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PubMed2005

Trace analysis of bromate, chlorate, iodate, and perchlorate in natural and bottled waters.

A simple and rapid method has been developed to simultaneously measure sub-microg/L quantities of the oxyhalide anions bromate, chlorate, iodate, and perchlorate in water samples. Water samples (10 mL) are passed through barium and hydronium cartridges to remove sulfate and carbonate, respectively. The method utilizes the direct injection of 10 microL volumes of water samples into a liquid chromatography-tandem triple-quadrupole mass spectrometry (LC-MS/MS) system. Ionization is accomplished using electrospray ionization in negative mode. The method detection limits were 0.021 microg/L for perchlorate, 0.045 microg/L for bromate, 0.070 microg/L for iodate, and 0.045 microg/L for chlorate anions in water. The LC-MS/MS method described here was compared to established EPA methods 300.1 and 317.1 for bromate analysis and EPA method 314.0 for perchlorate analysis. Samples collected from sites with known contamination were split and sent to certified laboratories utilizing EPA methods for bromate and perchlorate analysis. At concentrations above the reporting limits for EPA methods, the method described here was always within 20% of the established methods, and generally within 10%. Twenty-one commercially available bottled waters were analyzed for oxyhalides. The majority of bottled waters contained detectable levels of oxyhalides, with perchlorate < or = 0.74 microg/L, bromate < or = 76 microg/L, iodate < or = 25 microg/ L, and chlorate < or = 5.8 microg/L. Perchlorate, iodate, and chlorate were detectable in nearly all natural waters tested, while bromate was only detected in treated waters. Perchlorate was found in several rivers and reservoirs where itwas not found previously using EPA 314.0 (reporting limit of 4 microg/L). This method was also applied to common detergents used for cleaning laboratory glassware and equipmentto evaluate the potential for sample contamination. Only chlorate appeared as a major oxyhalide in the detergents evaluated, with concentrations up to 517 microg/g. Drinking water treatment plants were also evaluated using this method. Significant formations of chlorate and bromate are demonstrated from hypochlorite generation and ozonation. From the limited data set provided here, it appears that perchlorate is a ubiquitous contaminant of natural waters at trace levels.

Bromates↗
PubMed2004

Effects of sodium chlorate on antibiotic resistance in Escherichia coli O157:H7.

The spread of antibiotic resistance from farm animals to human pathogens has become a matter of great public health significance, and methods to reduce foodborne pathogenic bacteria without utilizing traditional antibiotics have been sought. Chlorate kills Escherichia coli O157:H7 in vitro and in vivo and has been proposed as a feed additive to be included in food animal rations immediately prior to slaughter to reduce E. coli O157:H7 populations in the animal gastrointestinal tract. This study was designed to examine the effect that the development of chlorate resistance in E. coli O157:H7 has on resistance to 32 medically important antibiotics. Chlorate resistance numerically increased antibiotic resistance in E. coli O157:H7 strain 6058 and strain 933 to six and four antibiotics, respectively, but chlorate resistance affected resistance to only two antibiotics (cefoxotin and sulfadimethoxine) in both strains examined. Based on the fact that chlorate resistant mutants do not appear to compete well in vivo and based on the results of the current study, it appears unlikely that chlorate treatment will result in a dissemination of antibiotic resistance. However, further research is needed to confirm these results.

Animals↗
PubMed2006

Interference of chlorate and chlorite with nitrate reduction in resting cells of Paracoccus denitrificans.

When grown anaerobically on a succinate+nitrate (SN) medium, Paracoccus denitrificans forms the membrane-bound, cytoplasmically oriented, chlorate-reducing nitrate reductase Nar, while the periplasmic enzyme Nap is expressed during aerobic growth on butyrate+oxygen (BO) medium. Preincubation of SN cells with chlorate produced a concentration-dependent decrease in nitrate utilization, which could be ascribed to Nar inactivation. Toluenization rendered Nar less sensitive to chlorate, but more sensitive to chlorite, suggesting that the latter compound may be the true inactivator. The Nap enzyme of BO cells was inactivated by both chlorate and chlorite at concentrations that were at least two orders of magnitude lower than those shown to affect Nar. Partial purification of Nap resulted in insensitivity to chlorate and diminished sensitivity to chlorite. Azide was specific for SN cells in protecting nitrate reductase against chlorate attack, the protective effect of nitrate being more pronounced in BO cells. The results are discussed in terms of different metabolic activation of chlorine oxoanions in both types of cells, and limited permeation of chlorite across the cell membrane.

Chlorates↗
PubMed2003

A gene cluster for chlorate metabolism in Ideonella dechloratans.

Chlorate reductase has been isolated from the chlorate-respiring bacterium Ideonella dechloratans, and the genes encoding the enzyme have been sequenced. The enzyme is composed of three different subunits and contains molybdopterin, iron, probably in iron-sulfur clusters, and heme b. The genes (clr) encoding chlorate reductase are arranged as clrABDC, where clrA, clrB, and clrC encode the subunits and clrD encodes a specific chaperone. Judging from the subunit composition, cofactor content, and sequence comparisons, chlorate reductase belongs to class II of the dimethyl sulfoxide reductase family. The clr genes are preceded by a novel insertion sequence (transposase gene surrounded by inverted repeats), denoted ISIde1. Further upstream, we find the previously characterized gene for chlorite dismutase (cld), oriented in the opposite direction. Chlorate metabolism in I. dechloratans starts with the reduction of chlorate, which is followed by the decomposition of the resulting chlorite to chloride and molecular oxygen. The present work reveals that the genes encoding the enzymes catalyzing both these reactions are in close proximity.

Amino Acid Sequence↗
PubMed2000

Bactericidal effect of sodium chlorate on Escherichia coli O157:H7 and Salmonella typhimurium DT104 in rumen contents in vitro.

Escherichia coli O157:H7 and Salmonella Typhimurium DT104 are important foodborne pathogens affecting the beef and dairy industries and strategies are sought to rid these organisms from cattle at slaughter. Both pathogens possess respiratory nitrate reductase that also reduces chlorate to the lethal chlorite ion. Because most anaerobes lack respiratory nitrate reductase, we hypothesized that chlorate may selectively kill E. coli O157:H7 and Salmonella Typhimurium DT104 but not potentially beneficial anaerobes. In support of this hypothesis, we found that concentrations of E. coli O157:H7 and Salmonella Typhimurium DT104 were reduced from approximately 1,000,000 colony forming units (CFU) to below our level of detection (< or = 10 CFU) following in vitro incubation (24 h) in buffered ruminal contents (pH 6.8) containing 5 mM added chlorate. In contrast, chlorate had little effect on the most probable number (mean +/- SD) of total culturable anaerobes (ranging from 9.9 +/- 0.72 to 10.7 +/- 0.01 log10 cells/ml). Thus, chlorate was bactericidal to E. coli O157:H7 and Salmonella Typhimurium DT104 but not to potentially beneficial bacteria. The bactericidal effect of chlorate was concentration dependent (less at 1.25 mM) and markedly affected by pH (more bactericidal at pH 6.8 than pH 5.6).

Animals↗
PubMed2003

Escherichia coli O157:H7 populations in sheep can be reduced by chlorate supplementation.

Ruminant animals are a natural reservoir of the foodborne pathogen Escherichia coli O157:H7. Some foodborne pathogens (e.g., E. coli) are equipped with a nitrate reductase that cometabolically reduces chlorate. The intracellular reduction of chlorate to chlorite kills nitrate reductase-positive bacteria; however, species that do not reduce nitrate are not affected by chlorate. Therefore, it has been suggested that ruminants be supplemented with chlorate prior to shipment for slaughter in order to reduce foodborne illnesses in human consumers. Sheep (n = 14) were fed a high-grain ration and were experimentally infected with E. coli O157:H7. These sheep were given an experimental product (XCP) containing the equivalent of either 2.5 mM NaNO3 and 100 mM NaCl (control sheep; n = 7) or 2.5 mM NaNO3 and 100 mM NaClO3 (chlorate [XCP]-treated sheep; n = 7). Control and XCP-treated sheep were treated for 24 h; XCP treatment reduced the population of inoculated E. coli O157:H7 (P < 0.05) from 10(2), 10(5), and 10(5) CFU/g in the rumen, cecum, and rectum, respectively, to < 10(1) CFU/g in all three sections of the gastrointestinal tract. The number of sheep testing positive for E. coli O157:H7 was significantly reduced by XCP treatment. In a similar fashion, total E. coli and coliforms were also reduced (P < 0.05) in all three compartments of the intestinal tract. Intestinal pH, total volatile fatty acid production, and the acetate/propionate ratio were unaffected by XCP treatment. On the basis of these results, it appears that chlorate treatment can be an effective method for the reduction of E. coli O157:H7 populations in ruminant animals immediately prior to slaughter.

Animals↗
PubMedDate not supplied

Sodium chlorate induces undersulfation of cellular proteoglycans and increases in FSH-stimulated estradiol production in immature rat Sertoli cells.

The functional influence of cell proteoglycan (PG) undersulfation on estradiol synthesis by immature rat Sertoli cell cultures was investigated by using sodium chlorate, an inhibitor of the active sulfate donor for sulfotransferases. The addition of sodium chlorate to 20-day-old rat Sertoli cell cultures abolished [35S]-sulfate incorporation into neosynthesized PG and consequently reduced the residence time of undersulfated PG in cell membrane. Simultaneously, follicle-stimulating hormone (FSH)-stimulated estradiol synthesis was increased by 45%. The effects of sodium chlorate upon Sertoli cell PG synthesis and steroidogenesis were not reproduced with the addition of sodium chloride. Addition of phosphodiesterase inhibitors (MIX or Ro20-1724) decreased the magnitude of the chlorate effect on FSH-stimulated steroidogenesis, suggesting that part of chlorate's effect on steroidogenesis resulted from a decrease in adenosine cyclic 3',5'-phosphate (cAMP)-specific phosphodiesterase activity. Additionally, chlorate 1) increased Sertoli cell steroidogenesis at a step located beyond cAMP (restricted to Sertoli cell cultures exhibiting moderate steroidogenic response to (Bu)2cAMP) and 2) abolished the inhibition of steroidogenesis induced by transforming growth factor-beta. These results support our previous data, which showed that alteration in PG synthesis and the consequent decrease in cell membrane PG content induce an increase in FSH-stimulated estradiol synthesis in Sertoli cell cultures. The identification of cAMP-specific phosphodiesterase activity as a signal transduction step modified by PG undersulfation suggests the possible involvement of cell PG in the regulation of phosphodiesterase activity and, therefore, of FSH responsiveness during testicular development.

Animals↗
PubMed1988

Influence of chlorate on proteoglycan biosynthesis by cultured human fibroblasts.

The influence of chlorate, an inhibitor of sulfate adenylyltransferase, on biosynthesis and secretion of proteoglycans was investigated in cultured human skin fibroblasts. At up to 10 mM concentrations, chlorate caused a reduction of [35S]sulfate incorporation into small chondroitin sulfate/dermatan sulfate proteoglycan by up to 96%. Incorporation of [3H]leucine and [3H] glucosamine was only slightly affected. No influence was seen on the polymerization degree of the polysaccharide chain as judged by gel filtration, and on the kinetics of secretion of the proteoglycan. Concomitant with reduced sulfation, however, was an increased sensitivity toward chondroitin AC lyase which suggests a diminished epimerization of D-glucuronic acid to L-iduronic acid residues. Agarose gel electrophoresis revealed that all polysaccharide chains of control chondroitin sulfate/dermatan sulfate proteoglycan exhibited a similar sulfation degree. Chlorate treatment led to the formation of polysaccharide chains of widely varying degree of sulfation, but fully sulfated chains were synthesized even in the presence of 3 mM chlorate, and sulfate-free chondroitin was not detected. Studying the effects of chlorate treatment on the synthesis of other proteoglycan types it was found that, in cell-associated galactosaminoglycans, 6-sulfation of N-acetylgalactosamine residues was less affected than was 4-sulfation. In case of heparan sulfate the synthesis of sulfamate groups was less impaired than sulfate ester formation. Nitrous acid degradation at pH 4.1 indicated the presence of unsubstituted amino groups. Chlorate treatment may be considered as a means for the production of proteoglycans with defined structural alterations.

Adult↗
PubMed1994

Chlorate-induced inhibition of tyrosine sulfation on bone sialoprotein synthesized by a rat osteoblast-like cell line (UMR 106-01 BSP).

Bone sialoprotein (BSP) is a major noncollagenous, RGD-containing glycoprotein found in the extracellular matrix of bone. The RGD sequence is flanked by two tyrosine-rich regions, which fit the established consensus requirements for tyrosine sulfation. Tyrosine sulfation is suggested to be important in the regulation of protein secretion and function. The role of this post-translational modification on the cell attachment activity and secretion of a highly sulfated form of BSP isolated from a rat osteoblast-like cell line (UMR 106-01 BSP) was investigated by inhibiting sulfation with chlorate. [35S]Sulfate, [3H]glucosamine, and [3H]tyrosine were used as metabolic precursors to monitor biosynthetic products. Chlorate was effective in inhibiting total [35S]sulfate incorporation by 90% without altering overall protein synthesis and secretion in cultures up to 72 h under serum-free conditions. Isolated proteoglycans and purified BSP were analyzed for sulfate incorporation. Proteoglycans isolated from the medium of cells treated with chlorate displayed a difference in the hydrodynamic properties of the molecules as compared with control cultures. An increase in the specific activity of proteoglycans labeled with [3H]glucosamine isolated from chlorate-treated cells was also observed suggesting a change in hexosamine metabolism induced by chlorate. BSP purified from the medium of chlorate-treated cells contained approximately 7% of the 35S incorporation as compared with nontreated control cultures. Quantification of sulfate incorporation into glycoconjugates versus tyrosine sulfate of BSP indicates that the amount of sulfate associated with N- and O-linked oligosaccharides was reduced by approximately 97%, while that on tyrosine residues was reduced by approximately 90%. Using normal human bone cells, the cell attachment activity of the reduced sulfate form of BSP was nearly equivalent to that of the fully sulfated product.

Animals↗
PubMed1988

The Kinetics of Chlorate Uptake by XD Tobacco Cells.

The uptake of [(36)Cl]chlorate by the 14U variant of the XD cell line of Nicotiana tobaccum L. cv Xanthi was investigated to examine the use of chlorate as a nitrate analog in transport studies. The kinetics of chlorate uptake against concentration was complex. Evidence was obtained, e.g., by means of nitrate competition, that these kinetics could be resolved into two components indicating the existence of two influx mechanisms: a saturable high affinity transport system (HATS) and a low affinity transport system (LATS) that showed first order kinetics. HATS has an apparent K(m) for chlorate of 0.3 millimolar, and a marked pH dependence. The V(max) dropped about fivefold as the pH was changed from the optimum pH (5.5-6.5), while the K(m) remained virtually unchanged. The activity of HATS was completely inhibited by 15 millimolar nitrate and was less sensitive to chloride. LATS was inhibited by chloride and showed some inhibition by nitrate. It was concluded that [(36)Cl]chlorate can be used as an analog for nitrate uptake studies only in a limited low concentration range where HATS is the main route for chlorate influx.

Journal Article↗
PubMed1990

Genetic analysis of Aspergillus niger: isolation of chlorate resistance mutants, their use in mitotic mapping and evidence for an eighth linkage group.

This paper describes the use of chlorate resistant mutants in genetic analysis of Aspergillus niger. The isolated mutants could be divided into three phenotypic classes on the basis of nitrogen utilization. These were designated nia, nir and cnx as for Aspergillus nidulans. All mutations were recessive to their wild-type allele in heterokaryons as well as in heterozygous diploids. The mutations belong to nine different complementation groups. In addition a complex overlapping complementation group was found. Evidence for the existence of eight linkage groups was obtained. Two linked chlorate resistance mutations and two tryptophan auxotrophic markers, which were unlinked to any of the known markers, form linkage group VIII. We used the chlorate resistance mutations as genetic markers for the improvement of the mitotic linkage map of A. niger. We determined the linear order of three markers in linkage group VI as well as the position of the centromere by means of direct selection of homozygous cnxA1 recombinants. In heterozygous diploid cultures diploid chlorate resistant segregants appeared among conidiospores with a frequency of 3.9 x 10(-5) (cnxG13 in linkage group I) to 2.1 x 10(-2) (cnxD6 in linkage group III). The mean frequency of haploid chlorate resistant segregants was 1.3 x 10(-3). The niaD1 and niaD2 mutations were also complemented by transformation with the A. niger niaD+ gene cloned by Unkles et al. (1989). Mitotic stability of ten Nia+ transformants was determined. Two distinct stability classes were found, showing revertant frequencies of 5.0 x 10(-3) and 2.0 x 10(-5) respectively.

Aspergillus niger↗
PubMed2007

Zoonotic bacterial populations, gut fermentation characteristics and methane production in feedlot steers during oral nitroethane treatment and after the feeding of an experimental chlorate product.

Nitroethane inhibits the growth of certain zoonotic pathogens such as Campylobacter and Salmonella spp., foodborne pathogens estimated to cause millions of human infections each year, and enhances the Salmonella- and Escherichia coli-killing effect of an experimental chlorate product being developed as a feed additive to kill these bacteria immediately pre-harvest. Limited studies have shown that nitroethane inhibits ruminal methane production, which represents a loss of 2-12% of the host's gross energy intake and contributes to global warming and destruction of the ozone layer. The present study was conducted to assess the effects of 14-day oral nitroethane administration, 0 (0X), 80 (1X) or 160 (2X)mg nitroethane/kg body weight per day on ruminal and fecal E. coli and Campylobacter, ruminal and fecal methane-producing and nitroethane-reducing activity, whole animal methane emissions, and ruminal and fecal fermentation balance in Holstein steers (n=6 per treatment) averaging 403+/-26 (SD) kg BW. An experimental chlorate product was fed the day following the last nitroethane administration to determine effects on E. coli and Campylobacter. The experimental chlorate product decreased (P<0.001) fecal, but not ruminal (P>0.05) E. coli concentrations by 1000- and 10-fold by 24 and 48 h, respectively, after chlorate feeding when compared to pre-treatment concentrations (>5.7 log(10) colony forming units/g). No effects (P>0.05) of nitroethane or the experimental chlorate product were observed on fecal Campylobacter concentrations; Campylobacter were not recovered from ruminal contents. Nitroethane treatment decreased (P<0.01) ruminal (8.46, 7.91 and 4.74+/-0.78 micromol/g/h) and fecal (3.90, 1.36 and 1.38+/-0.50 micromol/g/h) methane-producing activity for treatments 0X, 1X and 2X, respectively. Administration of nitroethane increased (P<0.001) nitroethane-reducing activity in ruminal, but not fecal samples. Day of study affected ruminal (P<0.0001) but not fecal (P>0.05) methane-producing and nitroethane-reducing activities (P<0.01); treatment by day interactions were not observed (P>0.05). Ruminal accumulations of acetate decreased (P<0.05) in 2X-treated steers when compared with 0X- and 1X-treated steers, but no effect (P>0.05) of nitroethane was observed on propionate, butyrate or the acetate to propionate ratio. Whole animal methane emissions, expressed as L/day or as a proportion of gross energy intake (%GEI), were unaffected by nitroethane treatment (P>0.05), and were not correlated (P>0.05) with ruminal methane-producing activity. These results demonstrate that oral nitroethane administration reduces ruminal methane-producing activity but suggest that a microbial adaptation, likely due to an in situ enrichment of ruminal nitroethane-reducing bacteria, may cause depletion of nitroethane, at least at the 1X administration dose, to concentrations too low to be effective. Further research is warranted to determine if the optimization of dosage of nitroethane or related nitrocompouds can maintain the enteropathogen control and anti-methanogen effect in fed steers.

Administration, Oral↗
PubMed2004

Kinetics and mechanism of chloride based chlorine dioxide generation process from acidic sodium chlorate.

The reaction between sodium chlorate and sodium chloride in presence of aqueous sulfuric acid is studied in a well stirred reactor at various temperatures and molar concentrations of chlorate, chloride and acid. The reaction rate is evaluated by analyzing the consumption of chlorate or chloride iodometrically or argentometrically. The rate law is established. Reaction has been found first and second order with respect to chlorate and chloride concentration, respectively. Reaction order is found about 13-14 with respect to molar concentration of sulfuric acid but it reduced to 2.4 when acidity function, h_, is substituted in place of molar concentration. The temperature dependence of the reaction is also investigated and pre-exponential Arrhenius parameter as well as activation energy are determined. It has been observed that ClO(2)/Cl(2) ratio is markedly affected by chlorate to chloride ratio. Reaction mechanism compatible with the reaction kinetics is proposed.

Chemical Industry↗
PubMed2006

RAPD cluster analysis and chlorate sensitivity of some Indian isolates of Macrophomina phaseolina from sorghum and their relationships with pathogenicity.

Charcoal rot caused by Macrophomina phaseolina is an economically important disease in sorghum grown during the post rainy season in India. Variations in random amplified polymorphic DNA (RAPD) polymorphisms, chlorate sensitivity and pathogenicity were studied among sorghum isolates of M. phaseolina collected from different parts of India. RAPD data based on 14 random primers of Kit A and C (OPA and OPC) on 20 isolates showed a high degree of polymorphism (98.1%) in different isolates. UPGMA dendrogram on RAPD data produced 7 clusters at the level of 37% similarity. Isolates from the same locations showed a tendency to group closer, substantiating closer genetic relatedness. Sorghum infecting Macrophomina isolates showed a mixed response for sensitivity to potassium chlorate (120 mM). Chlorate-resistant isolates were predominant (>65% of the isolates) over sensitive isolates. Chlorate-sensitive isolates were found to be genetically closer among them than the resistant ones. For the first time it was shown that chlorate sensitivity in Macrophomina had some relations with charcoal rot severity in sorghum.

Ascomycota↗
PubMed1986

Chlorate--a potent inhibitor of protein sulfation in intact cells.

Chlorate is known to be an in vitro inhibitor of ATP-sulfurylase, the first enzyme in the biosynthesis of PAPS which is the ubiquitous co-substrate for sulfation. Here, the effect of chlorate on protein sulfation in intact cells was investigated. Treatment of various cell cultures with 1 mM sodium chlorate in a medium low in sulfate and sulfur-containing amino acids resulted in an inhibition of protein sulfation greater than 95%. Tyrosine as well as carbohydrate sulfation was blocked. Chlorate did not inhibit protein synthesis and did not exhibit any other toxic effects, even after prolonged treatment of cell cultures. Thus, chlorate treatment provides a powerful tool for studying the biological significance of protein sulfation.

Animals↗
PubMed1999

Determination of chlorate at low microgram/l levels by ion-chromatography with postcolumn reaction.

A new method for the determination of low concentrations of chlorate in natural waters is described. Chlorate is analyzed by ion-chromatography followed by an osmate-catalyzed postcolumn reaction of chlorate with iodide and UV-detection of triiodide. The new osmate catalysis allows to carry out the oxidation of iodide by chlorate at pH 3 instead of 6 M HCl for the uncatalyzed reaction. A detection limit of 5 nM (0.4 microgram/l) chlorate is achieved. The method also allows the simultaneous determination of chlorite, bromate, and nitrite at the low microgram/l level.

Calibration↗
PubMed1989

Modulation of cell surface heparan sulfate structure by growth of cells in the presence of chlorate.

Swiss mouse 3T3 cells, when grown in the presence of 5 mM chlorate, an inhibitor of PAPS synthesis, produce heparan sulfate glycosaminoglycan chains containing only about 8% of the sulfate normally present and which have lost the ability to bind to fibronectin. These undersulfated chains are sensitive to nitrous acid at pH 4.5, indicating that many glucosaminyl residues have unsubstituted amino groups. The iduronic acid content of the heparan sulfate produced in the presence of chlorate is reduced to less than 7% as compared to the 36% in that from untreated cells. The chlorate-treated cells do not demonstrate any alterations in their growth control. However, the spreading behavior of these cells is altered to a flat rounded morphology compared to the more typical fibroblastic appearance of the untreated cell. The sulfation of chondroitin chains is also inhibited, but at a lower chlorate concentration which does not alter growth control or the spreading ability of the cells. These data indicate that (a) 3T3 cell surface heparan sulfate proteoglycan is not involved in growth control but may be involved in cell spreading, (b) the use of chlorate should be a valuable method for the study of the biosynthesis and structure/function relationships of sulfated glycosaminoglycans, and (c) the temporal sequence of the heparan sulfate chain modification reactions predicted from results of studies with cell-free extracts also operates in the cell.

Animals↗
PubMed2005

Novel preharvest strategies involving the use of experimental chlorate preparations and nitro-based compounds to prevent colonization of food-producing animals by foodborne pathogens.

Foodborne diseases caused by enterohemorrhagic Escherichia coli, Salmonella, and Campylobacter species are of public health and economic significance. Shedding of these pathogens during production and slaughter are risks for contamination of products for human consumption. Consequently, strategies are sought to prevent or reduce the carriage of these pathogens in food animals before slaughter. Experimental products containing chlorate salts have been proven efficacious in reducing concentrations of E. coli and Salmonella Typhimurium in the gut of cattle, sheep, swine, and poultry when administered as feed or water additives. Mechanistically, chlorate selectively targets bacteria expressing respiratory nitrate reductase activity, such as most members of the family Enterobacteriaceae, as this enzyme catalyzes the reduction of chlorate to lethal chlorite. Most beneficial gut bacteria lack respiratory nitrate reductase activity, and thus the technology appears compatible with many bacteria exhibiting competitive exclusion capabilities. More recently, select nitrocompounds have been investigated as potential feed additives, and although these nitrocompounds significantly reduce pathogens on their own, evidence indicates that they may most effectively be used to complement the bactericidal activity of chlorate. A particularly attractive aspect of the nitrocompound technology is that, as potent inhibitors of ruminal methanogenesis, they may allow producers the opportunity to recoup costs associated with their use. At present, neither chlorate nor the nitrocompounds have been approved as feed additives by the US Food and Drug Administration, and consequently they are not yet available for commercial use.

Animal Feed↗