Histamine production by wine lactic acid bacteria: isolation of a histamine-producingstrain of Leuconostoc oenos

1994 ◽  
Vol 77 (4) ◽  
pp. 401-407 ◽  
Author(s):  
Aline Lonvaud-Funel ◽  
Annick Joyeux
2020 ◽  
Vol 86 (3) ◽  
pp. 204-213
Author(s):  
YUJI HAMAYA ◽  
AYUMI HONDA-FURUTANI ◽  
YOUHEI FUKUI ◽  
YUTAKA YANO ◽  
TOSHIHIKO TAKEWA ◽  
...  

1989 ◽  
Vol 52 (4) ◽  
pp. 240-243 ◽  
Author(s):  
D. F. SPLITTSTOESSER ◽  
B. O. STOYLA

Various compounds were tested to determine whether they would substitute for SO2 as inhibitors of strains of Leuconostoc oenos when inoculated into a model fruit beverage containing 5°C Brix Concord grape and 0.1% yeast extract. The following additives and their maximal concentrations exhibited varying degrees of inhibitory activity: fumaric acid, 1.5 mg/ml; sorbic acid, 300 μg/ml; decanoic acid, 20 μg/ml; nisin, 100 IU/ml; and carbon dioxide, 2.8 volumes. Effectiveness of the inhibitors was enhanced by the presence of 8 to 10% ethanol, and was inversely related to the size of the inoculum.


2005 ◽  
Vol 71 (3) ◽  
pp. 1417-1424 ◽  
Author(s):  
Patrick M. Lucas ◽  
Wout A. M. Wolken ◽  
Olivier Claisse ◽  
Juke S. Lolkema ◽  
Aline Lonvaud-Funel

ABSTRACT Histamine production from histidine in fermented food products by lactic acid bacteria results in food spoilage and is harmful to consumers. We have isolated a histamine-producing lactic acid bacterium, Lactobacillus hilgardii strain IOEB 0006, which could retain or lose the ability to produce histamine depending on culture conditions. The hdcA gene, coding for the histidine decarboxylase of L. hilgardii IOEB 0006, was located on an 80-kb plasmid that proved to be unstable. Sequencing of the hdcA locus disclosed a four-gene cluster encoding the histidine decarboxylase, a protein of unknown function, a histidyl-tRNA synthetase, and a protein, which we named HdcP, showing similarities to integral membrane transporters driving substrate/product exchange. The gene coding for HdcP was cloned downstream of a sequence specifying a histidine tag and expressed in Lactococcus lactis. The recombinant HdcP could drive the uptake of histidine into the cell and the exchange of histidine and histamine. The combination of HdcP and the histidine decarboxylase forms a typical bacterial decarboxylation pathway that may generate metabolic energy or be involved in the acid stress response. Analyses of sequences present in databases suggest that the other two proteins have dispensable functions. These results describe for the first time the genes encoding a histamine-producing pathway and provide clues to the parsimonious distribution and the instability of histamine-producing lactic acid bacteria.


OENO One ◽  
1985 ◽  
Vol 19 (3) ◽  
pp. 149
Author(s):  
Annick Joyeux ◽  
Aline Lonvaud-Funel

<p style="text-align: justify;">La réactivation préalable des bactéries lactiques est indispensable avant l'inoculation des vins. Le mode opératoire est précisé : le milieu optimum est à base de jus de raisin.</p><p style="text-align: justify;">Différentes préparations industrielles ont été testées au laboratoire. Celles de <em>Leuconostoc œnos</em> ont donné de bons résultats. L'une d'entre elles a été utilisée dans la pratique au cours des deux dernières campagnes de vinification. Les succès obtenus, surtout en 1984 dans des cas particulièrement difficiles montrent bien l'efficacité de ce procédé pour le déclenchement de la fermentation malolactique.</p><p style="text-align: justify;">+++</p><p style="text-align: justify;">The previous reactivation of lactic acid bacteria is essential before the inoculation of the wine. The method is specified: the optimium media is made with grape must.</p><p style="text-align: justify;">Several industrial preparations of bacteria were tried; those constituted with <em>Leuconostoc oenos</em> gave good results. One of them was utilized in practice during the two last vinification campaigns. The success obtained, especially in 1984 in particular difficult cases give proof of the efficiency of this process to start the malolactic fermentation.</p>


2000 ◽  
Vol 6 (2) ◽  
pp. 117-121 ◽  
Author(s):  
G. del Campo ◽  
I. Lavado ◽  
M. Dueñas ◽  
A. Irastorza

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.


2016 ◽  
Vol 66 (3) ◽  
pp. 1277-1284 ◽  
Author(s):  
Takeshi Kobayashi ◽  
Xuguang Wang ◽  
Naoki Shigeta ◽  
Chihiro Taguchi ◽  
Kouichi Ishii ◽  
...  

1991 ◽  
Vol 37 (3) ◽  
pp. 211-217 ◽  
Author(s):  
Gerd Battermann ◽  
Ferdinand Radler

Malolactic enzyme of lactic acid bacteria catalyzes the decarboxylation of L-malate to L-lactate. The appropriate enzyme of Lactobacillus casei, Leuconostoc oenos, and Leuconostoc mesenteroides, as well as the malic enzyme of Lactobacillus casei, were purified to electrophoretic homogeneity by salmine sulphate precipitation, ion-exchange chromatography, hydrophobic chromatography, and gel filtration. The malolactic enzymes investigated were similar and showed only minor variations in the isoelectric point and the temperature optimum. The molecular weight of the subunit of all malolactic enzymes was about 65 000. Aggregates were formed, depending on the pH. The optimum activity of malolactic enzyme was observed at pH 5.8–6.0, and at this pH the dimer was stable. In addition to Mn2+ and NAD, the malolactic enzyme required K+, which was replaceable by NH4+, for maximum activity. The Km values for L-malate were 10.9 mM (Leuconostoc mesenteroides B116) and 3 mM (Leuconostoc oenos). The Km values for Mn2+ were 0.1 mM (Leuconostoc mesenteroides B116) and 0.017 mM (Leoconostoc oenos). Malic enzyme oxidatively decarboxylates L-malate to pyruvate. This enzyme consists of a 37 000 subunit that forms dimers and tetramers. The NAD-dependent malic enzyme of Lactobacillus casei decarboxylates oxalacetate and is therefore regarded as a L-malate:NAD+ oxidoreductase (oxalacetate decarboxylating), EC 1.1.1.38. Key words: malolactic enzyme, malic enzyme, Lactobacillus, Leuconostoc.


OENO One ◽  
1988 ◽  
Vol 22 (1) ◽  
pp. 11
Author(s):  
Aline Lonvaud-Funel ◽  
Jean-Philippe Masclef ◽  
Annick Joyeux ◽  
Yiannis Paraskevopoulos

<p style="text-align: justify;">Les interactions entre levures et bactéries lactiques sont déterminées par la nature des souches en présence, leur population et la constitution chimique du moût et du vin. Normalement, pendant la fermentation, les bactéries lactiques sont inhibées par les produits du métabolisme levurien. Mais dans certaines conditions, la croissance précoce des bactéries provoque une chute de la viabilité des levures et, par conséquent, un ralentissement ou un arrêt de la dégradation des sucres. Tous les mécanismes mis en jeu ne sont pas connus.</p><p style="text-align: justify;">+++</p><p style="text-align: justify;">ln wine-making, lactic acid bacteria succeed to yeasts to promote the malolactic fermentation (MLF), after the completion of the alcoholic fermentation. Yeasts are better adapted than bacteria to growth in grape must. So their development easily starts and the alcoholic fermentation triggers soon after the harvest. In the same time, the natural bacterial inoculum decreases, due to an antagonism between these two microorganisms. ln addition to ethanol, fatty acids synthesized by actively growing yeasts exert their toxic effect against lactic acid bacteria. At the end of the alcoholic fermentation, the remaining bacterial population (10<sup>4</sup> to 10<sup>3</sup> cell.p.ml) begins growing. It is mainly constitued by <em>Leuconostoc oenos</em> more resistant than lactobacilli. At that time, autolysis products from decline phase yeasts act as bacterial growth factors. Then, when the bacterial population is large enough (about 10<sup>6</sup> cell.p.ml) MLF happens. So, normally, MLF follows alcoholic fermentation within a few days. But in some conditions, the interactions between yeasts and bacteria do not work in this way. If the weather is particularly hot and dry during the last weeks of the maturation, the pH of the must may be high and generally sulfiting is lowered as there are no rotten grapes. Growing conditions are better than usually for bacteria that, in such a case, compete with yeasts. The bacterial population reach a sufficient level that can actually increase the yeast decline rate. Hydrolase activities of bacteria against yeast cell walls may occur. That leads to a fermentation stuck. These antagonism effects between yeasts and lactic acid bacteria in fermenting must control the wine-making process. Their extent vary with must composition even with both yeast and bacteria strains. Further research is needed to clear up involved machanisms.</p>


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