sodium-acetate--anhydrous and propionic-acid

Numerous factors have the potential to affect the amount of forage or pasture eaten by ruminant animals, including gut capacity, ability of tissues to metabolize nutrients, ruminal acidity, and osmolality. Much research into the control of food intake has tested one particular theory, often by applying greater degrees of stimulation than occur naturally, and is then unable to explain how physiological changes in that stimulus can be responsible for controlling intake. We have found that the effects of two or three stimuli (sodium acetate, sodium propionate, ruminal distension) applied together were additive. As to the site of this integration, receptors in the rumen wall are sensitive to both mechanical stimulation and acids, with transmission of impulses in vagal afferent fibers probably modulated by the osmolality of ruminal fluid. Thus, a certain degree of integration ("polymodal") is likely to have occurred at the level of the transceiving organ. A second level of integration is "polytopic." In this level stimulation of one visceral site modifies the effects of the same type of stimulus at another site. A third level of integration occurs in the central nervous system, whereby the effects of visceral stimulation might be balanced with signals from other stimuli (e.g., the special senses) to determine whether feeding should take place at any given moment. The thesis presented is that the central nervous system receives a nonspecific signal from the viscera; the animal might then learn to eat that amount of food that minimizes the competing discomforts of excessive abdominal visceral stimulation and shortage or imbalance of nutrients.

Topics: Animals; Central Nervous System; Eating; Models, Biological; Propionates; Rumen; Ruminants; Sodium Acetate

The neutralization effects of 0.1M NaHCO(3), KPO(4)-buffer (pH 7.0) and sodium acetate (NaOAc) solutions (500 ml/kg food waste/day) on controlling the pH and leachate quality in an acidogenic reactor of food waste anaerobic digestion was investigated. pH of leachate from the reactor was low and ranged from 3.24 to 4.15. Although differences in chemical oxygen demand (COD) were observed, the cumulative COD yields were almost similar. Ammonia concentrations gradually decreased from 26 to 3mg/l after 15 days. Acetic acid was the major fraction and the total VFAs decreased gradually for a week and increased thereafter, with a sharp increase in NaOAc treatment. VFAs yield and acetate/propionate ratio were the highest in NaOAc treatment, followed by NaHCO(3) and KPO(4) treatments. Volatile solids reduction was the lowest in NaOAc treatment (47.5%) and highest in NaHCO(3) treatment (67.0%). With lower decomposition and higher yield of VFA and COD, NaOAc could be used as a neutralizing agent in acidogenic reactors to improve the efficiency of the acidogenesis process.

Topics: Acetates; Acetic Acid; Ammonia; Bioreactors; Buffers; Equipment Design; Fatty Acids, Volatile; Food; Hydrogen-Ion Concentration; Hydrolysis; Nitrogen; Oxygen; Propionates; Refuse Disposal; Sodium Acetate

Histone deacetylases (HDACs) are important enzymes for the transcriptional regulation of gene expression in eukaryotic cells. Deacetylation of epsilon-acetyl-lysine residues within the N-terminal tail of core histones mediates changes in both histone-DNA and histone-non-histone protein interactions. However, surprisingly little is known about the substrate specificities of different HDACs. Here, we use the epsilon-acyl moieties of epsilon-modified l-lysine in peptidic substrates as a probe to examine the active site cavity of HDACs and HDAC-like enzymes. Measurements were based on a fluorogenic assay with small synthetic substrates. Four different enzyme preparations were used derived from rat, human, and bacterial sources. None of the enzymes was able to utilize substrates with epsilon-acyl moieties larger than acetyl, except rat liver HDAC, which was the only enzyme to convert a substrate containing epsilon-propionyl-l-lysine. All enzymes exhibited a distinct enantioselectivity toward l-lysine-containing substrates except FB188 HDAH which also deacetylated Boc-d-Lys(epsilon-acetyl)-MCA. Moreover, all enzymes also exhibited a distinct specificity for the length of the lysine side chain; acetylated ornithine, which comprises one CH(2) unit less in the side chain, was not a substrate. In line with these results, only acetylcadaverin the metabolic degradation product of lysine but neither acetylputrescine (degradation product of ornithine) nor acetylspermidine strongly inhibited enzyme activity. Boc-l-Lys(epsilon-trifluoroacetyl)-MCA was observed to be a superior substrate for FB188 HDAH, Pseudomonas aeruginosa HDAH (PA3774), and particularly HDAC 8 compared to rat liver HDAC, and is the first suitable (synthetic) substrate for (human-derived) HDAC 8 reported to date. Altogether, the results reveal clear differences in substrate specificity between different HDACs as analyzed in the fluorogenic HDAC assay. Finally, we present the first candidates for HDAC-type-selective substrates that may be useful as biochemical tools to establish the function of particular pathways and to elucidate the role of distinct HDAC subtypes in cellular differentiation and cancer.

Topics: Animals; Binding Sites; Bordetella; Catalytic Domain; Chromatography, High Pressure Liquid; Cloning, Molecular; DNA; Histone Deacetylases; Histones; Humans; Immunoblotting; Kinetics; Lysine; Models, Chemical; Oligonucleotide Probes; Polyamines; Propionates; Protein Binding; Protein Structure, Tertiary; Pseudomonas aeruginosa; Rats; Recombinant Proteins; Repressor Proteins; Sodium Acetate; Sodium Chloride; Substrate Specificity; Time Factors; Trifluoroacetic Acid

The effectiveness of low-toxicity chemicals as possible alternatives to synthetic fungicides for the control of post-harvest green and blue moulds of citrus was evaluated. A preliminary selection of chemicals, mostly common food additives, was made through in vivo primary screenings with oranges artificially inoculated with Penicillium digitatum or P italicum. Selected compounds and mixtures were tested as heated solutions in small-scale trials. Immersion of artificially inoculated oranges or lemons for 120 s in solutions at 40.6 degrees C and natural pH of potassium sorbate (0.2 M), sodium benzoate (0.2 M) or mixtures (0.1 + 0.1 M) of potassium sorbate with sodium benzoate, sodium propionate or sodium acetate were the most effective organic acid salts tested and reduced green mould by 70-80% after 7 days of storage at 20 degrees C. The mixtures did not significantly enhance the effectiveness of potassium sorbate or sodium benzoate alone. These solutions were as effective as sodium carbonate or calcium polysulphide treatments and, in general, they were more effective on lemons than on oranges. Satisfactory control of green and blue moulds was obtained by dipping oranges for 150 s in solutions of sodium molybdate (24.2 mM) or ammonium molybdate (1.0 mM) at 48 or 53 degrees C, but not at 20 degrees C. At 53 degrees C, however, the effectiveness of hot water was not enhanced by either molybdate. Molybdenum salts at higher concentrations were phytotoxic and stained the fruit. At non-phytotoxic concentrations, the effectiveness of these solutions was more influenced by temperature than by concentration. In general, the inhibitory effects of all compounds tested were not fungicidal but fungistatic and not very persistent. In conclusion, potassium sorbate, sodium benzoate and ammonium molybdate, among the wide range of chemicals tested, were superior for the control of post-harvest Penicillium decay of citrus fruit.

Topics: Citrus; Drug Interactions; Food Additives; Fruit; Hot Temperature; Hydrogen-Ion Concentration; Molybdenum; Organic Chemicals; Penicillium; Propionates; Sodium Acetate; Sodium Benzoate; Sorbic Acid

The role of the key catalytic residues Glu134 and Glu138 in the retaining 1,3-1,4-beta-glucanase from Bacillus licheniformis is probed by a chemical rescue methodology based on enzyme activation of inactive mutants by the action of added nucleophiles. While Glu134 was proposed as the catalytic nucleophile on the basis of affinity labeling experiments, no functional proof supported the assignment of Glu138 as the general acid-base catalyst. Alanine replacements are prepared by site-directed mutagenesis to produce the inactive E138A and E134A mutants. Addition of azide reactivates the mutants in a concentration-dependent manner using an activated 2, 4-dinitrophenyl glycoside substrate. The chemical rescue operates by a different mechanism depending on the mutant as deduced from 1H NMR monitoring and kinetic analysis of enzyme reactivation. E138A yields the beta-glycosyl azide product arising from nucleophilic attack of azide on the glycosyl-enzyme intermediate, thus proving that Glu138 is the general acid-base residue. Azide activates the deglycosylation step (increasing kcat), but it also has a large effect on a previous step (as seen by the large decrease in KM, the increase in kcat/KM, and the pH dependence of activation), probably increasing the rate of glycosylation through Bronsted acid catalysis by enzyme-bound HN3. By contrast, azide reactivates the E134A mutant through a single inverting displacement to give the alpha-glycosyl azide product, consistent with Glu134 being the catalytic nucleophile. Formate as an exogenous nucleophile has no effect on the E138A mutant, whereas it is a better activator of E134A than azide. Although the reaction yields the normal hydrolysis product, a transient compound was detected by 1H NMR, tentatively assigned to the alpha-glycosyl formate adduct. This is the first case where a nonmodified sugar gives a long-lived covalent intermediate that mimics the proposed glycosyl-enzyme intermediate of retaining glycosidases.

Topics: Alanine; Amino Acid Substitution; Bacillus; Catalysis; Energy Transfer; Enzyme Activation; Formates; Glutamic Acid; Glycoside Hydrolases; Hydrolysis; Kinetics; Mutagenesis, Site-Directed; Propionates; Sodium Acetate; Sodium Azide; Substrate Specificity

The effects of sodium propionate, acetate, lactate and citrate on cell proliferation, glucose and oxygen consumption, and ATP production in Listeria monocytogenes were investigated in growing and resting cells. Media pH was 6.7-6.8. Growth inhibition increased while glucose consumption continued in the presence of > or = 1% propionate, > or = 3% acetate and > or = 5% lactate in broth during incubation at 35 degrees C, indicating that glucose consumption was uncoupled from cell proliferation. Acetate and propionate were the most effective antilisterials, whereas citrate (5%) was only slightly inhibitory. Of the four salts, only lactate supported growth, oxygen consumption and ATP production. While concentrations of 1 and 5% propionate, acetate and citrate did not have an effect on oxygen consumption, they inhibited ATP production. ATP production in the presence of the four salts was consistently lower at pH 6.0 than at neutral pH. Lactate served as an alternative energy source for L. monocytogenes in the absence of glucose but became toxic to the organism in the presence of the carbohydrate.

Topics: Adenosine Triphosphate; Fatty Acids, Volatile; Glucose; Listeria monocytogenes; Oxygen Consumption; Propionates; Sodium Acetate; Sodium Lactate

The effects of 1 to 100 mM volatile fatty acids (VFA) on the cranial dorsal rumen musculature of sheep were examined in vitro. Sodium acetate, sodium propionate and sodium butyrate, either singly or as a mixture, stimulated marked dose-dependent contractions of longitudinal muscle (LM) and internal oblique muscle (IOM). The threshold concentration was between 1 and 3 mM depending on the VFA and the muscle tissue and the responses were modified by the presence of the mucosal epithelium. The responses to VFA were significantly decreased by atropine (10(-6) M) and tetrodotoxin (10(-7) M) but were unaffected by hexamethonium (10(-3) M). Indomethacin (10(-6) M) modified the responses, suggesting that prostaglandins may also be involved. Acetic, propionic and butyric acids also stimulated dose-dependent contractions of LM and IOM. After having been stimulated with 100 mM acids the preparations became refractory to further stimulation by acetylcholine. It is concluded that in vitro the acid and salt forms of VFA excite contractions of the rumen by both cholinergic and non-cholinergic mechanisms.

Topics: Acetylcholine; Animals; Atropine; Butyrates; Butyric Acid; Fatty Acids, Volatile; Female; Gastric Mucosa; Gastrointestinal Motility; Hexamethonium; In Vitro Techniques; Indomethacin; Male; Muscle Contraction; Muscle, Smooth; Propionates; Rumen; Sheep; Sodium Acetate; Tetrodotoxin