메뉴 건너뛰기




Volumn 15, Issue 4, 2016, Pages 801-826

Biogenic Amines in Dairy Products: Origin, Incidence, and Control Means

Author keywords

biogenic amines; biosynthesis; control; dairy products

Indexed keywords

AMINES; BIOCHEMISTRY; BIOSYNTHESIS; CARBOXYLATION; CONTROL ENGINEERING; DAIRY PRODUCTS; DECISION MAKING; III-V SEMICONDUCTORS; LACTIC ACID; RISK ASSESSMENT;

EID: 84971268430     PISSN: None     EISSN: 15414337     Source Type: Journal    
DOI: 10.1111/1541-4337.12212     Document Type: Article
Times cited : (211)

References (212)
  • 1
    • 61449218052 scopus 로고    scopus 로고
    • Biogenic amines in fish: roles in intoxication, spoilage, and nitrosamine formation—a review
    • Al Bulushi I, Poole S, Deeth HC, Dykes GA. 2009. Biogenic amines in fish: roles in intoxication, spoilage, and nitrosamine formation—a review. Crit Rev Food Sci Nutr 49:369–77.
    • (2009) Crit Rev Food Sci Nutr , vol.49 , pp. 369-377
    • Al Bulushi, I.1    Poole, S.2    Deeth, H.C.3    Dykes, G.A.4
  • 2
    • 0028236794 scopus 로고
    • Decrease in ornithine decarboxylase activity after eradication of Helicobacter pylori
    • Alam K, Arlow FL, Ma CK, Schubert TT. 1994. Decrease in ornithine decarboxylase activity after eradication of Helicobacter pylori. Am J Gastr 89:888–93.
    • (1994) Am J Gastr , vol.89 , pp. 888-893
    • Alam, K.1    Arlow, F.L.2    Ma, C.K.3    Schubert, T.T.4
  • 3
    • 84961660140 scopus 로고    scopus 로고
    • Effect of gamma irradiation on the quality and safety of Egyptian Karish cheese
    • Aly SA, Farag DE, Galal E. 2012. Effect of gamma irradiation on the quality and safety of Egyptian Karish cheese. J Am Sci 8:761–6.
    • (2012) J Am Sci , vol.8 , pp. 761-766
    • Aly, S.A.1    Farag, D.E.2    Galal, E.3
  • 4
    • 33847101288 scopus 로고    scopus 로고
    • Selection criteria for lactic acid bacteria to be used as functional starter cultures in dry sausage production: an update
    • Ammor MS, Mayo B. 2007. Selection criteria for lactic acid bacteria to be used as functional starter cultures in dry sausage production: an update. Meat Sci 76:138–46.
    • (2007) Meat Sci , vol.76 , pp. 138-146
    • Ammor, M.S.1    Mayo, B.2
  • 5
    • 77957839148 scopus 로고    scopus 로고
    • Determination of biogenic amines in herby cheese
    • Andic SH, Genccelep H, Kose S. 2010. Determination of biogenic amines in herby cheese. Int J Food Prop 13:1300–14.
    • (2010) Int J Food Prop , vol.13 , pp. 1300-1314
    • Andic, S.H.1    Genccelep, H.2    Kose, S.3
  • 6
    • 0016764372 scopus 로고
    • Biodegradative ornithine decarboxylase of Escherichia coli. Purification, properties and pyridoxal 5′-phosphate binding site
    • Applebaum D, Sabo DL, Fischer EH, Morris DR. 1975. Biodegradative ornithine decarboxylase of Escherichia coli. Purification, properties and pyridoxal 5′-phosphate binding site. Biochemistry 14:3675–81.
    • (1975) Biochemistry , vol.14 , pp. 3675-3681
    • Applebaum, D.1    Sabo, D.L.2    Fischer, E.H.3    Morris, D.R.4
  • 7
    • 0035134087 scopus 로고    scopus 로고
    • Biogenic amine production by Lactobacillus
    • Arena ME, Manca de Nadra MC. 2001. Biogenic amine production by Lactobacillus. J Appl Microbiol 90:158–62.
    • (2001) J Appl Microbiol , vol.90 , pp. 158-162
    • Arena, M.E.1    Manca de Nadra, M.C.2
  • 8
    • 0032705196 scopus 로고    scopus 로고
    • Arginine, citrulline, and ornithine metabolism by lactic acid bacteria from wine
    • Arena ME, Saguir FM, Manca de Nadra MC. 1999. Arginine, citrulline, and ornithine metabolism by lactic acid bacteria from wine. Int J Food Microbiol 52:155–61.
    • (1999) Int J Food Microbiol , vol.52 , pp. 155-161
    • Arena, M.E.1    Saguir, F.M.2    Manca de Nadra, M.C.3
  • 11
    • 0036842085 scopus 로고    scopus 로고
    • Gene structure, organization, expression, and potential regulatory mechanisms of arginine catabolism in Enterococcus faecalis
    • Barcelona-Andres B, Marina A, Rubio V. 2002. Gene structure, organization, expression, and potential regulatory mechanisms of arginine catabolism in Enterococcus faecalis. J Bacteriol 184:6289–300.
    • (2002) J Bacteriol , vol.184 , pp. 6289-6300
    • Barcelona-Andres, B.1    Marina, A.2    Rubio, V.3
  • 12
    • 58649122671 scopus 로고    scopus 로고
    • Antimicrobial activity of lysozyme with special relevance to milk
    • Benkerroum N. 2008. Antimicrobial activity of lysozyme with special relevance to milk. Af J Biotechnol 7:4856–67.
    • (2008) Af J Biotechnol , vol.7 , pp. 4856-4867
    • Benkerroum, N.1
  • 13
    • 77954370007 scopus 로고    scopus 로고
    • Antimicrobial peptide generated from milk: a survey and prospects for application in the food industry: a review
    • Benkerroum N. 2010. Antimicrobial peptide generated from milk: a survey and prospects for application in the food industry: a review. Int J Dairy Technol 63:320–38.
    • (2010) Int J Dairy Technol , vol.63 , pp. 320-338
    • Benkerroum, N.1
  • 14
    • 1842588044 scopus 로고    scopus 로고
    • Technology transfer of some Moroccan traditional dairy products (lben, jben and smen) to small industrial scale: a review
    • Benkerroum N, Tamime AY. 2004. Technology transfer of some Moroccan traditional dairy products (lben, jben and smen) to small industrial scale: a review. Food Microbiol 21:399–413.
    • (2004) Food Microbiol , vol.21 , pp. 399-413
    • Benkerroum, N.1    Tamime, A.Y.2
  • 15
    • 0023664476 scopus 로고
    • Purification and characterization of arginase from Neurospora crassa
    • Borkovich KA, Weiss RL. 1987. Purification and characterization of arginase from Neurospora crassa. J Biol Chem 262:7081–6.
    • (1987) J Biol Chem , vol.262 , pp. 7081-7086
    • Borkovich, K.A.1    Weiss, R.L.2
  • 16
    • 0033408543 scopus 로고    scopus 로고
    • Improved screening procedure for biogenic amine production by lactic acid bacteria
    • Bover-Cid S, Holzapfel WH. 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
  • 17
    • 0035092576 scopus 로고    scopus 로고
    • Effectiveness of a Lactobacillus sakei starter culture in the reduction of biogenic amine accumulation as a function of the raw material quality
    • Bover-Cid S, Izquierdo-Pulido M, Vidal-Carou MC. 2001. Effectiveness of a Lactobacillus sakei starter culture in the reduction of biogenic amine accumulation as a function of the raw material quality. J Food Prot 64:367–73.
    • (2001) J Food Prot , vol.64 , pp. 367-373
    • Bover-Cid, S.1    Izquierdo-Pulido, M.2    Vidal-Carou, M.C.3
  • 18
    • 0015919568 scopus 로고
    • Spermidine biosynthesis: purification and properties of propylamine transferase from Escherichia coli
    • Bowman WH, Tabor CW, Tabor H. 1973. Spermidine biosynthesis: purification and properties of propylamine transferase from Escherichia coli. J Biol Chem 248:2480–6.
    • (1973) J Biol Chem , vol.248 , pp. 2480-2486
    • Bowman, W.H.1    Tabor, C.W.2    Tabor, H.3
  • 19
    • 84939257328 scopus 로고    scopus 로고
    • Biogenic amine content in Chilean Gouda cheese: physico-chemical and microbiological factors that may influence this content
    • Brito C, Cid N, Muñoz O, Báez A, Horzella M. 2014. Biogenic amine content in Chilean Gouda cheese: physico-chemical and microbiological factors that may influence this content. Int J Dairy Technol 67:554–61.
    • (2014) Int J Dairy Technol , vol.67 , pp. 554-561
    • Brito, C.1    Cid, N.2    Muñoz, O.3    Báez, A.4    Horzella, M.5
  • 20
    • 0018166104 scopus 로고
    • Oxygen and nitrate in utilization by Bacillus licheniformis of the arginase and arginine deiminase routes of arginine catabolism and other factors affecting their syntheses
    • Broman K, Lauwers N, Stalon V, Wiame JM. 1978. Oxygen and nitrate in utilization by Bacillus licheniformis of the arginase and arginine deiminase routes of arginine catabolism and other factors affecting their syntheses. J Bacteriol 135:920–7.
    • (1978) J Bacteriol , vol.135 , pp. 920-927
    • Broman, K.1    Lauwers, N.2    Stalon, V.3    Wiame, J.M.4
  • 21
    • 33749535579 scopus 로고    scopus 로고
    • Genetic structure and transcriptional analysis of the arginine deiminase (ADI) cluster in Lactococcus lactis MG1363
    • Budin-Verneuil A, Maguin E, Auffray Y, Ehrlich DS, Pichereau V. 2006. Genetic structure and transcriptional analysis of the arginine deiminase (ADI) cluster in Lactococcus lactis MG1363. Can J Microbiol 52:617–22.
    • (2006) Can J Microbiol , vol.52 , pp. 617-622
    • Budin-Verneuil, A.1    Maguin, E.2    Auffray, Y.3    Ehrlich, D.S.4    Pichereau, V.5
  • 22
    • 84877586626 scopus 로고    scopus 로고
    • Monitoring of biogenic amines in cheeses manufactured at small-scale farms and in fermented dairy products in the Czech Republic
    • Bunkova L, Adamcova G, Hudcova K, Velichova H, Pachlova V, Lorencova E, Bunka F. 2013. Monitoring of biogenic amines in cheeses manufactured at small-scale farms and in fermented dairy products in the Czech Republic. Food Chem 141:548–51.
    • (2013) Food Chem , vol.141 , pp. 548-551
    • Bunkova, L.1    Adamcova, G.2    Hudcova, K.3    Velichova, H.4    Pachlova, V.5    Lorencova, E.6    Bunka, F.7
  • 24
    • 35448967978 scopus 로고    scopus 로고
    • Biogenic amine-forming microbial communities in cheese
    • Burdychova R, Komprda T. 2007. Biogenic amine-forming microbial communities in cheese. FEMS Microbiol Lett 276:149–55.
    • (2007) FEMS Microbiol Lett , vol.276 , pp. 149-155
    • Burdychova, R.1    Komprda, T.2
  • 25
    • 0028208257 scopus 로고
    • RocR, a novel regulatory protein controlling arginine utilization in Bacillus subtilis, belongs to the NtrC/NifA family of transcriptional activators
    • Calogero S, Gardan R, Glaser P, Schweizer J, Rapoport G, Debarbouille M. 1994. RocR, a novel regulatory protein controlling arginine utilization in Bacillus subtilis, belongs to the NtrC/NifA family of transcriptional activators. J Bacteriol 176:1234–41.
    • (1994) J Bacteriol , vol.176 , pp. 1234-1241
    • Calogero, S.1    Gardan, R.2    Glaser, P.3    Schweizer, J.4    Rapoport, G.5    Debarbouille, M.6
  • 26
    • 84880615294 scopus 로고    scopus 로고
    • Proteolysis and biogenic amine buildup in high-pressure treated ovine milk blue-veined cheese
    • Calzada J, del Olmo A, Picon A, Gaya P, Nuñez M. 2013. Proteolysis and biogenic amine buildup in high-pressure treated ovine milk blue-veined cheese. J Dairy Sci 96:4816–29.
    • (2013) J Dairy Sci , vol.96 , pp. 4816-4829
    • Calzada, J.1    del Olmo, A.2    Picon, A.3    Gaya, P.4    Nuñez, M.5
  • 27
    • 84873973481 scopus 로고    scopus 로고
    • Biogenic amines degradation by Lactobacillus plantarum: Toward a potential application in wine
    • Available from, Accessed 2016 April 8
    • Capozzi V, Russo P, Ladero V, Fernandez M, Fiocco D, Alvarez MA, Spano G. 2012. Biogenic amines degradation by Lactobacillus plantarum: Toward a potential application in wine. Front Microbiol 3:122. doi: 10.3389/fmicb.2012.00122. Available from:http://www.ncbi.nlm.nih.gov/pubmed/22485114. Accessed 2016 April 8.
    • (2012) Front Microbiol , vol.3 , pp. 122
    • Capozzi, V.1    Russo, P.2    Ladero, V.3    Fernandez, M.4    Fiocco, D.5    Alvarez, M.A.6    Spano, G.7
  • 29
    • 67649646788 scopus 로고    scopus 로고
    • Determination of histamine and biogenic amines in fish cubes (Tetrapturus angustirostris) implicated in a food-borne poisoning
    • Chen H-C, Huang Y-R, Hsu H-H, Lin C-S, Chen W-C, Lin C-M, Tsai Y-H. 2010. Determination of histamine and biogenic amines in fish cubes (Tetrapturus angustirostris) implicated in a food-borne poisoning. Food Control 21:13–8.
    • (2010) Food Control , vol.21 , pp. 13-18
    • Chen, H.-C.1    Huang, Y.-R.2    Hsu, H.-H.3    Lin, C.-S.4    Chen, W.-C.5    Lin, C.-M.6    Tsai, Y.-H.7
  • 30
    • 84884177779 scopus 로고    scopus 로고
    • Listeria monocytogenes aguA1, but not aguA2, encodes a functional agmatine deiminase: biochemical characterization of its catalytic properties and roles in acid tolerance
    • Cheng C, Chen J, Fang C, Xia Y, Shan Y, Liu Y, Fang W. 2013. Listeria monocytogenes aguA1, but not aguA2, encodes a functional agmatine deiminase: biochemical characterization of its catalytic properties and roles in acid tolerance. J Biol Chem 288:26606–15.
    • (2013) J Biol Chem , vol.288 , pp. 26606-26615
    • Cheng, C.1    Chen, J.2    Fang, C.3    Xia, Y.4    Shan, Y.5    Liu, Y.6    Fang, W.7
  • 31
    • 84974841747 scopus 로고
    • The polyamine cell composition as a chemotaxonomic marker in lactic acid bacteria identification
    • Chipeva V, Mehandjiyska L, Dumanova E. 1995. The polyamine cell composition as a chemotaxonomic marker in lactic acid bacteria identification. J Cult Collect 1:28–33.
    • (1995) J Cult Collect , vol.1 , pp. 28-33
    • Chipeva, V.1    Mehandjiyska, L.2    Dumanova, E.3
  • 34
    • 33745736293 scopus 로고    scopus 로고
    • Commission Regulation (EC) No 2073/2005 of 15 November 2005 on microbiological criteria for foodstuffs
    • Commission Regulation. 2005. Commission Regulation (EC) No 2073/2005 of 15 November 2005 on microbiological criteria for foodstuffs. OJEU Lett L 338:1–26.
    • (2005) OJEU Lett L , vol.338 , pp. 1-26
  • 35
    • 85018113448 scopus 로고    scopus 로고
    • Determination of biogenic amines by high-performance liquid chromatography (HPLC-DAD) in probiotic cow's and goat's fermented milks and acceptance
    • Costa MP, Balthazar CF, Rodrigues BL, Lazaro CA, Silva AC, Cruz AG, Conte Junior CA. 2015. Determination of biogenic amines by high-performance liquid chromatography (HPLC-DAD) in probiotic cow's and goat's fermented milks and acceptance. Food Sci Nutr 3:172–8.
    • (2015) Food Sci Nutr , vol.3 , pp. 172-178
    • Costa, M.P.1    Balthazar, C.F.2    Rodrigues, B.L.3    Lazaro, C.A.4    Silva, A.C.5    Cruz, A.G.6    Conte Junior, C.A.7
  • 36
    • 77955979275 scopus 로고    scopus 로고
    • Origin of the putrescine-producing ability of the coagulase-negative bacterium Staphylococcus epidermidis 2015B
    • Coton E, Mulder N, Coton M, Pochet S, Trip H, Lolkema JS. 2010a. Origin of the putrescine-producing ability of the coagulase-negative bacterium Staphylococcus epidermidis 2015B. Appl Environ Microbiol 76:5570–6.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 5570-5576
    • Coton, E.1    Mulder, N.2    Coton, M.3    Pochet, S.4    Trip, H.5    Lolkema, J.S.6
  • 37
  • 39
    • 0020314359 scopus 로고
    • Arginine metabolism in lactic streptococci
    • Crow VL, Thomas TD. 1982. Arginine metabolism in lactic streptococci. J Bacteriol 150:1024–32.
    • (1982) J Bacteriol , vol.150 , pp. 1024-1032
    • Crow, V.L.1    Thomas, T.D.2
  • 41
    • 33846810673 scopus 로고    scopus 로고
    • Extraction of bioactive amines from grated Parmesan cheese using acid, alkaline and organic solvents
    • Custódio FB, Tavares É, Glória MBA. 2007. Extraction of bioactive amines from grated Parmesan cheese using acid, alkaline and organic solvents. J Food Comp Anal 20:280–8.
    • (2007) J Food Comp Anal , vol.20 , pp. 280-288
    • Custódio, F.B.1    Tavares, É.2    Glória, M.B.A.3
  • 43
    • 0022531131 scopus 로고
    • Compartmental and regulatory mechanisms in the arginine pathways of Neurospora crassa and Saccharomyces cerevisiae
    • Davis RH. 1986. Compartmental and regulatory mechanisms in the arginine pathways of Neurospora crassa and Saccharomyces cerevisiae. Microbiol Rev 50:280–313.
    • (1986) Microbiol Rev , vol.50 , pp. 280-313
    • Davis, R.H.1
  • 44
    • 0014789268 scopus 로고
    • Arginaseless Neurospora: genetics, physiology, and polyamine synthesis
    • Davis RH, Lawless MB, Port LA. 1970. Arginaseless Neurospora: genetics, physiology, and polyamine synthesis. J Bacteriol 102:299–305.
    • (1970) J Bacteriol , vol.102 , pp. 299-305
    • Davis, R.H.1    Lawless, M.B.2    Port, L.A.3
  • 45
    • 34250618577 scopus 로고    scopus 로고
    • Gene organization of the ornithine decarboxylase-encoding region in Morganella morganii
    • de las Rivas B, Marcobal A, Munoz R. 2007. Gene organization of the ornithine decarboxylase-encoding region in Morganella morganii. J Appl Microbiol 102:1551–60.
    • (2007) J Appl Microbiol , vol.102 , pp. 1551-1560
    • de las Rivas, B.1    Marcobal, A.2    Munoz, R.3
  • 46
    • 49649111936 scopus 로고    scopus 로고
    • Biogenic amine production by Gram-positive bacteria isolated from Spanish dry-cured “chorizo” sausage treated with high pressure and kept in chilled storage
    • de Las Rivas B, Ruiz-Capillas C, Carrascosa AV, Curiel JA, Jimenez-Colmenero F, Munoz R. 2008. Biogenic amine production by Gram-positive bacteria isolated from Spanish dry-cured “chorizo” sausage treated with high pressure and kept in chilled storage. Meat Sci 80:272–7.
    • (2008) Meat Sci , vol.80 , pp. 272-277
    • de Las Rivas, B.1    Ruiz-Capillas, C.2    Carrascosa, A.V.3    Curiel, J.A.4    Jimenez-Colmenero, F.5    Munoz, R.6
  • 47
    • 84925439314 scopus 로고    scopus 로고
    • Lactose-mediated carbon catabolite repression of putrescine production in dairy Lactococcus lactis is strain dependent
    • del Rio B, Ladero V, Redruello B, Linares DM, Fernandez M, Martin MC, Alvarez MA. 2015a. Lactose-mediated carbon catabolite repression of putrescine production in dairy Lactococcus lactis is strain dependent. Food Microbiol 48:163–70.
    • (2015) Food Microbiol , vol.48 , pp. 163-170
    • del Rio, B.1    Ladero, V.2    Redruello, B.3    Linares, D.M.4    Fernandez, M.5    Martin, M.C.6    Alvarez, M.A.7
  • 48
    • 84925518181 scopus 로고    scopus 로고
    • Putrescine production via the agmatine deiminase pathway increases the growth of Lactococcus lactis and causes the alkalinization of the culture medium
    • del Rio B, Linares DM, Ladero V, Redruello B, Fernandez M, Martin MC, Alvarez MA. 2015b. Putrescine production via the agmatine deiminase pathway increases the growth of Lactococcus lactis and causes the alkalinization of the culture medium. Appl Microbiol Biotechnol 99:897–905.
    • (2015) Appl Microbiol Biotechnol , vol.99 , pp. 897-905
    • del Rio, B.1    Linares, D.M.2    Ladero, V.3    Redruello, B.4    Fernandez, M.5    Martin, M.C.6    Alvarez, M.A.7
  • 49
    • 0242584380 scopus 로고    scopus 로고
    • Molecular characterization of Oenococcus oeni genes encoding proteins involved in arginine transport
    • Divol B, Tonon T, Morichon S, Gindreau E, Lonvaud-Funel A. 2003. Molecular characterization of Oenococcus oeni genes encoding proteins involved in arginine transport. J Appl Microbiol 94:738–46.
    • (2003) J Appl Microbiol , vol.94 , pp. 738-746
    • Divol, B.1    Tonon, T.2    Morichon, S.3    Gindreau, E.4    Lonvaud-Funel, A.5
  • 50
    • 0023793137 scopus 로고
    • Transport of diamines by Enterococcus faecalis is mediated by an agmatine-putrescine antiporter
    • Driessen AJ, Smid EJ, Konings WN. 1988. Transport of diamines by Enterococcus faecalis is mediated by an agmatine-putrescine antiporter. J Bacteriol 170:4522–7.
    • (1988) J Bacteriol , vol.170 , pp. 4522-4527
    • Driessen, A.J.1    Smid, E.J.2    Konings, W.N.3
  • 51
    • 0036816961 scopus 로고    scopus 로고
    • Biogenic amine content of some Turkish cheeses
    • Durlu-Ozkaya F. 2002. Biogenic amine content of some Turkish cheeses. J Food Process Preserv 26:259–65.
    • (2002) J Food Process Preserv , vol.26 , pp. 259-265
    • Durlu-Ozkaya, F.1
  • 52
    • 84987325049 scopus 로고
    • Public health significance of amines in cheese
    • Edwards ST, Sandine WE. 1981. Public health significance of amines in cheese. J Dairy Sci 64:2431–8.
    • (1981) J Dairy Sci , vol.64 , pp. 2431-2438
    • Edwards, S.T.1    Sandine, W.E.2
  • 53
    • 85032113654 scopus 로고    scopus 로고
    • Scientific opinion on risk based control of biogenic amine formation in fermented foods
    • Available from, Accessed 2015 April 25
    • EFSA. 2011. Scientific opinion on risk based control of biogenic amine formation in fermented foods. EFSA J 9/2393:1–93. Available from: http://www.efsa.europa.eu/en/search/doc/2393.pdf. Accessed 2015 April 25.
    • (2011) EFSA J , vol.9-2393 , pp. 1-93
  • 56
    • 35348813614 scopus 로고    scopus 로고
    • HPLC quantification of biogenic amines in cheeses: correlation with PCR-detection of tyramine-producing microorganisms
    • Fernandez M, Linares DM, del Rio B, Ladero V, Alvarez MA. 2007. HPLC quantification of biogenic amines in cheeses: correlation with PCR-detection of tyramine-producing microorganisms. J Dairy Res 74:276–82.
    • (2007) J Dairy Res , vol.74 , pp. 276-282
    • Fernandez, M.1    Linares, D.M.2    del Rio, B.3    Ladero, V.4    Alvarez, M.A.5
  • 57
    • 33747084425 scopus 로고    scopus 로고
    • Amino acid catabolic pathways of lactic acid bacteria
    • Fernández M, Zúñiga M. 2006. Amino acid catabolic pathways of lactic acid bacteria. Cr Rev Microbiol 32:155–83.
    • (2006) Cr Rev Microbiol , vol.32 , pp. 155-183
    • Fernández, M.1    Zúñiga, M.2
  • 58
    • 0033761929 scopus 로고    scopus 로고
    • Formation of biogenic amines in raw milk Hispanico cheese manufactured with proteinases and different levels of starter culture
    • Fernandez-Garcia E, Tomillo J, Nunez M. 2000. Formation of biogenic amines in raw milk Hispanico cheese manufactured with proteinases and different levels of starter culture. J Food Prot 63:1551–5.
    • (2000) J Food Prot , vol.63 , pp. 1551-1555
    • Fernandez-Garcia, E.1    Tomillo, J.2    Nunez, M.3
  • 59
    • 84974835004 scopus 로고    scopus 로고
    • Fish and fishery products hazards and controls guidance
    • 4th ed., Washington, DC, FDA
    • Food and Drug Administration. 2011. Fish and fishery products hazards and controls guidance. 4th ed. Washington, DC: FDA, Center for Food Safety and Applied Nutrition.
    • (2011) Center for Food Safety and Applied Nutrition
  • 62
    • 84875771304 scopus 로고    scopus 로고
    • Focused review: Agmatine in fermented foods
    • Available from, Accessed 2014 April 7
    • Galgano F, Caruso M, Condelli N, Favati F. 2012. Focused review: Agmatine in fermented foods. Front Microbiol 3:199. doi: 10.3389/fmicb.2012.00199. Available from:http://journal.frontiersin.org/article/10.3389/fmicb.2012.00199/pdf. Accessed 2014 April 7.
    • (2012) Front Microbiol , vol.3 , pp. 199
    • Galgano, F.1    Caruso, M.2    Condelli, N.3    Favati, F.4
  • 64
    • 0030967333 scopus 로고    scopus 로고
    • Role of the transcriptional activator RocR in the arginine-degradation pathway of Bacillus subtilis
    • Gardan R, Rapoport G, Debarbouille M. 1997. Role of the transcriptional activator RocR in the arginine-degradation pathway of Bacillus subtilis. Mol Microbiol 24:825–37.
    • (1997) Mol Microbiol , vol.24 , pp. 825-837
    • Gardan, R.1    Rapoport, G.2    Debarbouille, M.3
  • 65
    • 4944242891 scopus 로고    scopus 로고
    • Polyamines and cancer: old molecules, new understanding
    • Gerner EW, Meyskens FL, Jr. 2004. Polyamines and cancer: old molecules, new understanding. Nat Rev Cancer 4:781–92.
    • (2004) Nat Rev Cancer , vol.4 , pp. 781-792
    • Gerner, E.W.1    Meyskens, F.L.2
  • 66
    • 84901447519 scopus 로고    scopus 로고
    • Milk availability: current production and demand and medium-term outlook
    • In, Muehlhoff E, Bennett A, McMahon D, editors., Rome, Italy
    • Gerosa S, Skoet J. 2013. Milk availability: current production and demand and medium-term outlook. In: Muehlhoff E, Bennett A, McMahon D, editors. Milk and dairy products in human nutrition. Rome, Italy: Food and Agricultural Organisation of the United nations (FAO). p 11–40.
    • (2013) Milk and dairy products in human nutrition, Milk and dairy products in human nutrition , pp. 11-40
    • Gerosa, S.1    Skoet, J.2
  • 67
    • 84890892296 scopus 로고    scopus 로고
    • Review of potential sources and control of thermoduric bacteria in bulk-tank milk
    • Gleeson D, O'Connell A, Jordan K. 2013. Review of potential sources and control of thermoduric bacteria in bulk-tank milk. Irish J Agr Food Res 52:217–27.
    • (2013) Irish J Agr Food Res , vol.52 , pp. 217-227
    • Gleeson, D.1    O'Connell, A.2    Jordan, K.3
  • 68
    • 78751629889 scopus 로고    scopus 로고
    • Bioactive amines changes in raw and sterilised milk inoculated with Pseudomonas fluorescens stored at different temperatures
    • Gloria MBA, Saraiva PR, Rigueira JCS, Brandão SCC. 2011. Bioactive amines changes in raw and sterilised milk inoculated with Pseudomonas fluorescens stored at different temperatures. Int J Dairy Technol 64:45–51.
    • (2011) Int J Dairy Technol , vol.64 , pp. 45-51
    • Gloria, M.B.A.1    Saraiva, P.R.2    Rigueira, J.C.S.3    Brandão, S.C.C.4
  • 70
    • 0025058098 scopus 로고
    • The purification and characterization of arginase from Saccharomyces cerevisiae
    • Green SM, Eisenstein E, McPhie P, Hensley P. 1990. The purification and characterization of arginase from Saccharomyces cerevisiae. J Biol Chem 265:1601–7.
    • (1990) J Biol Chem , vol.265 , pp. 1601-1607
    • Green, S.M.1    Eisenstein, E.2    McPhie, P.3    Hensley, P.4
  • 71
    • 1542286881 scopus 로고    scopus 로고
    • Analysis of an agmatine deiminase gene cluster in Streptococcus mutans UA159
    • Griswold AR, Chen YY, Burne RA. 2004. Analysis of an agmatine deiminase gene cluster in Streptococcus mutans UA159. J Bacteriol 186:1902–4.
    • (2004) J Bacteriol , vol.186 , pp. 1902-1904
    • Griswold, A.R.1    Chen, Y.Y.2    Burne, R.A.3
  • 72
    • 31344480412 scopus 로고    scopus 로고
    • Regulation and physiologic significance of the agmatine deiminase system of Streptococcus mutans UA159
    • Griswold AR, Jameson-Lee M, Burne RA. 2006. Regulation and physiologic significance of the agmatine deiminase system of Streptococcus mutans UA159. J Bacteriol 188:834–41.
    • (2006) J Bacteriol , vol.188 , pp. 834-841
    • Griswold, A.R.1    Jameson-Lee, M.2    Burne, R.A.3
  • 73
    • 0024651720 scopus 로고
    • Distribution of spermine in bacilli and lactic acid bacteria
    • Hamana K, Akiba T, Uchino F, Matsuzaki S. 1989. Distribution of spermine in bacilli and lactic acid bacteria. Can J Microbiol 35:450–5.
    • (1989) Can J Microbiol , vol.35 , pp. 450-455
    • Hamana, K.1    Akiba, T.2    Uchino, F.3    Matsuzaki, S.4
  • 74
    • 83355174050 scopus 로고    scopus 로고
    • Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota
    • Hanfrey CC, Pearson BM, Hazeldine S, Lee J, Gaskin DJ, Woster PM, Michael AJ. 2011. Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota. J Biol Chem 286:43301–12.
    • (2011) J Biol Chem , vol.286 , pp. 43301-43312
    • Hanfrey, C.C.1    Pearson, B.M.2    Hazeldine, S.3    Lee, J.4    Gaskin, D.J.5    Woster, P.M.6    Michael, A.J.7
  • 79
    • 14644417138 scopus 로고    scopus 로고
    • Polyamine analysis for chemotaxonomy of thermophilic eubacteria: polyamine distribution profiles within the orders Aquificales, Thermotogales, Thermodesulfobacteriales, Thermales, Thermoanaerobacteriales, Clostridiales, and Bacillales
    • Hosoya R, Hamana K, Niitsu M, Itoh T. 2004. Polyamine analysis for chemotaxonomy of thermophilic eubacteria: polyamine distribution profiles within the orders Aquificales, Thermotogales, Thermodesulfobacteriales, Thermales, Thermoanaerobacteriales, Clostridiales, and Bacillales. J Gen Appl Microbiol 50:271–87.
    • (2004) J Gen Appl Microbiol , vol.50 , pp. 271-287
    • Hosoya, R.1    Hamana, K.2    Niitsu, M.3    Itoh, T.4
  • 80
    • 34147138305 scopus 로고    scopus 로고
    • Changes in biogenic amines in fermented silver carp sausages inoculated with mixed starter cultures
    • Hu Y, Xia W, Liu X. 2007. Changes in biogenic amines in fermented silver carp sausages inoculated with mixed starter cultures. Food Chem 104:188–95.
    • (2007) Food Chem , vol.104 , pp. 188-195
    • Hu, Y.1    Xia, W.2    Liu, X.3
  • 81
    • 85008469093 scopus 로고    scopus 로고
    • Complete genome sequence of Pseudomonas aeruginosa strain 8380, isolated from the human gut
    • Available from, Accessed 2016 April 7
    • Ichise YK, Kosuge T, Uwate M, Nakae T, Maseda H. 2015. Complete genome sequence of Pseudomonas aeruginosa strain 8380, isolated from the human gut. Genome Announc 3:e00520–15. doi: 10.1128/genomeA.00520-15. Available from:http://www.ncbi.nlm.nih.gov/pubmed/25999558. Accessed 2016 April 7.
    • (2015) Genome Announc , vol.3 , pp. e00515-e00520
    • Ichise, Y.K.1    Kosuge, T.2    Uwate, M.3    Nakae, T.4    Maseda, H.5
  • 82
    • 70549083899 scopus 로고    scopus 로고
    • Modulation of cellular function by polyamines
    • Igarashi K, Kashiwagi K. 2010. Modulation of cellular function by polyamines. Int J Biochem Cell Biol 42:39–51.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 39-51
    • Igarashi, K.1    Kashiwagi, K.2
  • 85
    • 84893867864 scopus 로고    scopus 로고
    • Statistical screening of media components for the production of arginine deiminase by Weissella confusa GR7
    • Kaur B, Kaur R. 2012. Statistical screening of media components for the production of arginine deiminase by Weissella confusa GR7. Int J Food Ferm Technol 2:71–9.
    • (2012) Int J Food Ferm Technol , vol.2 , pp. 71-79
    • Kaur, B.1    Kaur, R.2
  • 86
    • 84938974452 scopus 로고    scopus 로고
    • Isolation, identification and genetic organization of the ADI operon in Enterococcus faecium GR7
    • Kaur B, Kaur R. 2015. Isolation, identification and genetic organization of the ADI operon in Enterococcus faecium GR7. Ann Microbiol 65:1427–37.
    • (2015) Ann Microbiol , vol.65 , pp. 1427-1437
    • Kaur, B.1    Kaur, R.2
  • 88
    • 58649090844 scopus 로고    scopus 로고
    • Contents of some biologically active amines in a Czech blue-vein cheese
    • Komprda T, Dohnal V, Závodníková R. 2008b. Contents of some biologically active amines in a Czech blue-vein cheese. Czech J Food Sc 26:428–40.
    • (2008) Czech J Food Sc , vol.26 , pp. 428-440
    • Komprda, T.1    Dohnal, V.2    Závodníková, R.3
  • 89
    • 0023728819 scopus 로고
    • Tyramine pressor effect in man: studies with moclobemide, a novel, reversible monoamine oxidase inhibitor
    • Korn A, Da Prada M, Raffesberg W, Allen S, Gasic S. 1988a. Tyramine pressor effect in man: studies with moclobemide, a novel, reversible monoamine oxidase inhibitor. J Neural Transm Suppl 26:57–71.
    • (1988) J Neural Transm Suppl , vol.26 , pp. 57-71
    • Korn, A.1    Da Prada, M.2    Raffesberg, W.3    Allen, S.4    Gasic, S.5
  • 90
    • 0023882148 scopus 로고
    • Effect of moclobemide, a new reversible monoamine oxidase inhibitor, on absorption, and pressor effect of tyramine
    • Korn A, Da Prada M, Raffesberg W, Gasic S, Eichler HG. 1988b. Effect of moclobemide, a new reversible monoamine oxidase inhibitor, on absorption, and pressor effect of tyramine. J Cardiovasc Pharmacol 11:17–23.
    • (1988) J Cardiovasc Pharmacol , vol.11 , pp. 17-23
    • Korn, A.1    Da Prada, M.2    Raffesberg, W.3    Gasic, S.4    Eichler, H.G.5
  • 92
    • 47249122499 scopus 로고    scopus 로고
    • Polyamines: essential factors for growth and survival
    • Kusano T, Berberich T, Tateda C, Takahashi Y. 2008. Polyamines: essential factors for growth and survival. Planta 228:367–81.
    • (2008) Planta , vol.228 , pp. 367-381
    • Kusano, T.1    Berberich, T.2    Tateda, C.3    Takahashi, Y.4
  • 93
    • 79551494125 scopus 로고    scopus 로고
    • Identification of a tyrosine decarboxylase gene (tdcA) in Streptococcus thermophilus 1TT45 and analysis of its expression and tyramine production in milk
    • La Gioia F, Rizzotti L, Rossi F, Gardini F, Tabanelli G, Torriani S. 2011. Identification of a tyrosine decarboxylase gene (tdcA) in Streptococcus thermophilus 1TT45 and analysis of its expression and tyramine production in milk. Appl Environ Microbiol 77:1140–4.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 1140-1144
    • La Gioia, F.1    Rizzotti, L.2    Rossi, F.3    Gardini, F.4    Tabanelli, G.5    Torriani, S.6
  • 95
    • 84860534307 scopus 로고    scopus 로고
    • Multiplex qPCR for the detection and quantification of putrescine-producing lactic acid bacteria in dairy products
    • Ladero V, Cañedo E, Pérez M, Martín MC, Fernández M, Alvarez MA. 2012a. Multiplex qPCR for the detection and quantification of putrescine-producing lactic acid bacteria in dairy products. Food Control 27:307–13.
    • (2012) Food Control , vol.27 , pp. 307-313
    • Ladero, V.1    Cañedo, E.2    Pérez, M.3    Martín, M.C.4    Fernández, M.5    Alvarez, M.A.6
  • 97
    • 80052815937 scopus 로고    scopus 로고
    • Sequencing and transcriptional analysis of the biosynthesis gene cluster of putrescine-producing Lactococcus lactis
    • Ladero V, Rattray FP, Mayo B, Martin MC, Fernandez M, Alvarez MA. 2011a. Sequencing and transcriptional analysis of the biosynthesis gene cluster of putrescine-producing Lactococcus lactis. Appl Environ Microbiol 77:6409–18.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 6409-6418
    • Ladero, V.1    Rattray, F.P.2    Mayo, B.3    Martin, M.C.4    Fernandez, M.5    Alvarez, M.A.6
  • 98
    • 79951996261 scopus 로고    scopus 로고
    • Survival of biogenic amine-producing dairy LAB strains at pasteurisation conditions
    • Ladero V, Sánchez-Llana E, Fernández M, Alvarez MA. 2011b. Survival of biogenic amine-producing dairy LAB strains at pasteurisation conditions. Int J Food Sci Technol 46:516–21.
    • (2011) Int J Food Sci Technol , vol.46 , pp. 516-521
    • Ladero, V.1    Sánchez-Llana, E.2    Fernández, M.3    Alvarez, M.A.4
  • 99
    • 79953185435 scopus 로고    scopus 로고
    • The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
    • Landete JM, Arena ME, Pardo I, Manca de Nadra MC, Ferrer S. 2010. The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase. Int Microbiol 13:169–77.
    • (2010) Int Microbiol , vol.13 , pp. 169-177
    • Landete, J.M.1    Arena, M.E.2    Pardo, I.3    Manca de Nadra, M.C.4    Ferrer, S.5
  • 100
    • 65649147535 scopus 로고    scopus 로고
    • An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae
    • Lee J, Sperandio V, Frantz DE, Longgood J, Camilli A, Phillips MA, Michael AJ. 2009. An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae. J Biol Chem 284:9899–907.
    • (2009) J Biol Chem , vol.284 , pp. 9899-9907
    • Lee, J.1    Sperandio, V.2    Frantz, D.E.3    Longgood, J.4    Camilli, A.5    Phillips, M.A.6    Michael, A.J.7
  • 101
    • 0032219904 scopus 로고    scopus 로고
    • Tyramine degradation by micrococci during ripening of fermented sausage
    • Leuschner RG, Hammes WP. 1998a. Tyramine degradation by micrococci during ripening of fermented sausage. Meat Sci 49:289–96.
    • (1998) Meat Sci , vol.49 , pp. 289-296
    • Leuschner, R.G.1    Hammes, W.P.2
  • 102
    • 0032126881 scopus 로고    scopus 로고
    • Degradation of histamine and tyramine by Brevibacterium linens during surface ripening of Munster cheese
    • Leuschner RGK, Hammes WP. 1998b. Degradation of histamine and tyramine by Brevibacterium linens during surface ripening of Munster cheese. J Food Prot 61:874–8.
    • (1998) J Food Prot , vol.61 , pp. 874-878
    • Leuschner, R.G.K.1    Hammes, W.P.2
  • 104
    • 84878132027 scopus 로고    scopus 로고
    • The putrescine biosynthesis pathway in Lactococcus lactis is transcriptionally regulated by carbon catabolic repression, mediated by CcpA
    • Linares DM, del Rio B, Ladero V, Redruello B, Martin MC, Fernandez M, Alvarez MA. 2013. The putrescine biosynthesis pathway in Lactococcus lactis is transcriptionally regulated by carbon catabolic repression, mediated by CcpA. Int J Food Microbiol 165:43–50.
    • (2013) Int J Food Microbiol , vol.165 , pp. 43-50
    • Linares, D.M.1    del Rio, B.2    Ladero, V.3    Redruello, B.4    Martin, M.C.5    Fernandez, M.6    Alvarez, M.A.7
  • 105
    • 84943642103 scopus 로고    scopus 로고
    • AguR, a transmembrane transcription activator of the putrescine biosynthesis operon in Lactococcus lactis, acts in response to the agmatine concentration
    • Linares DM, del Rio B, Redruello B, Ladero V, Martin MC, de Jong A, Alvarez MA. 2015. AguR, a transmembrane transcription activator of the putrescine biosynthesis operon in Lactococcus lactis, acts in response to the agmatine concentration. Appl Environ Microbiol 81:6145–57.
    • (2015) Appl Environ Microbiol , vol.81 , pp. 6145-6157
    • Linares, D.M.1    del Rio, B.2    Redruello, B.3    Ladero, V.4    Martin, M.C.5    de Jong, A.6    Alvarez, M.A.7
  • 107
    • 0028819210 scopus 로고
    • Occurrence of arginine deiminase pathway enzymes in arginine catabolism by wine lactic acid bacteria
    • Liu S, Pritchard GG, Hardman MJ, Pilone GJ. 1995. Occurrence of arginine deiminase pathway enzymes in arginine catabolism by wine lactic acid bacteria. Appl Environ Microbiol 61:310–6.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 310-316
    • Liu, S.1    Pritchard, G.G.2    Hardman, M.J.3    Pilone, G.J.4
  • 108
    • 65549128078 scopus 로고    scopus 로고
    • AguR is required for induction of the Streptococcus mutans agmatine deiminase system by low pH and agmatine
    • Liu Y, Zeng L, Burne RA. 2009. AguR is required for induction of the Streptococcus mutans agmatine deiminase system by low pH and agmatine. Appl Environ Microbiol 75:2629–37.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 2629-2637
    • Liu, Y.1    Zeng, L.2    Burne, R.A.3
  • 110
    • 33644771430 scopus 로고    scopus 로고
    • Pathways and regulation of bacterial arginine metabolism and perspectives for obtaining arginine overproducing strains
    • Lu CD. 2006. Pathways and regulation of bacterial arginine metabolism and perspectives for obtaining arginine overproducing strains. Appl Microbiol Biotechnol 70:261–72.
    • (2006) Appl Microbiol Biotechnol , vol.70 , pp. 261-272
    • Lu, C.D.1
  • 111
    • 84912048733 scopus 로고    scopus 로고
    • The effects of starter cultures and plant extracts on the biogenic amine accumulation in traditional Chinese smoked horsemeat sausages
    • Lu S, Ji H, Wang Q, Li B, Li K, Xu C, Jiang C. 2015. The effects of starter cultures and plant extracts on the biogenic amine accumulation in traditional Chinese smoked horsemeat sausages. Food Control 50:869–75.
    • (2015) Food Control , vol.50 , pp. 869-875
    • Lu, S.1    Ji, H.2    Wang, Q.3    Li, B.4    Li, K.5    Xu, C.6    Jiang, C.7
  • 112
    • 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 PM, Blancato VS, Claisse O, Magni C, Lolkema JS, 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 153:2221–30.
    • (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
  • 113
    • 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 67:878–83.
    • (2004) J Food Prot , vol.67 , pp. 878-883
    • Lyte, M.1
  • 114
    • 0014346703 scopus 로고
    • Activities of arginine dihydrolase and phosphatase in Streptococcus faecalis and Streptococcus faecium
    • Mackey JK, Jr., Beck RW. 1968. Activities of arginine dihydrolase and phosphatase in Streptococcus faecalis and Streptococcus faecium. Appl Microbiol 16:1543–7.
    • (1968) Appl Microbiol , vol.16 , pp. 1543-1547
    • Mackey, J.K.1    Beck, R.W.2
  • 115
    • 0032440064 scopus 로고    scopus 로고
    • The arcABDC gene cluster, encoding the arginine deiminase pathway of Bacillus licheniformis, and its activation by the arginine repressor argR
    • Maghnouj A, de Sousa Cabral TF, Stalon V, Vander Wauven C. 1998. The arcABDC gene cluster, encoding the arginine deiminase pathway of Bacillus licheniformis, and its activation by the arginine repressor argR. J Bacteriol 180:6468–75.
    • (1998) J Bacteriol , vol.180 , pp. 6468-6475
    • Maghnouj, A.1    de Sousa Cabral, T.F.2    Stalon, V.3    Vander Wauven, C.4
  • 116
    • 63449116397 scopus 로고    scopus 로고
    • Inhibition of biogenic amine formation in a salted and fermented anchovy by Staphylococcus xylosus as a protective culture
    • Mah J-H, Hwang H-J. 2009. Inhibition of biogenic amine formation in a salted and fermented anchovy by Staphylococcus xylosus as a protective culture. Food Control 20:796–801.
    • (2009) Food Control , vol.20 , pp. 796-801
    • Mah, J.-H.1    Hwang, H.-J.2
  • 117
    • 84872450065 scopus 로고    scopus 로고
    • Identification of the Enterobacteriaceae in Montasio cheese and assessment of their amino acid decarboxylase activity
    • Maifreni M, Frigo F, Bartolomeoli I, Innocente N, Biasutti M, Marino M. 2013. Identification of the Enterobacteriaceae in Montasio cheese and assessment of their amino acid decarboxylase activity. J Dairy Res 80:122–7.
    • (2013) J Dairy Res , vol.80 , pp. 122-127
    • Maifreni, M.1    Frigo, F.2    Bartolomeoli, I.3    Innocente, N.4    Biasutti, M.5    Marino, M.6
  • 119
    • 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 MV, Munoz R. 2006a. Evidence for horizontal gene transfer as origin of putrescine production in Oenococcus oeni RM83. Appl Environ Microbiol 72:7954–8.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 7954-7958
    • Marcobal, A.1    de las Rivas, B.2    Moreno-Arribas, M.V.3    Munoz, R.4
  • 120
    • 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, Munoz R. 2006b. First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58. FEMS Microbiol Lett 258:144–9.
    • (2006) FEMS Microbiol Lett , vol.258 , pp. 144-149
    • Marcobal, A.1    de las Rivas, B.2    Munoz, R.3
  • 121
    • 0000654275 scopus 로고
    • Water activity in cheese in relation to composition, stability and safety
    • In, Fox PF, editor., London, Chapman & Hall
    • Marcos A. 1993. Water activity in cheese in relation to composition, stability and safety. In: Fox PF, editor. Cheese: chemistry, physics and microbiology. London: Chapman & Hall, p 439–69.
    • (1993) Cheese: chemistry, physics and microbiology , pp. 439-469
    • Marcos, A.1
  • 122
  • 125
    • 0022531002 scopus 로고
    • Dietary tyramine and other pressor amines in MAOI regimens: a review
    • McCabe BJ. 1986. Dietary tyramine and other pressor amines in MAOI regimens: a review. J Am Diet Assoc 86:1059–64.
    • (1986) J Am Diet Assoc , vol.86 , pp. 1059-1064
    • McCabe, B.J.1
  • 126
    • 33646508750 scopus 로고    scopus 로고
    • Tyramine in foods and monoamine oxidase inhibitor drugs: a crossroad where medicine, nutrition, pharmacy, and food industry converge
    • McCabe-Sellers BJ, Staggs CG, Bogle ML. 2006. Tyramine in foods and monoamine oxidase inhibitor drugs: a crossroad where medicine, nutrition, pharmacy, and food industry converge. J Food Comp Anal 19:S58–65.
    • (2006) J Food Comp Anal , vol.19 , pp. S58-65
    • McCabe-Sellers, B.J.1    Staggs, C.G.2    Bogle, M.L.3
  • 128
    • 10044227058 scopus 로고    scopus 로고
    • Quantitative analysis of biogenic amines in raw and processed foods of animal origin on Korean domestic market
    • Min JS, Lee SO, Jang A, Lee M, Kim Y. 2004. Quantitative analysis of biogenic amines in raw and processed foods of animal origin on Korean domestic market. Asian-Aust J Anim Sci 17:1764–8.
    • (2004) Asian-Aust J Anim Sci , vol.17 , pp. 1764-1768
    • Min, J.S.1    Lee, S.O.2    Jang, A.3    Lee, M.4    Kim, Y.5
  • 129
    • 15344340623 scopus 로고    scopus 로고
    • Polyamines: metabolism and implications in human diseases
    • Moinard C, Cynober L, de Bandt JP. 2005. Polyamines: metabolism and implications in human diseases. Clin Nutr 24:184–97.
    • (2005) Clin Nutr , vol.24 , pp. 184-197
    • Moinard, C.1    Cynober, L.2    de Bandt, J.P.3
  • 130
    • 0027191082 scopus 로고
    • Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri
    • Molenaar D, Bosscher JS, ten Brink B, Driessen AJ, Konings WN. 1993. Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri. J Bacteriol 175:2864–70.
    • (1993) J Bacteriol , vol.175 , pp. 2864-2870
    • Molenaar, D.1    Bosscher, J.S.2    ten Brink, B.3    Driessen, A.J.4    Konings, W.N.5
  • 131
    • 0035808975 scopus 로고    scopus 로고
    • Purification and characterization of tyrosine decarboxylase of Lactobacillus brevis IOEB 9809 isolated from wine
    • Moreno-Arribas V, Lonvaud-Funel A. 2001. Purification and characterization of tyrosine decarboxylase of Lactobacillus brevis IOEB 9809 isolated from wine. FEMS Microbiol Lett 195:103–7.
    • (2001) FEMS Microbiol Lett , vol.195 , pp. 103-107
    • Moreno-Arribas, V.1    Lonvaud-Funel, A.2
  • 132
    • 84974787764 scopus 로고    scopus 로고
    • Control of thermoduric bacteria in raw milk supplies
    • Available from, Accessed 2015 Nov 21
    • Murphy P. 2015. Control of thermoduric bacteria in raw milk supplies. Glanbia. Available from: https://agrilink.ie/MilkNews2007/4241 Thermoduric Bacteria.pdf. Accessed 2015 Nov 21.
    • (2015) Glanbia
    • Murphy, P.1
  • 133
    • 77957153983 scopus 로고    scopus 로고
    • Control of biogenic amines in food—existing and emerging approaches
    • Naila A, Flint S, Fletcher G, Bremer P, Meerdink G. 2010. Control of biogenic amines in food—existing and emerging approaches. J Food Sci 75:R139–R50.
    • (2010) J Food Sci , vol.75 , pp. R139-R150
    • Naila, A.1    Flint, S.2    Fletcher, G.3    Bremer, P.4    Meerdink, G.5
  • 134
    • 84930178274 scopus 로고    scopus 로고
    • Histamine degradation by diamine oxidase, Lactobacillus and Vergibacillus halodonitrificans Nai18
    • Naila A, Flint S, Fletcher GC, Bremer PJ, Meerdink G. 2012. Histamine degradation by diamine oxidase, Lactobacillus and Vergibacillus halodonitrificans Nai18. J Food Process Technol 3:1–4.
    • (2012) J Food Process Technol , vol.3 , pp. 1-4
    • Naila, A.1    Flint, S.2    Fletcher, G.C.3    Bremer, P.J.4    Meerdink, G.5
  • 135
    • 0034750704 scopus 로고    scopus 로고
    • Molecular characterization and regulation of the aguBA operon, responsible for agmatine utilization in Pseudomonas aeruginosa PAO1
    • Nakada Y, Jiang Y, Nishijyo T, Itoh Y, Lu CD. 2001. Molecular characterization and regulation of the aguBA operon, responsible for agmatine utilization in Pseudomonas aeruginosa PAO1. J Bacteriol 183:6517–24.
    • (2001) J Bacteriol , vol.183 , pp. 6517-6524
    • Nakada, Y.1    Jiang, Y.2    Nishijyo, T.3    Itoh, Y.4    Lu, C.D.5
  • 137
    • 84907165253 scopus 로고    scopus 로고
    • Modulation of resistance artery tone by the trace amine beta-phenylethylamine: dual indirect sympathomimetic and alpha1-adrenoceptor blocking actions
    • Narang D, Kerr PM, Lunn SE, Beaudry R, Sigurdson J, Lalies MD, Plane F. 2014. Modulation of resistance artery tone by the trace amine beta-phenylethylamine: dual indirect sympathomimetic and alpha1-adrenoceptor blocking actions. J Pharmacol Exp Ther 351:164–71.
    • (2014) J Pharmacol Exp Ther , vol.351 , pp. 164-171
    • Narang, D.1    Kerr, P.M.2    Lunn, S.E.3    Beaudry, R.4    Sigurdson, J.5    Lalies, M.D.6    Plane, F.7
  • 139
    • 67349173525 scopus 로고    scopus 로고
    • Technological characterization of Lactobacillus isolates from traditional Manchego cheese for potential use as adjunct starter cultures
    • Nieto-Arribas P, Poveda JM, Seseña S, Palop L, Cabezas L. 2009. Technological characterization of Lactobacillus isolates from traditional Manchego cheese for potential use as adjunct starter cultures. Food Control 20:1092–8.
    • (2009) Food Control , vol.20 , pp. 1092-1098
    • Nieto-Arribas, P.1    Poveda, J.M.2    Seseña, S.3    Palop, L.4    Cabezas, L.5
  • 140
    • 33646505580 scopus 로고
    • Fermented foods and food safety
    • Nout MJR. 1994. Fermented foods and food safety. Food Res Int 27:291–8.
    • (1994) Food Res Int , vol.27 , pp. 291-298
    • Nout, M.J.R.1
  • 146
    • 84998577522 scopus 로고    scopus 로고
    • The complete genome sequence of Pseudomonas putida NBRC 14164T confirms high intraspecies variation
    • Available from, Accessed 2016 April 7
    • Ohji S, Yamazoe A, Hosoyama A, Tsuchikane K, Ezaki T, Fujita N. 2014. The complete genome sequence of Pseudomonas putida NBRC 14164T confirms high intraspecies variation. Genome Announc 2:e00029–14. doi: 10.1128/genomeA.00029-14. Available from:http://www.ncbi.nlm.nih.gov/pubmed/24526630. Accessed 2016 April 7.
    • (2014) Genome Announc , vol.2 , pp. e00014-e00029
    • Ohji, S.1    Yamazoe, A.2    Hosoyama, A.3    Tsuchikane, K.4    Ezaki, T.5    Fujita, N.6
  • 147
    • 77952426746 scopus 로고    scopus 로고
    • Biogenic amine content of kefir: a fermented dairy product
    • Ozdestan O, Uren A. 2010. Biogenic amine content of kefir: a fermented dairy product. Eur Food Res Technol 231:101–7.
    • (2010) Eur Food Res Technol , vol.231 , pp. 101-107
    • Ozdestan, O.1    Uren, A.2
  • 148
    • 0018642112 scopus 로고
    • Effects of cadaverine on histamine transport and metabolism in isolated gut sections of the guinea-pig
    • Paik Jung HY, Bjeldanes LF. 1979. Effects of cadaverine on histamine transport and metabolism in isolated gut sections of the guinea-pig. Food Cosmet Toxicol 17:629–32.
    • (1979) Food Cosmet Toxicol , vol.17 , pp. 629-632
    • Paik Jung, H.Y.1    Bjeldanes, L.F.2
  • 149
    • 0023368759 scopus 로고
    • Biosynthesis of polyamines in ornithine decarboxylase, arginine decarboxylase, and agmatine ureohydrolase deletion mutants of Escherichia coli strain K-12
    • Panagiotidis CA, Blackburn S, Low KB, Canellakis ES. 1987. Biosynthesis of polyamines in ornithine decarboxylase, arginine decarboxylase, and agmatine ureohydrolase deletion mutants of Escherichia coli strain K-12. Proc Natl Acad Sci USA 84:4423–7.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4423-4427
    • Panagiotidis, C.A.1    Blackburn, S.2    Low, K.B.3    Canellakis, E.S.4
  • 150
    • 0029022445 scopus 로고
    • Pressor effect of oral tyramine during treatment with befloxatone, a new reversible monoamine oxidase—a inhibitor, in healthy subjects
    • Patat A, Berlin I, Durrieu G, Armand P, Fitoussi S, Molinier P, Caille P. 1995. Pressor effect of oral tyramine during treatment with befloxatone, a new reversible monoamine oxidase—a inhibitor, in healthy subjects. J Clin Pharmacol 35:633–43.
    • (1995) J Clin Pharmacol , vol.35 , pp. 633-643
    • Patat, A.1    Berlin, I.2    Durrieu, G.3    Armand, P.4    Fitoussi, S.5    Molinier, P.6    Caille, P.7
  • 151
    • 57149099622 scopus 로고    scopus 로고
    • Production of biogenic amines by some enterobacteriaceae strains isolated from dairy products
    • Pattono D, Grassi MA, Civera TI. 2008. Production of biogenic amines by some enterobacteriaceae strains isolated from dairy products. Ital J Food Sci 20:411–7.
    • (2008) Ital J Food Sci , vol.20 , pp. 411-417
    • Pattono, D.1    Grassi, M.A.2    Civera, T.I.3
  • 152
    • 0031427091 scopus 로고    scopus 로고
    • Dietary polyamines promote the growth of azoxymethane-induced aberrant crypt foci in rat colon
    • Paulsen JE, Reistad R, Eliassen KA, Sjaastad OV, Alexander J. 1997. Dietary polyamines promote the growth of azoxymethane-induced aberrant crypt foci in rat colon. Carcinogenesis 18:1871–5.
    • (1997) Carcinogenesis , vol.18 , pp. 1871-1875
    • Paulsen, J.E.1    Reistad, R.2    Eliassen, K.A.3    Sjaastad, O.V.4    Alexander, J.5
  • 154
    • 0029455991 scopus 로고
    • Ornithine decarboxylase as a target for chemoprevention
    • Pegg AE, Shantz LM, Coleman CS. 1995. Ornithine decarboxylase as a target for chemoprevention. J Cell Biochem Suppl 22:132–8.
    • (1995) J Cell Biochem Suppl , vol.22 , pp. 132-138
    • Pegg, A.E.1    Shantz, L.M.2    Coleman, C.S.3
  • 155
    • 72849144325 scopus 로고    scopus 로고
    • Weissella halotolerans W22 combines arginine deiminase and ornithine decarboxylation pathways and converts arginine to putrescine
    • Pereira CI, San Romao MV, Lolkema JS, Crespo MT. 2009. Weissella halotolerans W22 combines arginine deiminase and ornithine decarboxylation pathways and converts arginine to putrescine. J Appl Microbiol 107:1894–902.
    • (2009) J Appl Microbiol , vol.107 , pp. 1894-1902
    • Pereira, C.I.1    San Romao, M.V.2    Lolkema, J.S.3    Crespo, M.T.4
  • 158
    • 84885579666 scopus 로고    scopus 로고
    • Effect of irradiation and storage on biogenic amine contents in ripened Egyptian smoked cooked sausage
    • Rabie MA, Toliba AO. 2013. Effect of irradiation and storage on biogenic amine contents in ripened Egyptian smoked cooked sausage. J Food Sci Technol 50:1165–71.
    • (2013) J Food Sci Technol , vol.50 , pp. 1165-1171
    • Rabie, M.A.1    Toliba, A.O.2
  • 159
    • 84908590378 scopus 로고    scopus 로고
    • Food irradiation is safe: half a century of studies
    • Roberts PB. 2014. Food irradiation is safe: half a century of studies. Radiat Phys Chem 105:78–82.
    • (2014) Radiat Phys Chem , vol.105 , pp. 78-82
    • Roberts, P.B.1
  • 160
    • 84864330586 scopus 로고    scopus 로고
    • Dietary exposure assessment of putrescine and cadaverine and derivation of tolerable levels in selected foods consumed in Austria
    • Rauscher-Gabernig E, Gabernig R, Brueller W, Grossgut R, Bauer F, Paulsen P. 2012. Dietary exposure assessment of putrescine and cadaverine and derivation of tolerable levels in selected foods consumed in Austria. Eur Food Res Technol 235:209–20.
    • (2012) Eur Food Res Technol , vol.235 , pp. 209-220
    • Rauscher-Gabernig, E.1    Gabernig, R.2    Brueller, W.3    Grossgut, R.4    Bauer, F.5    Paulsen, P.6
  • 161
    • 55049118688 scopus 로고    scopus 로고
    • Assessment of alimentary histamine exposure of consumers in Austria and development of tolerable levels in typical foods
    • Rauscher-Gabernig E, Grossgut R, Bauer F, Paulsen P. 2009. Assessment of alimentary histamine exposure of consumers in Austria and development of tolerable levels in typical foods. Food Control 20:423–9.
    • (2009) Food Control , vol.20 , pp. 423-429
    • Rauscher-Gabernig, E.1    Grossgut, R.2    Bauer, F.3    Paulsen, P.4
  • 162
    • 0028949628 scopus 로고
    • Observations on the effect of raw milk quality on the keeping quality of pasteurized milk
    • Ravanis S, Lewis MJ. 1995. Observations on the effect of raw milk quality on the keeping quality of pasteurized milk. Lett Appl Microbiol 20:164–7.
    • (1995) Lett Appl Microbiol , vol.20 , pp. 164-167
    • Ravanis, S.1    Lewis, M.J.2
  • 163
    • 29144504167 scopus 로고    scopus 로고
    • Metabolic and transcriptomic adaptation of Lactococcus lactis subsp. lactis Biovar diacetylactis in response to autoacidification and temperature downshift in skim milk
    • Raynaud S, Perrin R, Cocaign-Bousquet M, Loubiere P. 2005. Metabolic and transcriptomic adaptation of Lactococcus lactis subsp. lactis Biovar diacetylactis in response to autoacidification and temperature downshift in skim milk. Appl Environ Microbiol 71:8016–23.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8016-8023
    • Raynaud, S.1    Perrin, R.2    Cocaign-Bousquet, M.3    Loubiere, P.4
  • 164
    • 84863773770 scopus 로고    scopus 로고
    • Expression of the arginine deiminase pathway genes in Lactobacillus sakei is strain dependent and is affected by the environmental pH
    • Rimaux T, Riviere A, Illeghems K, Weckx S, De Vuyst L, Leroy F. 2012. Expression of the arginine deiminase pathway genes in Lactobacillus sakei is strain dependent and is affected by the environmental pH. Appl Environ Microbiol 78:4874–83.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 4874-4883
    • Rimaux, T.1    Riviere, A.2    Illeghems, K.3    Weckx, S.4    De Vuyst, L.5    Leroy, F.6
  • 166
    • 84893489351 scopus 로고    scopus 로고
    • Putrescine production via the ornithine decarboxylation pathway improves the acid stress survival of Lactobacillus brevis and is part of a horizontally transferred acid resistance locus
    • Romano A, Ladero V, Alvarez MA, Lucas PM. 2014. Putrescine production via the ornithine decarboxylation pathway improves the acid stress survival of Lactobacillus brevis and is part of a horizontally transferred acid resistance locus. Int J Food Microbiol 175:14–9.
    • (2014) Int J Food Microbiol , vol.175 , pp. 14-19
    • Romano, A.1    Ladero, V.2    Alvarez, M.A.3    Lucas, P.M.4
  • 167
    • 84874733888 scopus 로고    scopus 로고
    • Three-component lysine/ornithine decarboxylation system in Lactobacillus saerimneri 30a
    • Romano A, Trip H, Lolkema JS, Lucas PM. 2013. Three-component lysine/ornithine decarboxylation system in Lactobacillus saerimneri 30a. J Bacteriol 195:1249–54.
    • (2013) J Bacteriol , vol.195 , pp. 1249-1254
    • Romano, A.1    Trip, H.2    Lolkema, J.S.3    Lucas, P.M.4
  • 168
    • 84857812510 scopus 로고    scopus 로고
    • Evidence of 2 functionally distinct ornithine decarboxylation systems in lactic acid bacteria
    • Romano A, Trip H, Lonvaud-Funel A, Lolkema JS, Lucas PM. 2012. Evidence of 2 functionally distinct ornithine decarboxylation systems in lactic acid bacteria. Appl Environ Microbiol 78:1953–61.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 1953-1961
    • Romano, A.1    Trip, H.2    Lonvaud-Funel, A.3    Lolkema, J.S.4    Lucas, P.M.5
  • 170
    • 1942487362 scopus 로고    scopus 로고
    • Free amino acids and biogenic amines in red and white muscle of tuna stored in controlled atmospheres
    • Ruiz-Capillas C, Moral A. 2004. Free amino acids and biogenic amines in red and white muscle of tuna stored in controlled atmospheres. Amino Acids 26:125–32.
    • (2004) Amino Acids , vol.26 , pp. 125-132
    • Ruiz-Capillas, C.1    Moral, A.2
  • 171
    • 58549111075 scopus 로고    scopus 로고
    • Molecular characterization of the arginine deiminase system in Listeria monocytogenes: regulation and role in acid tolerance
    • Ryan S, Begley M, Gahan CG, Hill C. 2009. Molecular characterization of the arginine deiminase system in Listeria monocytogenes: regulation and role in acid tolerance. Environ Microbiol 11:432–45.
    • (2009) Environ Microbiol , vol.11 , pp. 432-445
    • Ryan, S.1    Begley, M.2    Gahan, C.G.3    Hill, C.4
  • 172
    • 84871885496 scopus 로고    scopus 로고
    • Biogenic amines in Italian Pecorino cheese
    • Available from, Accessed 2016 April 8
    • Schirone M, Tofalo R, Visciano P, Corsetti A, Suzzi G. 2012. Biogenic amines in Italian Pecorino cheese. Frontiers in Microbiology 3:171. doi: 10.3389/fmicb.2012.00171. Available from:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347038/pdf/fmicb-03-00171.pdf. Accessed 2016 April 8.
    • (2012) Frontiers in Microbiology , vol.3 , pp. 171
    • Schirone, M.1    Tofalo, R.2    Visciano, P.3    Corsetti, A.4    Suzzi, G.5
  • 173
    • 53249105532 scopus 로고    scopus 로고
    • Influence of pasteurised milk, raw milk, and different ripening cultures on biogenic amine concentrations in semi-soft cheeses during ripening
    • Schneller R, Good P, Jenny M. 1997. Influence of pasteurised milk, raw milk, and different ripening cultures on biogenic amine concentrations in semi-soft cheeses during ripening. Z Lebensm Unters Forsch 204:265–72.
    • (1997) Z Lebensm Unters Forsch , vol.204 , pp. 265-272
    • Schneller, R.1    Good, P.2    Jenny, M.3
  • 174
    • 0028843841 scopus 로고
    • A new model for disruption of the ornithine decarboxylase gene, SPE1, in Saccharomyces cerevisiae exhibits growth arrest and genetic instability at the MAT locus
    • Schwartz B, Hittelman A, Daneshvar L, Basu HS, Marton LJ, Feuerstein BG. 1995. A new model for disruption of the ornithine decarboxylase gene, SPE1, in Saccharomyces cerevisiae exhibits growth arrest and genetic instability at the MAT locus. Biochem J 312(Pt 1):83–90.
    • (1995) Biochem J , vol.312 , pp. 83-90
    • Schwartz, B.1    Hittelman, A.2    Daneshvar, L.3    Basu, H.S.4    Marton, L.J.5    Feuerstein, B.G.6
  • 175
    • 0025030562 scopus 로고
    • Polyamine metabolism
    • Seiler N. 1990. Polyamine metabolism. Digestion 46 Suppl 2:319–30.
    • (1990) Digestion , vol.2 , pp. 319-330
    • Seiler, N.1
  • 177
    • 0031928331 scopus 로고    scopus 로고
    • Characterization of polyamine synthesis pathway in Bacillus subtilis 168
    • Sekowska A, Bertin P, Danchin A. 1998. Characterization of polyamine synthesis pathway in Bacillus subtilis 168. Mol Microbiol 29:851–8.
    • (1998) Mol Microbiol , vol.29 , pp. 851-858
    • Sekowska, A.1    Bertin, P.2    Danchin, A.3
  • 178
    • 40549096043 scopus 로고    scopus 로고
    • A multifaceted role for polyamines in bacterial pathogens
    • Shah P, Swiatlo E. 2008. A multifaceted role for polyamines in bacterial pathogens. Mol Microbiol 68:4–16.
    • (2008) Mol Microbiol , vol.68 , pp. 4-16
    • Shah, P.1    Swiatlo, E.2
  • 179
    • 0030265217 scopus 로고    scopus 로고
    • Significance of biogenic amines to food safety and human health
    • Shalaby AR. 1996. Significance of biogenic amines to food safety and human health. Food Res Intl 29:675–90.
    • (1996) Food Res Intl , vol.29 , pp. 675-690
    • Shalaby, A.R.1
  • 180
    • 0042684931 scopus 로고    scopus 로고
    • Changes in biogenic amines in mature and germinating legume seeds and their behavior during cooking
    • Shalaby AR. 2000. Changes in biogenic amines in mature and germinating legume seeds and their behavior during cooking. Nahrung 44:23–7.
    • (2000) Nahrung , vol.44 , pp. 23-27
    • Shalaby, A.R.1
  • 181
    • 84975704445 scopus 로고    scopus 로고
    • Quality and safety of irradiated food regarding biogenic amines: ras cheese
    • Shalaby AR, Anwar MM, Sallam EM, Emam WH. 2016. Quality and safety of irradiated food regarding biogenic amines: ras cheese. Int J Food Sci Technol 51:1048–54.
    • (2016) Int J Food Sci Technol , vol.51 , pp. 1048-1054
    • Shalaby, A.R.1    Anwar, M.M.2    Sallam, E.M.3    Emam, W.H.4
  • 182
    • 0005225952 scopus 로고    scopus 로고
    • Biogenic amines: their importance in foods
    • Silla Santos MH. 1996. Biogenic amines: their importance in foods. Int J Food Microbiol 29:213–31.
    • (1996) Int J Food Microbiol , vol.29 , pp. 213-231
    • Silla Santos, M.H.1
  • 183
    • 0020422867 scopus 로고
    • Enzymes of agmatine degradation and the control of their synthesis in Streptococcus faecalis
    • Simon JP, Stalon V. 1982. Enzymes of agmatine degradation and the control of their synthesis in Streptococcus faecalis. J Bacteriol 152:676–81.
    • (1982) J Bacteriol , vol.152 , pp. 676-681
    • Simon, J.P.1    Stalon, V.2
  • 184
    • 0020315318 scopus 로고
    • Control of enzyme synthesis in the arginine deiminase pathway of Streptococcus faecalis
    • Simon JP, Wargnies B, Stalon V. 1982. Control of enzyme synthesis in the arginine deiminase pathway of Streptococcus faecalis. J Bacteriol 150:1085–90.
    • (1982) J Bacteriol , vol.150 , pp. 1085-1090
    • Simon, J.P.1    Wargnies, B.2    Stalon, V.3
  • 185
    • 0015053146 scopus 로고
    • The occurrence, metabolism and functions of amines in plants
    • Smith TA. 1971. The occurrence, metabolism and functions of amines in plants. Biol Rev 46:201–41.
    • (1971) Biol Rev , vol.46 , pp. 201-241
    • Smith, T.A.1
  • 186
    • 0000827479 scopus 로고
    • Towards a regulatory limit for biogenic amines in fish, cheese and sauerkraut
    • Spanjer MC, van Roode BASW. 1991. Towards a regulatory limit for biogenic amines in fish, cheese and sauerkraut. De Ware(n)-Chemicus 21:139–67.
    • (1991) De Ware(n)-Chemicus , vol.21 , pp. 139-167
    • Spanjer, M.C.1    van Roode, B.A.S.W.2
  • 187
    • 34147112929 scopus 로고    scopus 로고
    • Arginine metabolism in wine Lactobacillus plantarum: in vitro activities of the enzymes arginine deiminase (ADI) and ornithine transcarbamilase (OTCase)
    • Spano G, Massa S, Arena M, de Nadra M. 2007. Arginine metabolism in wine Lactobacillus plantarum: in vitro activities of the enzymes arginine deiminase (ADI) and ornithine transcarbamilase (OTCase). Ann Microbiol 57:67–70.
    • (2007) Ann Microbiol , vol.57 , pp. 67-70
    • Spano, G.1    Massa, S.2    Arena, M.3    de Nadra, M.4
  • 189
    • 0242549674 scopus 로고    scopus 로고
    • Application of lactic acid bacteria starter cultures for decreasing the biogenic amine levels in sauerkraut
    • Špička J, Kalač P, Bover-Cid S, Křížek M. 2002. Application of lactic acid bacteria starter cultures for decreasing the biogenic amine levels in sauerkraut. Eur Food Res Technol 215:509–14.
    • (2002) Eur Food Res Technol , vol.215 , pp. 509-514
    • Špička, J.1    Kalač, P.2    Bover-Cid, S.3    Křížek, M.4
  • 190
    • 84964316661 scopus 로고
    • Biogenic amines in cheese and other fermented foods: a review
    • Stratton JE, Hutkins RW, Taylor SL. 1991. Biogenic amines in cheese and other fermented foods: a review. J Food Prot 54:460–70.
    • (1991) J Food Prot , vol.54 , pp. 460-470
    • Stratton, J.E.1    Hutkins, R.W.2    Taylor, S.L.3
  • 191
    • 84885394429 scopus 로고    scopus 로고
    • Expression of the agmatine deiminase pathway in Enterococcus faecalis is activated by the AguR regulator and repressed by CcpA and PTS(Man) systems
    • Suarez C, Espariz M, Blancato VS, Magni C. 2013. Expression of the agmatine deiminase pathway in Enterococcus faecalis is activated by the AguR regulator and repressed by CcpA and PTS(Man) systems. PLoS One 8:e76170.
    • (2013) PLoS One , vol.8
    • Suarez, C.1    Espariz, M.2    Blancato, V.S.3    Magni, C.4
  • 192
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor CW, 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
  • 193
    • 0015484128 scopus 로고
    • Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines
    • Tabor H, Tabor CW. 1972. Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. Adv Enzymol Relat Areas Mol Biol 36:203–68.
    • (1972) Adv Enzymol Relat Areas Mol Biol , vol.36 , pp. 203-268
    • Tabor, H.1    Tabor, C.W.2
  • 194
    • 0020445270 scopus 로고
    • Outbreak of histamine poisoning associated with consumption of Swiss cheese
    • Taylor SL, Keefe TJ, Windham ES, Howell JF. 1982. Outbreak of histamine poisoning associated with consumption of Swiss cheese. J Food Prot 45:455–7.
    • (1982) J Food Prot , vol.45 , pp. 455-457
    • Taylor, S.L.1    Keefe, T.J.2    Windham, E.S.3    Howell, J.F.4
  • 197
    • 79251632949 scopus 로고    scopus 로고
    • Staphylococcus lugdunensis is the likely origin of the ornithine decarboxylase operon in Staphylococcus epidermidis 2015B
    • Tsoi HW, Tse H. 2011. Staphylococcus lugdunensis is the likely origin of the ornithine decarboxylase operon in Staphylococcus epidermidis 2015B. Appl Environ Microbiol 77:392–3.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 392-393
    • Tsoi, H.W.1    Tse, H.2
  • 199
    • 0037172348 scopus 로고    scopus 로고
    • An overview of small-scale food fermentation technologies in developing countries with special reference to Thailand: scope for their improvement
    • Valyasevi R, Rolle RS. 2002. An overview of small-scale food fermentation technologies in developing countries with special reference to Thailand: scope for their improvement. Int J Food Microbiol 75:231–9.
    • (2002) Int J Food Microbiol , vol.75 , pp. 231-239
    • Valyasevi, R.1    Rolle, R.S.2
  • 200
    • 67349108049 scopus 로고    scopus 로고
    • Relating microbiological criteria to food safety objectives and performance objectives
    • van Schothorst M, Zwietering MH, Ross T, Buchanan RL, Cole MB. 2009. Relating microbiological criteria to food safety objectives and performance objectives. Food Control 20:967–79.
    • (2009) Food Control , vol.20 , pp. 967-979
    • van Schothorst, M.1    Zwietering, M.H.2    Ross, T.3    Buchanan, R.L.4    Cole, M.B.5
  • 201
    • 0014250791 scopus 로고
    • Incorporation of DL-(2-14C) ornithine and DL-(5-14C) arginine in milk constituents by the isolated lactating sheep udder
    • Verbeke R, Peeters G, Massart-Leen AM, Cocquyt G. 1968. Incorporation of DL-(2-14C) ornithine and DL-(5-14C) arginine in milk constituents by the isolated lactating sheep udder. Biochem J 106:719–24.
    • (1968) Biochem J , vol.106 , pp. 719-724
    • Verbeke, R.1    Peeters, G.2    Massart-Leen, A.M.3    Cocquyt, G.4
  • 202
    • 69749099930 scopus 로고    scopus 로고
    • Environmental pH determines citrulline and ornithine release through the arginine deiminase pathway in Lactobacillus fermentum IMDO 130101
    • Vrancken G, Rimaux T, Weckx S, De Vuyst L, Leroy F. 2009. Environmental pH determines citrulline and ornithine release through the arginine deiminase pathway in Lactobacillus fermentum IMDO 130101. Int J Food Microbiol 135:216–22.
    • (2009) Int J Food Microbiol , vol.135 , pp. 216-222
    • Vrancken, G.1    Rimaux, T.2    Weckx, S.3    De Vuyst, L.4    Leroy, F.5
  • 204
    • 70350468848 scopus 로고    scopus 로고
    • Complete genome sequence of Lactobacillus johnsonii FI9785, a competitive exclusion agent against pathogens in poultry
    • Wegmann U, Overweg K, Horn N, Goesmann A, Narbad A, Gasson MJ, Shearman C. 2009. Complete genome sequence of Lactobacillus johnsonii FI9785, a competitive exclusion agent against pathogens in poultry. J Bacteriol 191:7142–3.
    • (2009) J Bacteriol , vol.191 , pp. 7142-7143
    • Wegmann, U.1    Overweg, K.2    Horn, N.3    Goesmann, A.4    Narbad, A.5    Gasson, M.J.6    Shearman, C.7
  • 205
    • 57049170788 scopus 로고    scopus 로고
    • Irradiated chinese Rugao ham: Changes in volatile N-nitrosamine, biogenic amine and residual nitrite during ripening and post-ripening
    • Wei F, Xu X, Zhou G, Zhao G, Li C, Zhang Y, Qi J. 2009. Irradiated chinese Rugao ham: Changes in volatile N-nitrosamine, biogenic amine and residual nitrite during ripening and post-ripening. Meat Sci 81:451–5.
    • (2009) Meat Sci , vol.81 , pp. 451-455
    • Wei, F.1    Xu, X.2    Zhou, G.3    Zhao, G.4    Li, C.5    Zhang, Y.6    Qi, J.7
  • 207
    • 8844233526 scopus 로고    scopus 로고
    • Histamine intolerance-like symptoms in healthy volunteers after oral provocation with liquid histamine
    • Wohrl S, Hemmer W, Focke M, Rappersberger K, Jarisch R. 2004. Histamine intolerance-like symptoms in healthy volunteers after oral provocation with liquid histamine. Allergy Asthma Proc 25:305–11.
    • (2004) Allergy Asthma Proc , vol.25 , pp. 305-311
    • Wohrl, S.1    Hemmer, W.2    Focke, M.3    Rappersberger, K.4    Jarisch, R.5
  • 209
    • 69349104713 scopus 로고    scopus 로고
    • Effect of fermentation temperature on the microbial and physicochemical properties of silver carp sausages inoculated with Pediococcus pentosaceus
    • Xu Y, Xia W, Yang F, Kim JM, Nie X. 2010. Effect of fermentation temperature on the microbial and physicochemical properties of silver carp sausages inoculated with Pediococcus pentosaceus. Food Chem 118:512–8.
    • (2010) Food Chem , vol.118 , pp. 512-518
    • Xu, Y.1    Xia, W.2    Yang, F.3    Kim, J.M.4    Nie, X.5
  • 210
    • 84876855409 scopus 로고    scopus 로고
    • Expression, purification, and biochemical properties of arginase from Bacillus subtilis 168
    • Yu JJ, Park KB, Kim SG, Oh SH. 2013. Expression, purification, and biochemical properties of arginase from Bacillus subtilis 168. J Microbiol 51:222–8.
    • (2013) J Microbiol , vol.51 , pp. 222-228
    • Yu, J.J.1    Park, K.B.2    Kim, S.G.3    Oh, S.H.4
  • 211
    • 0025653639 scopus 로고
    • Relationship between tyramine potentiation and monoamine oxidase (MAO) inhibition: comparison between moclobemide and other MAO inhibitors
    • Zimmer R. 1990. Relationship between tyramine potentiation and monoamine oxidase (MAO) inhibition: comparison between moclobemide and other MAO inhibitors. Acta Psychiatr Scand Suppl 360:81–3.
    • (1990) Acta Psychiatr Scand Suppl , vol.360 , pp. 81-83
    • Zimmer, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.