scholarly journals Tyrosine decarboxylase activity of Lactobacillus brevis IOEB 9809 isolated from wine and L. brevis ATCC 367

1999 ◽  
Vol 180 (1) ◽  
pp. 55-60 ◽  
Author(s):  
V. Moreno-Arribas ◽  
A. Lonvaud-Funel
Keyword(s):  
Lactobacillus Brevis ◽  
Decarboxylase Activity ◽  
Tyrosine Decarboxylase

scholarly journals The Mechanism of the Tyrosine Transporter TyrP Supports a Proton Motive Tyrosine Decarboxylation Pathway in Lactobacillus brevis

2006 ◽  
Vol 188 (6) ◽  
pp. 2198-2206 ◽  
Author(s):  
Wout A. M. Wolken ◽  
Patrick M. Lucas ◽  
Aline Lonvaud-Funel ◽  
Juke S. Lolkema
Keyword(s):  
Phenyl Ring ◽  
Lactobacillus Brevis ◽  
Proton Motive Force ◽  
Proton Pumping ◽  
Hydroxyl Group ◽  
Transporter Gene ◽  
Tyrosine Decarboxylase ◽  
Rate Analysis ◽  
Substrate Analogues ◽  
Decarboxylation Reaction

ABSTRACT The tyrosine decarboxylase operon of Lactobacillus brevis IOEB9809 contains, adjacent to the tyrosine decarboxylase gene, a gene for TyrP, a putative tyrosine transporter. The two genes potentially form a proton motive tyrosine decarboxylation pathway. The putative tyrosine transporter gene of L. brevis was expressed in Lactococcus lactis and functionally characterized using right-side-out membranes. The transporter very efficiently catalyzes homologous tyrosine-tyrosine exchange and heterologous exchange between tyrosine and its decarboxylation product tyramine. Tyrosine-tyramine exchange was shown to be electrogenic. In addition to the exchange mode, the transporter catalyzes tyrosine uniport but at a much lower rate. Analysis of the substrate specificity of the transporter by use of a set of 19 different tyrosine substrate analogues showed that the main interactions between the protein and the substrates involve the amino group and the phenyl ring with the para hydroxyl group. The carboxylate group that is removed in the decarboxylation reaction does not seem to contribute to the affinity of the protein for the substrates significantly. The properties of the TyrP protein are those typical for precursor-product exchangers that operate in proton motive decarboxylation pathways. It is proposed that tyrosine decarboxylation in L. brevis results in proton motive force generation by an indirect proton pumping mechanism.

Production of Tyrosine and Histidine Decarboxylase by Dairy-Related Bacteria

1977 ◽  
Vol 40 (4) ◽  
pp. 241-245 ◽  
Author(s):  
M. N. VOIGT ◽  
R. R. EITENMILLER
Keyword(s):  
Histidine Decarboxylase ◽  
Micrococcus Luteus ◽  
Coli Strain ◽  
Starter Cultures ◽  
Decarboxylase Activity ◽  
Tyrosine Decarboxylase ◽  
Streptococcus Lactis ◽  
Low Levels ◽  
Co2 Release ◽  
Manometric Technique

Manometric and radiometric procedures were used to determine the ability of 38 dairy-related bacteria and four commercial starter preparations to produce tyrosine and histidine decarboxylase. All of the cultures had slight ability to cause release of 14CO2 from carboxyl 14C-tyrosine and most released 14CO2 from labeled histidine; however, because of inherent errors of the assay in detecting low levels of specific decarboxylase activity, the CO2 release was not considered positive for specific decarboxylase activity unless the results were verified by the manometric technique. One strain of Streptococcus lactis, a Micrococcus luteus strain, and two Leuconostoc cremoris strains had active tyrosine decarboxylase systems. Only Clostridium perfringens and an Escherichia coli strain were found to produce histidine decarboxylase. None of the commercial starter cultures produced the enzymes. It was not determined whether tyramine or histamine was produced by the nonspecific decarboxylase activity.

Note. Histamine production by some lactic acid bacteria isolated from ciders / Nota. Producción de histamina por algunas bacterias lácticas aisladas a partir de sidras

2000 ◽  
Vol 6 (2) ◽  
pp. 117-121 ◽  
Author(s):  
G. del Campo ◽  
I. Lavado ◽  
M. Dueñas ◽  
A. Irastorza
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Histidine Decarboxylase ◽  
Lactobacillus Brevis ◽  
Oenococcus Oeni ◽  
Decarboxylase Activity ◽  
Histamine Production ◽  
Different Temperatures ◽  
Kinetics Of ◽  
Lactobacillus Spp

Histidine decarboxylase activity has been investigated in 23 strains of lactic acid bacteria, belonging to Oenococcus oeni, Lactobacillus brevis and Lactobacillus spp., isolated during the cidermaking process at different stages of fermentation. After 14 days at 25 °C on a semisynthetic medium supplemented with L-histidine, 13 strains were histamine producers and six of these strains were selected to study the kinetics of growth and histamine production at different temperatures. The results showed that histamine accumulation was maximal at 25 °C after 10-15 days of growth. Comparison of growth and histamine level curves demonstrated a delay time of eight days between maximal growth and the highest histamine content of the cultures.

Isolation of Tyrosine Decarboxylaseless Mutants of a Bacteriocin-Producing Enterococcus faecalis Strain and Their Application in Cheese

1995 ◽  
Vol 58 (11) ◽  
pp. 1222-1226 ◽  
Author(s):  
HAN M. L. J. JOOSTEN ◽  
PILAR GAYA ◽  
MANUEL NUÑEZ
Keyword(s):  
Enterococcus Faecalis ◽  
Parental Strain ◽  
Residual Activity ◽  
Raw Milk ◽  
Listeria Innocua ◽  
Decarboxylase Activity ◽  
Tyrosine Decarboxylase ◽  
Mutant Strains ◽  
Raw Milk Cheese ◽  
Tyrosine Content

Enterococcus faecalis INIA 4, a bacteriocin-producing strain, was exposed to the mutagenic agent ethyl methanesulfonate (EMS). A modified differential plating medium permitted the isolation of mutants INIA 4-01 to 4-09 with reduced tyrosine decarboxylase activity. All mutant strains displayed rapid growth in milk, while bacteriocin production ranged from 15 to 125% as compared to the parental strain. Enterococcus faecalis INIA 4, INIA 4-07 (less than 0.1% residual tyrosine decarboxylase activity) and INIA 4-03 (10% residual activity) were used in cheese-making experiments. In cheese made from pasteurized milk, using INIA 4-07 as adjunct starter, tyramine was not produced (< 5 mg/kg of cheese after 4 months of ripening). Suppression of Listeria innocua in raw-milk cheeses made using INIA 4-03 and INIA 4-07 was equal to that observed in the cheese made using the parental strain INIA 4. After 2 months of ripening, no free tyrosine and 195 mg/kg of tyramine were detected in the cheese with INIA 4. The tyrosine content of the cheeses made with INIA 4-03 and INIA 4-07 and of the control cheese was approximately 95 mg/kg. The cheeses with INIA 4-03 and 4-07 contained 116 and 120 mg/kg of tyramine respectively, values comparable to the level of 101 mg/kg detected in a control raw-milk cheese to which no enterococci were added. The relatively high tyramine formation in the cheeses made with INIA 4-03 and INIA 4-07 and in the control cheese was probably caused by the decarboxylating activity of the indigenous flora of the raw milk.

Rapid Detection and Quantification of Tyrosine Decarboxylase Gene (tdc) and Its Expression in Gram-Positive Bacteria Associated with Fermented Foods Using PCR-Based Methods†

2008 ◽  
Vol 71 (1) ◽  
pp. 93-101 ◽  
Author(s):  
SANDRA TORRIANI ◽  
VERONICA GATTO ◽  
SILVIA SEMBENI ◽  
ROSANNA TOFALO ◽  
GIOVANNA SUZZI ◽  
...  
Keyword(s):  
Meat Products ◽  
High Specificity ◽  
Fermented Foods ◽  
Decarboxylase Activity ◽  
Tyrosine Decarboxylase ◽  
Lactobacillus Curvatus ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Pure Cultures ◽  
Detection And Quantification

In this study, PCR-based procedures were developed to detect the occurrence and quantify the expression of the tyrosine decarboxylase gene (tdc) in gram-positive bacteria associated with fermented foods. Consensus primers were used in conventional and reverse transcription PCR to analyze a collection of 87 pure cultures of lactic acid bacteria and staphylococci. All enterococci, Staphylococcus epidermidis, Lactobacillus brevis, Lactobacillus curvatus, and Lactobacillus fermentum strains and1of 10 Staphylococcus xylosus strains produced amplification products with the primers DEC5 and DEC3 in accordance with results of the screening plate method and with previously reported result obtained with high-performance liquid chromatography. No amplicons were obtained for tyramine-negative strains, confirming the high specificity of these new primers. A novel quantitative real-time PCR assay was successfully applied to quantify tdc and its transcript in pure cultures and in meat and meat products. This assay allowed estimation of the influence of different variables (pH, temperature, and NaCl concentration) on the tdc expression of the tyraminogenic strain Enterococcus faecalis EF37 after 72 h of growth in M17 medium. Data obtained suggest that stressful conditions could induce greater tyrosine decarboxylase activity. The culture-independent PCR procedures developed here may be used for reliable and fast detection and quantification of bacterial tyraminogenic activity without the limitations of conventional techniques.

scholarly journals Tyrosine decarboxylase activity of Enterococcus mundtii : new insights into phenotypic and genetic aspects

2016 ◽  
Vol 9 (6) ◽  
pp. 801-813 ◽  
Author(s):  
Veronica Gatto ◽  
Giulia Tabanelli ◽  
Chiara Montanari ◽  
Valentina Prodomi ◽  
Eleonora Bargossi ◽  
...  
Keyword(s):  
Decarboxylase Activity ◽  
Tyrosine Decarboxylase ◽  
Enterococcus Mundtii

scholarly journals Modeling the Aminogenic Potential of Enterococcus faecalis EF37 in Dry Fermented Sausages through Chemical and Molecular Approaches

2008 ◽  
Vol 74 (9) ◽  
pp. 2740-2750 ◽  
Author(s):  
Fausto Gardini ◽  
Sara Bover-Cid ◽  
Rosanna Tofalo ◽  
Nicoletta Belletti ◽  
Veronica Gatto ◽  
...  
Keyword(s):  
Sodium Chloride ◽  
Enterococcus Faecalis ◽  
Chloride Concentration ◽  
Analytical Determination ◽  
Decarboxylase Activity ◽  
Sodium Chloride Concentration ◽  
Tyrosine Decarboxylase ◽  
Fermented Sausage ◽  
Fermentation Temperature ◽  
Molecular Approaches

ABSTRACT Amino acid decarboxylase activity of the Enterococcus faecalis strain EF37 was monitored during fermentation and ripening of a traditional dry fermented sausage from Northern Italy (Salame Veronese) by means of microbiological, chemical, and molecular approaches in relation to three technological factors: fermentation temperature, sodium chloride concentration, and amount of glucose added to the meat mixture. Besides the analytical determination of tyramine and phenylethylamine accumulation and the counts of enterococci, the presence and quantification of the tyrosine decarboxylase gene (tdc) and its mRNA transcript were also investigated by using real-time PCR. According to the mathematical models obtained, all of the three factors studied were statistically significant and microbiologically relevant for the early development of enterococci, although the fermentation temperature had a more relevant influence on the enterococcal viable cells of the ripened product. Sodium chloride concentration was the most determinant factor of the final tyramine and 2-phenylethylamine accumulation and also of the levels of tdc present in the final product. In contrast, an effect of glucose concentration on tdc expression was observed in the last period of ripening. Moreover, increasing amounts of sodium chloride and decreasing fermentation temperature resulted in a reduced tdc expression. This is the first time that bacterial tyrosine decarboxylase potential is directly examined through a molecular approach in a fermented meat. The quantification of tdc and its transcript can help to elucidate the critical steps and factors during food manufacturing at which bacterial aminogenesis is possible, thus allowing researchers to propose technological measures to control decarboxylase activities.

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