1987
DOI: 10.1007/bf00406127
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Pathway of propionate formation from ethanol in Pelobacter propionicus

Abstract: Abstract. Whole cells of Pelobacter propionicus fermented(1-13C) ethanol and CO2 to nearly equal amounts of (2-13C) and (3-13C) propionate and to (1-13C) acetate indicating a randomizing pathway of propionate formation. Enzymes involved in the fermentation were assayed in cell-free extracts and cetyltrimethylammonium bromide-permeabilized cells grown with ethanol as sole substrate. Alcohol dehydrogenase, aldehyde dehydrogenase (benzylviologen-reducing), phosphate acetyl transferase, acetate kinase, pyruvate sy… Show more

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Cited by 65 publications
(37 citation statements)
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(39 reference statements)
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“…vG o0 ¼ 3124 kJ per 3 mol ethanol and uses the methylmalonyl-CoA pathway [26]. P. propionicus exhibited di¡erent growth rates and growth yields when growing either with lactate or ethanol.…”
Section: Discussionmentioning
confidence: 99%
“…vG o0 ¼ 3124 kJ per 3 mol ethanol and uses the methylmalonyl-CoA pathway [26]. P. propionicus exhibited di¡erent growth rates and growth yields when growing either with lactate or ethanol.…”
Section: Discussionmentioning
confidence: 99%
“…OTU35a was related to Pelobacter propionicus ( Figure 5), which is known to convert ethanol to propionate (3 ethanol+2 bicarbonate → 2 propionate+1 acetate+1 proton+3 water; Schink et al, 1987) but not syntrophically to acetate and H 2 (reaction 11 in Supplementary Table S1) as do Pelobacter acetylenicus and Pelobacter carbinolicus (Schink, 1984;Seitz et al, 1990). However, only small concentrations of propionate were detected in ethanol-supplemented microcosms, whereas transient acetate accumulations were repeatedly observed at 15 and 5°C after the addition of ethanol (Supplementary Figures S4b and S8b).…”
Section: Syntrophic Methanogenesis In Peat O Schmidt Et Almentioning
confidence: 99%
“…Cells were permeabilized in the respective assay cuvettes with cetyltrimethyl ammonium bromide (CTAB; details see Schink et al 1987). Hydrogenase, acetaldehyde: ferredoxin oxidoreductase, and pyruvate: ferredoxin oxidoreductase were measured with benzylviologen as electron acceptor (Schink 1985;Odom & Peck 1981), phosphotransacetylase and acetate kinase after Bergmeyer (1974), malate dehydrogenase and fumarase after Stams et al (1984), succinate dehydrogenase after Boonstra et al (1975), propionyl CoA: succinate CoA transferase after Hilpert et al (1984), lactate dehydrogenase after Bergmeyer (1974) and Stams & Hansen (1982).…”
Section: Enzymesmentioning
confidence: 99%