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Results for “Ethanol utilization”

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At least 55 records · Page 3Linked to original sources
PubMed1989

Production and Utilization of Ethanol by the Homoacetogen Acetobacterium woodii.

Acetobacterium woodii formed ethanol as a fermentation product in addition to acetate when the phosphate concentration of the medium was between 0.2 and 8.4 mM. Considerable amounts of alanine were also found (2 to 11 mM). Supplementation with phosphate caused a shift to acetate as the only end product. Ethanol could also serve as a substrate for A. woodii. The fermentation yielded predominantly acetate and was strictly dependent on high bicarbonate concentrations. 1-Propanol, 1-butanol, and 1-pentanol were converted to the corresponding fatty acids but allowed only marginal growth. A. wieringae and A. carbinolicum grown under identical conditions were also able to form ethanol, and A. wieringae could use ethanol as a substrate, too. Alcohol dehydrogenase and acetaldehyde dehydrogenase activities were determined in A. woodii. Activity stains of polyacrylamide gels with crude extracts allowed the detection of acetaldehyde dehydrogenase but not of alcohol dehydrogenase. Trace amounts of methane were detected during growth of A. woodii on glucose and ethanol.

Journal Article↗
PubMed1998

Differential effects of monensin on asialoglycoprotein receptor function after short-term ethanol administration.

Chronic ethanol consumption is associated with multiple impairments in receptor-mediated endocytosis (RME) by the hepatic asialoglycoprotein receptor (ASGP-R). Previous work on this receptor has shown that its activity can be perturbed by the carboxylic ionophore monensin. This agent has been shown to preferentially affect receptor-ligand dissociation and receptor redistribution of one subset (State 2) of ASGP-R, while receptor function in a second subset (State 1 receptors) is unaffected. In the present study, we examined the effect of monensin on ASGP-R activity and intracellular receptor-ligand dissociation after 7-10 days of ethanol feeding, a time when we have shown altered ASGP-R function in ethanol-fed animals. Hepatocytes from male Wistar rats (fed an ethanol-containing or control diet) were utilized. Ethanol administration decreased total ligand binding by 35-40% (P < 0.01) without a change in receptor protein content. After monensin treatment, surface receptors on cells from control animals were inactivated and redistributed to the cell interior. In cells from ethanol-fed animals, a similar pattern of monensin-induced inactivation was shown, but no redistribution occurred. Intracellular receptor-ligand dissociation was impaired in both cell types, although the monensin-induced effect on dissociation was significantly less dramatic (two-fold) in the hepatocytes from ethanol-fed animals as compared with controls. Thus, although receptors on both cell types were susceptible to monensin, cells from the ethanol-fed animals were less vulnerable to the added effects of this agent. Since monensin affects functioning of State 2, but not State 1 receptors, a very early effect of ethanol may be a preferential impairment in the State 2 receptor population.

Animals↗
PubMedDate not supplied

[Selection method and the characteristics of a cytochrome (a+a3)-deficient mutant of Candida parapsilosis yeasts].

A method was developed for selecting cytochrome-deficient mutants of yeast Candida parapsilosis; the method is based on determining the rate of inhibition of oxygen uptake by benzhydroxamic acid, an inhibitor of cyanide-resistant oxidase in the cells of preliminarily obtained yeast mutants. The mutant (C. parapsilosis bhas-1) lacks cytochrome a+a3, contains the same quantity of cytochrome b as the wild strain and a twice as low quantity of cytochrome c. In contrast to the wild strain, the mutant does not grow on ethanol for the first two days but, being cultivated further (up to 5 days), in a medium with ethanol, it resumes its capability to utilize ethanol as a carbon and energy source. Prolonged cultivation in the medium with ethanol induces the biosynthesis of cytochrome oxidase while cytochrome a+a3 is not induced in a medium supplied with glucose. The biomass accumulated by the mutant in the medium with glucose is twice as low comparing to that of the wild strain. The oxidative activity of the mutant mitochondria involves cyanide, resistant oxidase. The mitochondria of the mutant oxidize NAD-dependent substrates, NADH, NADPH, succinate, alpha-glycerophosphate, ethanol and lactate. The mitochondria have a low respiratory control and phosphorylate ADP while oxidizing NAD-dependent substrates, ethanol and lactate, but not alpha-glycerophosphate, succinate, NADH and NADPH.

Candida↗
PubMed1982

[Exchange reactions in brain tissue under chronic ethanol intoxication].

The paper deals with characterization of systems utilizing ethanol and reactions conjugated with its exchange in the brain tissue under chronic alcohol intoxication. The following is established: the absence of the alcoholdehydrogenase pathway of ethanol oxidation in rabbits, unbalanced splitting of carbohydrates under two-months ethanol load, disturbance of oxidative processes in the tricarboxylic acids cycle, a decrease in the pool of oxidized nicotin amide coenzymes.

Alcohol Oxidoreductases↗
PubMed1999

Multiple regulatory elements control the expression of the yeast ACR1 gene.

The ACR1 gene, encoding a succinate-fumarate transporter, is required by the yeast Saccharomyces cerevisiae for ethanol utilization. Accordingly, gene expression is induced by ethanol and repressed by glucose. Here, we investigated three carbon source response elements present in its promoter region. Specific deletions as well as functional analysis of the elements in a heterologous promoter confirmed their role in transcriptional regulation. Protein binding to carbon source response elements of the ICL1 promoter was competed by all three elements to various extents by the respective ACR1 sequences. In addition, two putative stress response promoter elements present in the ACR1 promoter were investigated in deletion analyses and shown to contribute to gene expression.

Basic-Leucine Zipper Transcription Factors↗
PubMed1992

Kinetics of ethanol metabolism in sheep.

Kinetic aspects of ethanol metabolism were studied in sheep after intravenous or intraruminal infusion of ethanol. Vmax and Km in fed animals were respectively 295 +/- 10 mg.h-1.l-1 (l = litre of body water) and 32.1 +/- 2.4 mg.l-1. Elimination half-life was 1.47 +/- 0.26 h. The corresponding values in the fasted animal were not significantly different. During venous infusion an increase in plasma acetate, inversely correlated to plasma ethanol, was observed. No modification in glycemia occurred. Intraruminal infusion of ethanol increased the concentration of all SCFA in the rumen juice, the largest part of this modification being relative to acetate. Repetition of the infusion over a period of 11 consecutive days increased the number of SCFA in the rumen, indicating microflora adaptation to ethanol utilization. Taking into account the range of ethanol concentrations found in silage (10-50 g.kg-1 BW) we can consider that ethanol is readily metabolized simultaneously by the rumen microflora and the enzymatic system of the host. With a corresponding daily intake of ethanol (0.2-1 g.kg-1 BW) both systems are not saturated and plasma ethanol level always remains below 0.25 g.l-1.

Acetates↗