.Decarboxylative properties of some non starter bacteria. Neth. Milk Dairy J. 41: 259-280.
    • (1987) Milk Dairy J Neth , vol.41 , pp. 259-280
    • Joosten, H.M.L.J.1    Northolt, M.D.2
  • 34
    • 0030889906 scopus 로고    scopus 로고
    • Excretion and uptake of putrescine by the PotE protein in Escherichia coli
    • Kashiwagi, K., Shibuya, S., Tomitori, H., Kuraishi, A., and Igarashi, K. (1997). Excretion and uptake of putrescine by the PotE protein in Escherichia coli. J. Biol. Chem. 272: 6318-6323.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6318-6323
    • Kashiwagi, K.1    Shibuya, S.2    Tomitori, H.3    Kuraishi, A.4    Igarashi, K.5
  • 35
    • 0028337298 scopus 로고
    • Involvement of ribonuclease III in the enhancement of expression of the speF-potE operon encoding inducible ornithine decarboxylase and polyamine transport protein
    • Kashiwagi, K., Watanabe, R., and Igarashi, K. (1994). Involvement of ribonuclease III in the enhancement of expression of the speF-potE operon encoding inducible ornithine decarboxylase and polyamine transport protein. Biochem. Biophys. Res. Commun. 15: 591-597.
    • (1994) Commun. Biochem. Res. , vol.15 , pp. 591-597
    • Kashiwagi, K.1    Watanabe, R.2    Igarashi, K.3
  • 37
    • 55649116846 scopus 로고    scopus 로고
    • Real Time Quantitative PCR detection of histamine-producing lactic acid bacteria in cheese: Relation with histamine content
    • Ladero, V., Linares, D.M., Fernández, M., and Alvarez, M.A. (2008). Real Time Quantitative PCR detection of histamine-producing lactic acid bacteria in cheese: relation with histamine content. Food Res Int. 41: 1015-1019.
    • (2008) Food Res Int , vol.41 , pp. 1015-1019
    • Ladero, V.1    Linares, D.M.2    Fernández, M.3    Alvarez, M.A.4
  • 38
    • 34250860684 scopus 로고    scopus 로고
    • Molecular methods for the detection of biogenic amine-producing bacteria on foods
    • Landete, J.M., de Las Rivas, B.,Marcobal, A., and Muoz, R. (2007).Molecular methods for the detection of biogenic amine-producing bacteria on foods. Int. J. Food Microbiol. 117: 258-269.
    • (2007) Int. J. Food Microbiol. , vol.117 , pp. 258-269
    • Landete, J.M.1    de Las, R.B.2    Marcobal, A.3    Muoz, R.4
  • 39
    • 24044435872 scopus 로고    scopus 로고
    • Which lactic acid bacteria are responsible for histamine production in wine
    • Landete, J.M., Ferrer, S., and Pardo, I. (2005). Which lactic acid bacteria are responsible for histamine production in wine? J. Appl. Microbiol. 99: 580- 586.
    • (2005) J. Appl. Microbiol. , vol.99 , pp. 580-586
    • Landete, J.M.1    Ferrer, S.2    Pardo, I.3
  • 40
    • 0001426715 scopus 로고
    • Influence of pasteurization of milk on protein breakdown in Cheddar cheese during aging
    • Lau, K.L., Barbano, M., and Rasmussen, R.R. (1991). Influence of pasteurization of milk on protein breakdown in Cheddar cheese during aging. J. Dairy Sci. 74: 727-740.
    • (1991) J. Dairy Sci. , vol.74 , pp. 727-740
    • Lau, K.L.1    Barbano, M.2    Rasmussen, R.R.3
  • 41
    • 33947148545 scopus 로고    scopus 로고
    • CadC has a global translational effect during acid adaptation in Salmonella enterica serovar Typhimurium
    • Lee Y.H., Kim, B.H., Kim, J.H., Yoon,W.S. Bang, S.H., and Park, Y.K. (2007). CadC has a global translational effect during acid adaptation in Salmonella enterica serovar Typhimurium. J. Bacteriol. 189: 2417-2425.
    • (2007) J. Bacteriol. , vol.189 , pp. 2417-2425
    • Lee, Y.H.1    Kim, B.H.2    Kim, J.H.3    Yoon, W.S.4    Bang, S.H.5    Park, Y.K.6
  • 42
    • 0028964390 scopus 로고
    • Development of a detection system for histidine decarboxylating lactic acid bacteria based on DNA probes, PCR and activit test
    • Le Jeune, C., Lonvaud-Funel, A., Ten Brink, B., Holstra, H., and. van der Vossen, J.M.B.M. (1995). Development of a detection system for histidine decarboxylating lactic acid bacteria based on DNA probes, PCR and activit test. J. Appl. Bacteriol. 78: 316-326.
    • (1995) J. Appl. Bacteriol. , vol.78 , pp. 316-326
    • Le Jeune, C.1    Lonvaud-Funel, A.2    ten Brink, B.3    Holstra, H.4    van der Vossen, J.M.B.M.5
  • 43
    • 0034733877 scopus 로고    scopus 로고
    • Histamine fish poisoning revisited
    • Lehane, L. and Olley, J. (2000). Histamine fish poisoning revisited. Int. J. Food Microbiol. 58: 1-37.
    • (2000) Int. J. Food Microbiol. , vol.58 , pp. 1-37
    • Lehane, L.1    Olley, J.2
  • 44
    • 0031764614 scopus 로고    scopus 로고
    • Effect of enhanced proteolysis on formation of biogenic amines by lactobacilli during Gouda cheese ripening
    • Leuschner, R.G.K., Kurihara, R., and Hammes,W.P. (1998). Effect of enhanced proteolysis on formation of biogenic amines by lactobacilli during Gouda cheese ripening. Int. J. Food Microbiol. 44: 15-20.
    • (1998) Int. J. Food Microbiol. , vol.44 , pp. 15-20
    • Leuschner, R.G.K.1    Kurihara, R.2    Hammes, W.P.3
  • 45
    • 33846912925 scopus 로고    scopus 로고
    • The gene cluster for agmatine catabolism of Enterococcus faecalis
    • Studies of recombinant putrescine transcarbamylase and agmatine deiminase catalyzing this reaction
    • Lácer, J.L., Polo, L.M., Tavarez, S., Alarcón, B., Hilario, R., and Rubio, V. (2006). The gene cluster for agmatine catabolism of Enterococcus faecalis. Studies of recombinant putrescine transcarbamylase and agmatine deiminase catalyzing this reaction. J. Bacteriol. 189: 1254-1265.
    • (2006) J. Bacteriol. , vol.189 , pp. 1254-1265
    • Lácer, J.L.1    Polo, L.M.2    Tavarez, S.3    Alarcón, B.4    Hilario, R.5    Rubio, V.6
  • 46
    • 0028040693 scopus 로고
    • Evaluation of histidine decarboxylase activity of bacteria isolated from sardine (Sardina pilchardus) by an enzymatic method
    • López-Sabater, E.I., RodrÍguez-Jerez, J.J., Hernández-Herrero, M., and Mora- Ventura, M.T. (1994). Evaluation of histidine decarboxylase activity of bacteria isolated from sardine (Sardina pilchardus) by an enzymatic method. Lett. Appl. Microbiol. 19: 70-75.
    • (1994) Lett. Appl Microbiol. , vol.19 , pp. 70-75
    • López-Sabater, E.I.1    Rodríguez-Jerez, J.J.2    Hernández-Herrero, M.3    Mora-Ventura, M.T.4
  • 47
    • 38949168229 scopus 로고    scopus 로고
    • High frequency of histamine-producing bacteria in the enological environment and instability of the histidine decarboxylase production phenotype
    • Lucas, P.M., Claisse, O., and Lonvaud-Funel, A. (2008). High frequency of histamine-producing bacteria in the enological environment and instability of the histidine decarboxylase production phenotype. Appl. Environ. Microbiol. 74: 811-817.
    • (2008) Appl. Environ Microbiol. , vol.74 , pp. 811-817
    • Lucas, P.M.1    Claisse, O.2    Lonvaud-Funel, A.3
  • 48
    • 34447517605 scopus 로고    scopus 로고
    • Agmatine deiminase pathway genes in Lactobacillus brevis are linked to the tyrosine decarboxylation operon in a putative acid resistance locus
    • Lucas, P.M., Blancato,V.S., Claisse, O., Magni, C., Lolkema, J.S., and Lonvaud- Funel, A. (2007). Agmatine deiminase pathway genes in Lactobacillus brevis are linked to the tyrosine decarboxylation operon in a putative acid resistance locus. Microbiology 153: 2221-2230.
    • (2007) Microbiology , vol.153 , pp. 2221-2230
    • Lucas, P.M.1    Blancato, V.S.2    Claisse, O.3    Magni, C.4    Lolkema, J.S.5    Lonvaud-Funel, A.6
  • 49
    • 15444363094 scopus 로고    scopus 로고
    • Histamine-producing pathway encoded on an unstable plasmid in Lactobacillus hilgardii 0006
    • Lucas, P.M., Wolken, W.A., Claisse, O., Lolkema, J.S., and Lonvaud-Funel, A. (2005). Histamine-producing pathway encoded on an unstable plasmid in Lactobacillus hilgardii 0006 Appl. Environ. Microbiol. 71: 1417- 1424.
    • (2005) Appl. Environ Microbiol. , vol.71 , pp. 1417-1424
    • Lucas, P.M.1    Wolken, W.A.2    Claisse, O.3    Lolkema, J.S.4    Lonvaud-Funel, A.5
  • 50
    • 0344307647 scopus 로고    scopus 로고
    • The tyrosine decarboxylase operon of Lactobacillus brevis IOEB 9809: Characterization and conservation in tyramine producing bacteria
    • Lucas, P.M., Landete, J., Coton, M., Coton, E., and Lonvaud-Funel, A. (2003). The tyrosine decarboxylase operon of Lactobacillus brevis IOEB 9809: Characterization and conservation in tyramine producing bacteria. FEMS Microbiol. Lett. 229: 65-71.
    • (2003) Lett. FEMS Microbiol. , vol.229 , pp. 65-71
    • Lucas, P.M.1    Landete, J.2    Coton, M.3    Coton, E.4    Lonvaud-Funel, A.5
  • 51
    • 0037150038 scopus 로고    scopus 로고
    • Purification and partial gene sequence of the tyrosine decarboxylase of Lactobacillus brevis IOEB 9809
    • Lucas, P.M. and Lonvaud-Funel, A. (2002). Purification and partial gene sequence of the tyrosine decarboxylase of Lactobacillus brevis IOEB 9809. FEMS Microbiol. Lett. 211: 85-89.
    • (2002) FEMS Microbiol Lett , vol.211 , pp. 85-89
    • Lucas, P.M.1    Lonvaud-Funel, A.2
  • 52
    • 2442550838 scopus 로고    scopus 로고
    • The biogenic amine tyramine modulates the adherence of Escherichia coli O157:H7 to intestinal mucosa
    • Lyte, M. (2004). The biogenic amine tyramine modulates the adherence of Escherichia coli O157:H7 to intestinal mucosa. J. Food Prot. 67: 878-883.
    • (2004) J. Food Prot. , vol.67 , pp. 878-883
    • Lyte, M.1
  • 53
    • 0027181161 scopus 로고
    • Formation of histamine and tyramine by some lactic acid bacteria in MRS-broth and modified decarboxylation agar
    • Maijala, R.L. (1993). Formation of histamine and tyramine by some lactic acid bacteria in MRS-broth and modified decarboxylation agar 17: 40-43.
    • (1993) Lett. Appl. Microbiol. Lett. Appl. , vol.17 , pp. 40-43
    • Maijala, R.L.1
  • 54
    • 33645471027 scopus 로고    scopus 로고
    • First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
    • Marcobal, A., de las Rivas, B., Moreno-Arribas, M.V., and Muñoz, R. (2006a). First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58. FEMS Microbiol. Lett. 258: 144-149.
    • (2006) Lett FEMS Microbiol , vol.258 , pp. 144-149
    • Marcobal, A.1    de las Rivas, B.2    Moreno-Arribas, M.V.3    Ñoz, R.4
  • 55
    • 33845539696 scopus 로고    scopus 로고
    • Evidence for horizontal gene transfer as origin of putrescine production in Oenococcus oeni RM83
    • Marcobal, A., de las Rivas, B., Moreno-Arribas, M.V., and Muñoz, R. (2006b). Evidence for horizontal gene transfer as origin of putrescine production in Oenococcus oeni RM83. Appl. Environ. Microbiol. 72: 7954-7958.
    • (2006) Microbiol Appl. Environ. , vol.72 , pp. 7954-7958
    • Marcobal, A.1    de las Rivas, B.2    Moreno-Arribas, M.V.3    Ñoz, R.4
  • 56
    • 33744504634 scopus 로고    scopus 로고
    • A multifactorial design for studying factors influencing growth and tyramine production of the lactic acid bacteria Lactobacillus brevis CECT 4669 and BIFI-58
    • Marcobal, A., Martín-Alvarez, P.J., Moreno-Arribas M.V., and Muñoz, R. (2006c). A multifactorial design for studying factors influencing growth and tyramine production of the lactic acid bacteria Lactobacillus brevis CECT 4669 and BIFI-58. Res. Microbiol. 157: 417-424.
    • (2006) Res Microbiol , vol.157 , pp. 417-424
    • Marcobal, A.1    Martín-Alvarez, P.J.2    Moreno-Arribas, M.V.3    Muñoz, R.4
  • 57
    • 17144405314 scopus 로고    scopus 로고
    • Multiplex PCR method for the simultaneous detection of histamine-,tyramine-, and putrescine-producing lactic acid bacteria in foods
    • Marcobal, A., de las Rivas, B., Moreno-Arribas, M.V., and Muñoz, R. (2005). Multiplex PCR method for the simultaneous detection of histamine-,tyramine-, and putrescine-producing lactic acid bacteria in foods. J. Food Prot. 68: 874-878.
    • (2005) J. Food Prot. , vol.68 , pp. 874-878
    • Marcobal, A.1    de las Rivas, B.2    Moreno-Arribas, M.V.3    Ñoz, R.4
  • 58
    • 5144228141 scopus 로고    scopus 로고
    • Identification of the ornithine decarboxylase gene in the putrescine-producer Oenococcus oeni BIFI-83
    • Marcobal, A., de las Rivas, B., Moreno-Arribas, M.V., and Muñoz, R. (2004). Identification of the ornithine decarboxylase gene in the putrescine-producer Oenococcus oeni BIFI-83. FEMS Microbiol. Lett. 239: 213-220.
    • (2004) Lett FEMS Microbiol , vol.239 , pp. 213-220
    • Marcobal, A.1    de las Rivas, B.2    Moreno-Arribas, M.V.3    Muñoz, R.4
  • 59
    • 0033841986 scopus 로고    scopus 로고
    • The capacity of Enterobacteriaceae species to produce biogenic amines in cheese
    • Marino, M., Maifreni, M., Moret, S., and Rondinini, G. (2000). The capacity of Enterobacteriaceae species to produce biogenic amines in cheese. Lett. Appl. Microbiol. 31: 169-173.
    • (2000) Microbiol Lett. Appl. , vol.31 , pp. 169-173
    • Marino, M.1    Maifreni, M.2    Moret, S.3    Rondinini, G.4
  • 60
    • 33750341148 scopus 로고    scopus 로고
    • Comparative genomics of the lactic acid bacteria
    • USA
    • Makarova, K., Slesarev, A., Wolf, Y., et al. (2006). Comparative genomics of the lactic acid bacteria. Proc. Natl. Acad. Sci. U. S. A. 103: 15611-15616.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 15611-15616
    • Makarova, K.1    Slesarev, A.2    Wolf, Y.3
  • 61
    • 17644419266 scopus 로고    scopus 로고
    • Sequencing, characterization and transcriptional analysis of the histidine decarboxylase operon of Lactobacillus buchneri
    • Martín, M.C., Fernández, M., Linares, D.M., and Alvarez, M.A. (2005). Sequencing, characterization and transcriptional analysis of the histidine decarboxylase operon of Lactobacillus buchneri. Microbiology. 151: 1219-1228.
    • (2005) Microbiology , vol.151 , pp. 1219-1228
    • Martín, M.C.1    Fernández, M.2    Linares, D.M.3    Alvarez, M.A.4
  • 62
    • 0026772547 scopus 로고
    • Nucleotide sequence of the Escherichia coli cad operon: A system for neutralization of low extracellular pH
    • Meng, S.Y. and Bennett, G.N. (1992). Nucleotide sequence of the Escherichia coli cad operon: A system for neutralization of low extracellular pH. J. Bacteriol. 74: 2659-2669.
    • (1992) J. Bacteriol. , vol.74 , pp. 2659-2669
    • Meng, S.Y.1    Bennett, G.N.2
  • 63
    • 0027191082 scopus 로고
    • Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri
    • Molenaar, D., Bosscher, J.S., Ten Brink, B., Driessen, A.J.M., and Konings, W.N. (1993). Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri. J. Bacteriol. 175: 2864-2870.
    • (1993) J. Bacteriol. , vol.175 , pp. 2864-2870
    • Molenaar, D.1    Bosscher, J.S.2    Ten Brink, B.3    Driessen, A.J.M.4    Konings, W.N.5
  • 64
    • 0028921425 scopus 로고
    • Structural motifs for pyridoxal-50-phosphate binding in decarboxylases: An analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase
    • Momany, C., Ghosh, R., and Hackert, M.L. (1995) Structural motifs for pyridoxal-50-phosphate binding in decarboxylases: An analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase. Prot. Sci. 4: 849-854.
    • (1995) Prot Sci. , vol.4 , pp. 849-854
    • Momany, C.1    Ghosh, R.2    Hackert, M.L.3
  • 65
    • 0035808975 scopus 로고    scopus 로고
    • Purification and characterization of tyrosine decarboxylase of Lactobacillus brevis
    • Moreno-Arribas, M.V. and Lonvaud-Funel, A. (2001). Purification and characterization of tyrosine decarboxylase of Lactobacillus brevis.FEMSMicrobiol. Lett. 195: 103-107.
    • (2001) Lett FEMSMicrobiol , vol.195 , pp. 103-107
    • Moreno-Arribas, M.V.1    Lonvaud-Funel, A.2
  • 66
    • 0029812095 scopus 로고    scopus 로고
    • Kinetics of expression of the Escherichia coli cad operon as a function of pH and lysine
    • Neely, M.N. and Olson, E.R. (1996). Kinetics of expression of the Escherichia coli cad operon as a function of pH and lysine. J. Bacteriol. 178: 5522-5528.
    • (1996) J. Bacteriol. , vol.178 , pp. 5522-5528
    • Neely, M.N.1    Olson, E.R.2
  • 67
    • 2542596304 scopus 로고    scopus 로고
    • Evaluation of biogenic amines and microbial counts throughout the ripening of goat cheeses from pasteurized and raw milk
    • Novella-Rodríguez, S., Veciana-Nogués,M.T., Roig-Sagués, A., Trujillo-Mesa, A., and Vidal-Carou, M.C. (2004) Evaluation of biogenic amines and microbial counts throughout the ripening of goat cheeses from pasteurized and raw milk. J. Dairy Res. 71: 245-252.
    • (2004) J. Dairy Res. , vol.71 , pp. 245-252
    • Novella, R.S.1    Veciana, N.M.T.2    Roig, S.A.3    Trujillo, M.A.4    Vidal, C.M.C.5
  • 68
    • 0037394597 scopus 로고    scopus 로고
    • Distribution of biogenic amines and polyamines in cheese
    • Novella-Rodríguez, S.,Veciana-Nogués,M.T., Izquierdo-Pulido, M., andVidal-Carou, M.C. (2003a). Distribution of biogenic amines and polyamines in cheese. J. Food Sci. 68: 750-755.
    • (2003) J. Food Sci. , vol.68 , pp. 750-755
    • Novella, R.S.1    Veciana, N.M.T.2    Izquierdo, P.M.3    Vidal, C.M.C.4
  • 69
    • 0036812275 scopus 로고    scopus 로고
    • Profile of biogenic amines in goat cheese made from pasteurized and pressurized milks
    • Novella-Rodríguez, S., Veciana-Nogués, M.T., Trujillo-Mesa, A.J., and Vidal- Carou, M.C. (2003b). Profile of biogenic amines in goat cheese made from pasteurized and pressurized milks. J. Food Sci. 67: 2940-2944.
    • (2003) J. Food Sci. , vol.67 , pp. 2940-2944
    • Novella, R.S.1    Veciana, N.M.T.2    Trujillo, M.A.J.3    Vidal, C.M.C.4
  • 70
    • 0036780392 scopus 로고    scopus 로고
    • Influence of starter and non starter bacteria on the formation of biogenic amines in goat cheese during ripening
    • Novella-Rodríguez, S., Veciana-Nogués,M.T., Roig-Sagués, A., Trujillo-Mesa, A., and Vidal-Carou, M.C. (2002). Influence of starter and non starter bacteria on the formation of biogenic amines in goat cheese during ripening. J. Dairy Sci. 85: 2471-2478.
    • (2002) J. Dairy Sci. , vol.85 , pp. 2471-2478
    • Novella, R.S.1    Veciana, N.M.T.2    Roig, S.A.3    Trujillo, M.A.4    Vidal, C.M.C.5
  • 71
    • 0034730868 scopus 로고    scopus 로고
    • Electromigration methods for amino acids, biogenic amines and aromatic amines
    • Oguri, S. (2000). Electromigration methods for amino acids, biogenic amines and aromatic amines. J. Chromatogr B Biomed. Sci. Appl. 747: 1-19.
    • (2000) J. Chromatogr B Biomed. Sci. Appl. , vol.747 , pp. 1-19
    • Oguri, S.1
  • 72
    • 33947525787 scopus 로고    scopus 로고
    • A review: Current analytical methods for the determination of biogenic amines in food
    • Õnal, A. (2007). A review: Current analytical methods for the determination of biogenic amines in food. Food Chem. 103: 1475-1486.
    • (2007) Food Chem , vol.103 , pp. 1475-1486
    • Õnal, A.1
  • 73
    • 0030778609 scopus 로고    scopus 로고
    • Formation of biogenic amines in Idiazabal ewe's-milk cheese: Effect of ripening, pasteurization, and starter
    • Ordnez, A.I., Ibãnez, F.C., Torre, P., and Barcina, Y. (1997). Formation of biogenic amines in Idiazabal ewe's-milk cheese: effect of ripening, pasteurization, and starter. J. Food Prot. 60: 1371-1375.
    • (1997) J. Food Prot. , vol.60 , pp. 1371-1375
    • Ordnez, A.I.1    Ibãnez, F.C.2    Torre, P.3    Barcina, Y.4
  • 74
    • 0037470983 scopus 로고    scopus 로고
    • Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis
    • Paulsen, I.T., Banerjei, L., Myers, G.S., et al. (2003). Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science. 299: 2071-2074.
    • (2003) Science , vol.299 , pp. 2071-2074
    • Paulsen, I.T.1    Banerjei, L.2    Myers, G.S.3
  • 75
    • 0029897729 scopus 로고    scopus 로고
    • Internal pH crisis, lysine decarboxylase, and the acid tolerance response of Salmonella typhimurium
    • Park, Y.K., Bearson, B., Bang, S.H., Bang, I.S., and Foster, J.W. (1996). Internal pH crisis, lysine decarboxylase, and the acid tolerance response of Salmonella typhimurium. Mol. Microbiol. 20: 605-611.
    • (1996) Mol Microbiol , vol.20 , pp. 605-611
    • Park, Y.K.1    Bearson, B.2    Bang, S.H.3    Bang, I.S.4    Foster, J.W.5
  • 76
    • 0022382113 scopus 로고
    • Structure determination of histidine decarboxylase from Lactobacillus 30A at 3.0 Å resolution
    • Parks, E.H., Ernst, S.R., Hamlin, R., Xuong, N.H., and Hackert, M.L. (1985). Structure determination of histidine decarboxylase from Lactobacillus 30A at 3.0 Å resolution. J. Mol. Biol. 182: 455-465.
    • (1985) J. Mol. Biol , vol.182 , pp. 455-465
    • Parks, E.H.1    Ernst, S.R.2    Hamlin, R.3    Xuong, N.H.4    Hackert, M.L.5
  • 77
    • 10444268162 scopus 로고    scopus 로고
    • Interrelationships among microbial, physiochemical, and biochemical properties of Terrincho cheese, with emphasis on biogenic amines
    • Pinho, P., Pintado, A.I.E., Gomes, A.M.P., Pintado, M.M.E.,Malcasa, F.X., and Ferreira, I.M. (2004). Interrelationships among microbial, physiochemical, and biochemical properties of Terrincho cheese, with emphasis on biogenic amines. J. Food Prot. 67: 2779-2785.
    • (2004) J. Food Prot. , vol.67 , pp. 2779-2785
    • Pinho, P.1    Pintado, A.I.E.2    Gomes, A.M.P.3    Pintado, M.M.E.4    Malcasa, F.X.5    Ferreira, I.M.6
  • 78
    • 34648825698 scopus 로고    scopus 로고
    • Formation of cadaverine, histamine, putrescine and tyramine by bacteria isolated from meat, fermented sausages and cheeses
    • Pircher, A., Bauer, F., and Paulsen, P. (2007). Formation of cadaverine, histamine, putrescine and tyramine by bacteria isolated from meat, fermented sausages and cheeses. Eur. Food Res. Technol. 226: 225-231.
    • (2007) Eur. Food Res. Technol. , vol.226 , pp. 225-231
    • Pircher, A.1    Bauer, F.2    Paulsen, P.3
  • 80
    • 0021912751 scopus 로고
    • Pyruvoyl-dependent histidine decarboxylases-mechanism of cleavage of the proenzyme from Lactobacillus buchneri
    • Recsei, P.A. and Snell, E.E. (1985). Pyruvoyl-dependent histidine decarboxylases-mechanism of cleavage of the proenzyme from Lactobacillus buchneri. J. Biol. Chem. 260: 2804-2806.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2804-2806
    • Recsei, P.A.1    Snell, E.E.2
  • 81
    • 0020710757 scopus 로고
    • Conversion of prohistidine decarboxylase to histidine-decarboxylase-peptide-chain cleavage by non-hydrolytic serinolysis
    • USA
    • Recsei, P.A., Huynh, Q.K., and Snell, E.E. (1983). Conversion of prohistidine decarboxylase to histidine-decarboxylase-peptide-chain cleavage by non-hydrolytic serinolysis. Proc. Natl. Acad. Sci. U. S. A. 80: 973- 977.
    • (1983) Proc. Natl. Acad. Sci. , vol.80 , pp. 973-977
    • Recsei, P.A.1    Huynh, Q.K.2    Snell, E.E.3
  • 82
    • 27744486054 scopus 로고    scopus 로고
    • CadC activates pHdependent expression of the Vibrio vulnificus cadBA operon at a distance through direct binding to an upstream region
    • Rhee, J.E., Kim, K.S., and Choi, S.H. (2005). CadC activates pHdependent expression of the Vibrio vulnificus cadBA operon at a distance through direct binding to an upstream region. J. Bacteriol. 187: 7870-7875.
    • (2005) J. Bacteriol. , vol.187 , pp. 7870-7875
    • Rhee, J.E.1    Kim, K.S.2    Choi, S.H.3
  • 83
    • 0037022969 scopus 로고    scopus 로고
    • Identification of the cadBA operon from Vibrio vulnificus and its influence on survival to acid stress
    • Rhee, J.E., Rhee, J.H., Ryu, P.Y., and Choi, S.H. (2002). Identification of the cadBA operon from Vibrio vulnificus and its influence on survival to acid stress. FEMS Microbiol. Letts. 208: 245-251.
    • (2002) Letts FEMS Microbiol , vol.208 , pp. 245-251
    • Rhee, J.E.1    Rhee, J.H.2    Ryu, P.Y.3    Choi, S.H.4
  • 85
    • 0031132958 scopus 로고    scopus 로고
    • Gas chromatographic method for putrescine and cadaverine in canned tuna and mahimahi and fluorometric method for histamine (minor modification of AOAC Official Method 977.13): Collaborative study
    • Rogers, P.L. and Staruszkiewicz, W. (1997). Gas chromatographic method for putrescine and cadaverine in canned tuna and mahimahi and fluorometric method for histamine (minor modification of AOAC Official Method 977.13): collaborative study. J. AOAC Int. 80: 591-602.
    • (1997) J. AOAC Int. , vol.80 , pp. 591-602
    • Rogers, P.L.1    Staruszkiewicz, W.2
  • 86
    • 0037409630 scopus 로고    scopus 로고
    • Bioactive amines formation in milk by Lactococcus in the presence or not of rennet and NaCl at 20 and 32°C
    • 595-506
    • Santos W.C., Souza, M.R., Cerqueira, M.M.O.P., and Gĺoria, M.B.A. (2003). Bioactive amines formation in milk by Lactococcus in the presence or not of rennet and NaCl at 20 and 32°C. Food Chem. 81: 595-506.
    • (2003) Food Chem , vol.81
    • Santos, W.C.1    Souza, M.R.2    Cerqueira, M.M.O.P.3
  • 87
    • 0035793712 scopus 로고    scopus 로고
    • PH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus
    • Schelp E., Worley, S., Monzingo, A.F., Ernst, S., and Robertus, J.D. (2001). pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a. J. Mol. Biol. 306: 727-732.
    • (2001) J. Mol. Biol. , vol.306 , Issue.30 , pp. 727-732
    • Schelp, E.1    Worley, S.2    Monzingo, A.F.3    Ernst, S.4    Robertus, J.D.5
  • 88
    • 0033763135 scopus 로고    scopus 로고
    • Polyamine transport and role of potE in response to osmotic stress in Escherichia coli
    • Schiller, D., Kruse, D., Kneifel, H., Krãmer, R., and Burkovski, A. (2000). Polyamine transport and role of potE in response to osmotic stress in Escherichia coli. J. Bacteriol. 182: 6247-6249.
    • (2000) J. Bacteriol. , vol.182 , pp. 6247-6249
    • Schiller, D.1    Kruse, D.2    Kneifel, H.3    Krãmer, R.4    Burkovski, A.5
  • 89
    • 0030265217 scopus 로고    scopus 로고
    • Significance of biogenic amines to food safety and human health
    • Shalaby, A.R. (1996). Significance of biogenic amines to food safety and human health. Food Res. Int. 29: 675-690.
    • (1996) Int Food Res , vol.29 , pp. 675-690
    • Shalaby, A.R.1
  • 90
    • 0005225952 scopus 로고    scopus 로고
    • Biogenic amines: Their importance in foods
    • Silla Santos, M.H. (1996). Biogenic amines: Their importance in foods. Int. J. Food Microbiol. 29: 213-231
    • (1996) Int. J. Food Microbiol. , vol.29 , pp. 213-231
    • Silla Santos, M.H.1
  • 91
    • 0020422867 scopus 로고
    • Enzymes of the agamatine degradation and the control of their synthesis in Streptococcus faecalis
    • Simon, J.P. and Stalon, V. (1982). Enzymes of the agamatine degradation and the control of their synthesis in Streptococcus faecalis. J. Bacteriol. 152: 676-681.
    • (1982) J. Bacteriol. , vol.152 , pp. 676-681
    • Simon, J.P.1    Stalon, V.2
  • 92
    • 1542721578 scopus 로고    scopus 로고
    • Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli
    • Soksawatmaekhin, W., Kuraishi, A., Sakata, K., Kashiwagi, K., and Igarashi, K. (2004). Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli. Mol. Microbiol. 51: 1401-1412.
    • (2004) Mol Microbiol , vol.51 , pp. 1401-1412
    • Soksawatmaekhin, W.1    Kuraishi, A.2    Sakata, K.3    Kashiwagi, K.4    Igarashi, K.5
  • 93
    • 0028798082 scopus 로고
    • Amino acid transporters of lower eukaryotes: Regulation, structure and topogenesis
    • Sophianopoulou, V. and Diallinas, G. (1995). Amino acid transporters of lower eukaryotes: regulation, structure and topogenesis. FEMS Microbiol. Rev. 16: 53-75.
    • (1995) FEMS Microbiol Rev , vol.16 , pp. 53-75
    • Sophianopoulou, V.1    Diallinas, G.2
  • 94
    • 84964316661 scopus 로고
    • Biogenic amines in cheese and other fermented foods: A review
    • Stratton, J.E., Hutkins, R.W., and Taylor, S.L. (1991). Biogenic amines in cheese and other fermented foods: A review. J. Food Prot. 54: 460- 470.
    • (1991) J. Food Prot. , vol.54 , pp. 460-470
    • Stratton, J.E.1    Hutkins, R.W.2    Taylor, S.L.3
  • 95
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor, C.W. and Tabor, H. (1985). Polyamines in microorganisms. Microbiol. Rev. 49: 81-99.
    • (1985) Microbiol Rev , vol.49 , pp. 81-99
    • Tabor, C.W.1    Tabor, H.2
  • 96
    • 0038221148 scopus 로고    scopus 로고
    • Cloning and sequencing of the histidine decarboxylase genes of gram-negative, histamine-producing bacteria and their application in detection and identificatio of these organisms in fish
    • Takahashi, H., Kimura, B., Yoshikawa, M., and Fujii, T. (2003). Cloning and sequencing of the histidine decarboxylase genes of gram-negative, histamine-producing bacteria and their application in detection and identificatio of these organisms in fish. Appl. Environ. Microbiol. 69: 2568- 2579.
    • (2003) Appl. Environ Microbiol. , vol.69 , pp. 2568-2579
    • Takahashi, H.1    Kimura, B.2    Yoshikawa, M.3    Fujii, T.4
  • 97
    • 0003470848 scopus 로고
    • Histamine poisoning associated with fish, cheese and other foods
    • FAO/WHO monograph CX/PH 83/11. Taylor, S.L. and Sumner, S.S. Determination of histamine, putrescine, and cadaverine., Elsevier, Amsterdam
    • Taylor, S.L. (1983) Histamine poisoning associated with fish, cheese and other foods. FAO/WHO monograph CX/PH 83/11. Taylor, S.L. and Sumner, S.S. (1986). Determination of histamine, putrescine, and cadaverine., Elsevier, Amsterdam.
    • (1983) Cheese and other foods.
    • Taylor, S.L.1
  • 99
    • 0035919670 scopus 로고    scopus 로고
    • Complete genome sequence of a virulent isolate of Streptococcus pneumoniae
    • Tettelin, H., Nelson, K.E., Paulsen, I.T., et al. (2001). Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science. 293: 498- 506.
    • (2001) Science , vol.293 , pp. 498-506
    • Tettelin, H.1    Nelson, K.E.2    Paulsen, I.T.3
  • 100
    • 0034923283 scopus 로고    scopus 로고
    • The role of the natural polyamine putrescine in defense against oxidative stress in Escherichia coli
    • Tkachenko, A., Nesterova, L., and Pshenichnov, M. (2001). The role of the natural polyamine putrescine in defense against oxidative stress in Escherichia coli. Arch. Microbiol. 176: 155-157.
    • (2001) Arch Microbiol , vol.176 , pp. 155-157
    • Tkachenko, A.1    Nesterova, L.2    Pshenichnov, M.3
  • 103
    • 0025190927 scopus 로고
    • Cloning, sequencing, expression, and site-directed mutagenesis of the gene from Clostridium perfringens encoding pyruvoyl-dependent histidine decarboxylase
    • Van Poelje, P.D. and Snell, E.E. (1990). Cloning, sequencing, expression, and site-directed mutagenesis of the gene from Clostridium perfringens encoding pyruvoyl-dependent histidine decarboxylase. Biochem. 29: 132- 139.
    • (1990) Biochem , vol.29 , pp. 132-139
    • van Poelje, P.D.1    Snell, E.E.2
  • 104
    • 1542376972 scopus 로고    scopus 로고
    • Proteome analyses of heme-dependent respiration in Lactococcus lactis: Involvement of the proteolytic system
    • Vido, K., Le Bars, D., Mistou, M.Y., Anglade, P., Gruss, A., and Gaudu, P. (2004). Proteome analyses of heme-dependent respiration in Lactococcus lactis: Involvement of the proteolytic system. J. Bacteriol. 186: 1648-1657.
    • (2004) J. Bacteriol. , vol.186 , pp. 1648-1657
    • Vido, K.1    Le Bars, D.2    Mistou, M.Y.3    Anglade, P.4    Gruss, A.5    Gaudu, P.6
  • 105
    • 8844233526 scopus 로고    scopus 로고
    • Histamine intolerance-like symptoms in healthy volunteers after oral provocation with liquid histamine
    • Wöhrl, S., Hemmer, W., Focke, M., Rappersberger, K., and Jarisch, R. (2004). Histamine intolerance-like symptoms in healthy volunteers after oral provocation with liquid histamine. Allergy Asthma Proc. 25: 305- 311.
    • (2004) Allergy Asthma Proc , vol.25 , pp. 305-311
    • Wöhrl, S.1    Hemmer, W.2    Focke, M.3    Rappersberger, K.4    Jarisch, R.5
  • 106
    • 33644864295 scopus 로고    scopus 로고
    • The mechanism of the tyrosine transporter TyrP supports a proton motive tyrosine decarboxylation pathway in Lactobacillus brevis
    • Wolken, W.A., Lucas, P.M., Lonvaud-Funel, A., and Lolkema, J.S. (2006). The mechanism of the tyrosine transporter TyrP supports a proton motive tyrosine decarboxylation pathway in Lactobacillus brevis. J. Bacteriol. 188: 2198- 2206.
    • (2006) J. Bacteriol. , vol.188 , pp. 2198-2206
    • Wolken, W.A.1    Lucas, P.M.2    Lonvaud-Funel, A.3    Lolkema, J.S.4
  • 107
    • 0010764408 scopus 로고    scopus 로고
    • Role of selected yeasts in cheese ripening: An evaluation in foil wrapped Raclette cheese
    • Wyder, M.T., Bachmann, H.P., and Puhan, Z. (1999). Role of selected yeasts in cheese ripening: An evaluation in foil wrapped Raclette cheese. Lebensm.- Wiss. Technol. 32: 333-343.
    • (1999) Lebensm.-WissTechnol , vol.32 , pp. 333-343
    • Wyder, M.T.1    Bachmann, H.P.2    Puhan, Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.