Biologically Active Amines in Food: A Review

Rice, S. L.; Eitenmiller, Ronald R.; Koehler, P. E.

doi:10.4315/0022-2747-39.5.353

Cited by 178 publications

(64 citation statements)

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“…In contrast, no strain was able to produce tryptamine in any of the non-tryptophan-supplemented decarboxylase media. The weak tryptophan decarboxylase activity of our strains could be related to the low tryptamine concentrations previously reported in cheeses (Voight et al 1974 ;Rice et al 1976 ;Bütikofer et al 1990).…”

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confidence: 72%

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Biogenic amine production by wild lactococcal and leuconostoc strains

Llano

Cuesta

Rodríguez

1998

Letters in Applied Microbiology

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D. GONZÁ LEZ DE LLANO, P. CUESTA AND A. RODRÍGU EZ . 1998. Two qualitative and one quantitative HPLC methods were evaluated for the detection of biogenic amine producers among wild dairy lactococcal and leuconostoc strains. High tyramine producers ranging from 370 to 807 mg l −1 were detected by qualitative methods and confirmed by HPLC analysis. Tyramine levels detected throughout the incubation time depended on the concentration of the amino acid precursor available and no tyramine production was observed when strains were grown in milk. However, increasing amounts of tyramine were detected in cultures grown in milk supplemented with different concentrations of tyrosine. Qualitative methods failed to detect weak producers so that tryptamine production (³7 mg l −1 ) could only be determined by HPLC. None of the tested strains was able to produce histamine. Simultaneous production of different amines was observed by HPLC although no colour change was observed in the specific decarboxylase media. Thus, it was concluded that the amine forming ability should be taken into account when selecting starters for milk fermentations. Qualitative methods could be used as a first screening step to eliminate the highest amine producers while the quantitative methods would detect any producing strain.

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confidence: 72%

“…In these cases, the symptoms observed are nausea, respiratory distress, hot flushes, sweating, heart palpitations, headache, bright red rash, oral burning and hyper-or hypotension (Rice et al 1976).…”

Section: Introductionmentioning

confidence: 99%

Biogenic amine production by wild lactococcal and leuconostoc strains

Llano

Cuesta

Rodríguez

1998

Letters in Applied Microbiology

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“…Furthermore, beer production provides some necessary factors that govern and help in the formation of amines. Not only are the free amino acids precursors are available in raw materials of beer, but also the microorganisms with amino acid decarboxylating activity 7,8,11 can be present. There are three types of biogenic amine groups in beers based on their origin.…”

Section: Introductionmentioning

confidence: 99%

Biogenic Amine Content of Beers Consumed in Turkey and Influence of Storage Conditions on Biogenic Amine Formation

Anlı

Vural

Demiray

et al. 2006

Journal of the Institute of Brewing

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The biogenic amine content of beers available in Turkey, both domestic production and imported products, was investigated. A total of 17 domestic and 13 imported beers were evaluated in terms of 8 different biogenic amines (histamine, tyramine, spermine, spermidine, 2-phenylethylamine, putrescine, tryptamine and cadaverine). HPLC methodology with pre-column derivatization and photodiode array detection after derivatization with dansyl chloride was used for quantification. In addition, the evolution of important amines such as histamine, tyramine, putrescine and cadaverine were investigated during different storage conditions by response surface methodology. The results indicated that both storage temperature and storage time were important factors affecting biogenic amine content. Histamine and putrescine increased during storage, but then decreased after reaching a maximum level after six weeks. With the biogenic amines tyramine and cadaverine, the amounts increased during the entire storage period. At higher storage temperatures, the formation of biogenic amines increased.

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“…The histamine-producing L. buchnen ST2A was isolated from Swiss cheese implicated in an outbreak of food poisoning (24). The occurrence of histamine and other biogenic amines like cadaverine, putrescine, tyramine, and tryptamine in food products can result in food poisoning (19,24,25). These biogenic amines are formed by many different bacteria by decarboxylation of the corresponding amino acids (6,20).…”

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Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri

et al. 1993

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Lactobaciflus buchneri ST2A vigorously decarboxylates histidine to the biogenic amine histamine, which is excreted into the medium. Cells grown in the presence of histidine generate both a transmembrane pH gradient, inside alkaline, and an electrical potential (A*), inside negative, upon addition of histidine. Studies of the mechanism of histidine uptake and histamine excretion in membrane vesicles and proteoliposomes devoid of cytosolic histidine decarboxylase activity demonstrate that histidine uptake, histamine efflux, and histidine/ histamine exchange are electrogenic processes. Histidine/histamine exchange is much faster than the unidirectional fluxes of these substrates, is inhibited by an inside-negative A* and is stimulated by an inside positive A*. These data suggest that the generation of metabolic energy from histidine decarboxylation results from an electrogenic histidine/histamine exchange and indirect proton extrusion due to the combined action of the decarboxylase and carrier-mediated exchange. The abundance of amino acid decarboxylation reactions among bacteria suggests that this mechanism of metabolic energy generation and/or pH regulation is widespread.Several precursor/product antiport mechanisms have been shown or were anticipated to be involved in generation of metabolic energy (16). Metabolic energy can be obtained from these mechanisms by substrate level phosphorylation (5,17) or by the formation of transmembrane ion gradients (ion and proton motive force). Characteristic for all of these precursor/product antiport mechanisms is that the product is structurally similar to the precursor. Transport of precursor and product can be catalyzed by one membrane transport protein which binds both precursor and product with high affinity. The usual mode in which these carrier proteins function is that of exchange: i.e., reorientation of the substrate binding site to either side of the membrane takes place while a substrate is bound. When the product is more positively charged than the precursor, this antiport generates an inside-negative electrical potential gradient across the membrane. Two examples of such carriers which have been studied in detail are the oxalate/formate antiporter of Oxalobacter formigenes (22) and the malate/lactate carrier of Lactococcus lactis (18). Because the metabolic conversion from oxalate to formate or from malate to lactate is a decarboxylation whereby the carboxylic group leaves the cytoplasm as neutral carbon dioxide or dihydrogen carbonate, the net effect of metabolism and electrogenic precursor/ product antiport is the extrusion of one proton. Consequently, a proton motive force is generated from the free energy of decarboxylation.A different mechanism by which metabolic energy is generated from a decarboxylation reaction is found in the Na'-translocating oxaloacetate decarboxylase (3). In this system, decarboxylation is catalyzed by a membrane-bound protein which uses the free energy directly to translocate sodium ions across the membrane. In this study, it will b...

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Biologically Active Amines in Food: A Review

Cited by 178 publications

References 0 publications

Biogenic amine production by wild lactococcal and leuconostoc strains

Biogenic amine production by wild lactococcal and leuconostoc strains

Biogenic Amine Content of Beers Consumed in Turkey and Influence of Storage Conditions on Biogenic Amine Formation

Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri

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