scholarly journals NoxE NADH Oxidase and the Electron Transport Chain Are Responsible for the Ability of Lactococcus lactis To Decrease the Redox Potential of Milk

2009 ◽  
Vol 76 (5) ◽  
pp. 1311-1319 ◽  
Author(s):  
Sybille Tachon ◽  
Johannes Bernhard Brandsma ◽  
Mireille Yvon
Keyword(s):  
Electron Transport ◽  
Redox Potential ◽  
Lactococcus Lactis ◽  
Growth Phase ◽  
Dairy Products ◽  
Electron Transport Chain ◽  
Anaerobic Conditions ◽  
Transport Chain ◽  
Fermented Dairy Products ◽  
Fermented Dairy

ABSTRACT The redox potential plays a major role in the microbial and sensorial quality of fermented dairy products. The redox potential of milk (around 400 mV) is mainly due to the presence of oxygen and many other oxidizing compounds. Lactococcus lactis has a strong ability to decrease the redox potential of milk to a negative value (−220 mV), but the molecular mechanisms of milk reduction have never been addressed. In this study, we investigated the impact of inactivation of genes encoding NADH oxidases (noxE and ahpF) and components of the electron transport chain (ETC) (menC and noxAB) on the ability of L. lactis to decrease the redox potential of ultrahigh-temperature (UHT) skim milk during growth under aerobic and anaerobic conditions. Our results revealed that elimination of oxygen is required for milk reduction and that NoxE is mainly responsible for the rapid removal of oxygen from milk before the exponential growth phase. The ETC also contributes slightly to oxygen consumption, especially during the stationary growth phase. We also demonstrated that the ETC is responsible for the decrease in the milk redox potential from 300 mV to −220 mV when the oxygen concentration reaches zero or under anaerobic conditions. This suggests that the ETC is responsible for the reduction of oxidizing compounds other than oxygen. Moreover, we found great diversity in the reducing activities of natural L. lactis strains originating from the dairy environment. This diversity allows selection of specific strains that can be used to modulate the redox potential of fermented dairy products to optimize their microbial and sensorial qualities.

Persistence of Escherichia coli O157:H7 in Dairy Fermentation Systems

1998 ◽  
Vol 61 (12) ◽  
pp. 1602-1608 ◽  
Author(s):  
SEAN S. DINEEN ◽  
KAZUE TAKEUCHI ◽  
JANE E. SOUDAH ◽  
KATHRYN J. BOOR
Keyword(s):  
Escherichia Coli ◽  
Lactococcus Lactis ◽  
Dairy Products ◽  
Starter Cultures ◽  
Escherichia Coli O157 ◽  
Potential Health ◽  
E Coli ◽  
Lactococcus Lactis Subsp ◽  
Fermented Dairy Products ◽  
Fermented Dairy

We examined (i) the persistence of Escherichia coli O157:H7 as a postpasteurization contaminant in fermented dairy products; (ii) the ability of E. coli O157:H7 strains with and without the general stress regulatory protein, RpoS, to compete with commercial starter cultures in fermentation systems; and (iii) the survival of E. coli O157:H7 in the yogurt production process. In commercial products inoculated with 103 CFU/ml, E. coli O157:H7 was recovered for up to 12 days in yogurt (pH 4.0), 28 days in sour cream (pH 4.3), and at levels >102 CFU/ml at 35 days in buttermilk (pH 4.1). For the starter culture competition trials, the relative inhibition of E. coli O157:H7 in the experimental fermentation systems was, in decreasing order, thermophilic culture mixture, Lactobacillus delbrueckii subsp. bulgaricus R110 alone, Lactococcus lactis subsp. lactis D280 alone, Lactococcus lactis subsp. cremoris D62 alone, and Streptococcus thermophilus C90 alone showing the least inhibition. Recovery of the rpoS mutant was lower than recovery of its wild-type parent by 72 h or earlier in the presence of individual starter cultures. No E. coli O157:H7 were recovered after the curd formation step in yogurt manufactured with milk inoculated with 105 CFU/ml. Our results show that (i) postprocessing entry of E. coli O157:H7 into fermented dairy products represents a potential health hazard; (ii) commercial starter cultures differ in their ability to reduce E. coli O157:H7 CFU numbers in fermentation systems; and (iii) the RpoS protein appears to most effectively contribute to bacterial survival in the presence of conditions that are moderately lethal to the cell.

scholarly journals Experimental conditions affect the site of tetrazolium violet reduction in the electron transport chain of Lactococcus lactis

Microbiology ◽  
2009 ◽  
Vol 155 (9) ◽  
pp. 2941-2948 ◽  
Author(s):  
Sybille Tachon ◽  
Damien Michelon ◽  
Emilie Chambellon ◽  
Monique Cantonnet ◽  
Christine Mezange ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Electron Transport ◽  
Lactococcus Lactis ◽  
Electron Transport Chain ◽  
Experimental Conditions ◽  
Plate Test ◽  
Tetrazolium Salts ◽  
Transport Chain ◽  
Reduction Mechanisms ◽  
Tetrazolium Violet

The reduction of tetrazolium salts to coloured formazans is often used as an indicator of cell metabolism during microbiology studies, although the reduction mechanisms have never clearly been established in bacteria. The objective of the present study was to identify the reduction mechanisms of tetrazolium violet (TV) in Lactococcus lactis using a mutagenesis approach, under two experimental conditions generally applied in microbiology: a plate test with growing cells, and a liquid test with non-growing (resting) cells. The results showed that in both tests, TV reduction resulted from electron transfer from an intracellular donor (mainly NADH) to TV via the electron transport chain (ETC), but the reduction sites in the ETC depended on experimental conditions. Using the plate test, menaquinones were essential for TV reduction and membrane NADH dehydrogenases (NoxA and/or NoxB) were partly involved in electron transfer to menaquinones. In this case, TV reduction mainly occurred outside the cells and in the outer part of the plasma membrane. During the liquid test, TV was directly reduced by NoxA and/or NoxB, probably in the inner part of the membrane, where NoxA and NoxB are localized. In this case, reduction was directly related to the intracellular NADH pool. Based on these findings, new applications for TV tests are proposed, such as NADH pool determination with the liquid test and the screening of mutants affected in menaquinone biosynthesis with the plate test. Preliminary results using other tetrazolium salts in the plate test showed that the reduction sites depended on the salt, suggesting that similar studies should be carried out with other tetrazolium salts so that the outcome of each test can be interpreted correctly.

scholarly journals The microbial metabolism of C1 compounds. The electron-transport chain of Pseudomonas AM1

1975 ◽  
Vol 152 (2) ◽  
pp. 349-356 ◽  
Author(s):  
David Widdowson ◽  
Christopher Anthony
Keyword(s):  
Electron Transport ◽  
Cytochrome C ◽  
Redox Potential ◽  
Molecular Oxygen ◽  
Cytochrome B ◽  
Electron Transport Chain ◽  
Difference Spectrum ◽  
Reduced Form ◽  
Transport Chain ◽  
Oxidation By Molecular Oxygen

Pseudomonas AM1, Hyphomicrobium X and Pseudomonas MS all contain cytochrome a/a3 and a b-type cytochrome able to react with CO. Pseudomonas AM1 and Hyphomicrobium X also have a CO-binding cytochrome c. The purified cytochrome c (redox potential 0.26V) of Pseudomonas AM1 was not susceptible to oxidation by molecular oxygen. CO reacted slowly with the reduced form giving a CO difference spectrum with a peak at 412nm and troughs at 420nm and 550nm. Similar results were obtained with the cytochrome c of Hyphomicrobium (aerobically grown or anaerobically grown with nitrate) and with that of Pseudomonas extorquens. The results given in the present paper are incompatible with an oxygenase or oxidase function for the soluble cytochrome c of methylotrophs. Studies with whole cells of Pseudomonas AM1 and a cytochrome c-deficient mutant have demonstrated that cytochrome b (redox potential 0.009V) is the first cytochrome in the electron-transport chain for oxidation of all substrates except methanol (and ethanol) whose oxidation does not involve this cytochrome. All substrates are usually oxidized by way of cytochrome c and cytochrome oxidase (cytochrome a/a3), but there is an alternative route for the reduction of cytochrome a/a3 in the mutant lacking cytochrome c. Results of experiments on cyanide inhibition of respiration and cytochrome oxidation support the suggestion that the susceptibility of cytochrome b to oxidation by molecular oxygen (reflected in its ability to react with CO) is probably irrelevant to the normal physiology of Pseudomonas AM1.

scholarly journals Alternative splicing of coq-2 controls the levels of rhodoquinone in animals

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
June H Tan ◽  
Margot Lautens ◽  
Laura Romanelli-Cedrez ◽  
Jianbin Wang ◽  
Michael R Schertzberg ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Caenorhabditis Elegans ◽  
Electron Transport ◽  
Electron Transport Chain ◽  
Substrate Selection ◽  
Anaerobic Conditions ◽  
Parasitic Helminths ◽  
Transport Chain ◽  
Splice Forms ◽  
Electron Carriers

Parasitic helminths use two benzoquinones as electron carriers in the electron transport chain. In normoxia, they use ubiquinone (UQ), but in anaerobic conditions inside the host, they require rhodoquinone (RQ) and greatly increase RQ levels. We previously showed the switch from UQ to RQ synthesis is driven by a change of substrates by the polyprenyltransferase COQ-2 (Del Borrello et al., 2019; Roberts Buceta et al., 2019); however, the mechanism of substrate selection is not known. Here, we show helminths synthesize two coq-2 splice forms, coq-2a and coq-2e, and the coq-2e-specific exon is only found in species that synthesize RQ. We show that in Caenorhabditis elegans COQ-2e is required for efficient RQ synthesis and survival in cyanide. Importantly, parasites switch from COQ-2a to COQ-2e as they transit into anaerobic environments. We conclude helminths switch from UQ to RQ synthesis principally via changes in the alternative splicing of coq-2.

scholarly journals Draft Genome Sequences of Four Lactococcus lactis Strains Isolated from Diverse Niches, Including Dairy Products, Grass, and Green Peas

2019 ◽  
Vol 8 (35) ◽  
Author(s):  
Desirée Roman Naranjo ◽  
Michael Callanan ◽  
Olivia McAuliffe
Keyword(s):  
Lactococcus Lactis ◽  
Dairy Products ◽  
Draft Genome ◽  
Genome Sequences ◽  
Content Type ◽  
Fermented Dairy Products ◽  
Fermented Dairy ◽  
Green Peas

Lactococcus lactis has been used for millennia as a starter organism in the production of many fermented dairy products. This announcement includes the draft genome sequences of four strains of Lactococcus lactis, two of dairy origin and two from nondairy sources.

scholarly journals Activation of δ-aminolaevulate synthetase in extracts of Rhodopseudomonas spheroides

1970 ◽  
Vol 117 (3) ◽  
pp. 609-613 ◽  
Author(s):  
J. Marriott ◽  
A. Neuberger ◽  
G. H. Tait
Keyword(s):  
Electron Transport ◽  
Carboxylic Acids ◽  
Electron Transport Chain ◽  
Normal Rate ◽  
Inhibitory Effects ◽  
Anaerobic Conditions ◽  
Photo Oxidation ◽  
Transport Chain ◽  
Endogenous Compound ◽  
Rhodopseudomonas Spheroides

1. The spontaneous activation of δ-aminolaevulate synthetase in extracts from Rhodopseudomonas spheroides grown semi-anaerobically in the light requires oxygen and does not take place anaerobically in the dark. 2. Activation is completely prevented by azide or cyanide and is partially inhibited by chlorpromazine. These compounds inhibit markedly the succinoxidase activity of extracts. 3. NADH delays activation, but when it has been oxidized by the extract activation begins at the normal rate and complete activation occurs. By contrast both the rate and the extent of activation are markedly decreased by even small amounts of carboxylic acids. 4. The inhibitory effects of succinate and citrate on activation can be prevented by malonate and fluorocitrate respectively. 5. These results suggest that for activation to occur some endogenous compound has to be oxidized via the electron transport chain. 6. Activation occurs under anaerobic conditions in the light, probably by photo-oxidation.

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