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Methanosarcina barkeri

About: Methanosarcina barkeri is a research topic. Over the lifetime, 703 publications have been published within this topic receiving 32151 citations.


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Journal ArticleDOI
TL;DR: In this article, the effects of Mg2+ on thermophilic (55 degrees C) granules grown on acetate in 0.2liter upflow anaerobic sludge blanket reactors were studied.
Abstract: The effects of Mg2+ on thermophilic (55 degrees C) granules grown on acetate in 0.2-liter upflow anaerobic sludge blanket reactors were studied. The methanogens in the granules were identified and counted by using antibody probes and the antigenic fingerprinting method. Packets of large coccoidal cells antigenically related to Methanosarcina thermophila TM-1 were scarce in the absence of Mg2+ but increased with increasing Mg2+ concentrations up to 30 mM; Methanosarcina packets immunologically related to Methanosarcina barkeri R1M3 showed a similar trend, and their numbers increased up to 100 mM Mg2+. The number of single cells antigenically related to TM-1, R1M3, and Methanosarcina mazei S-6 were scarce at low Mg2+ concentrations but increased drastically at 30 and 100 mM Mg2+. The number of rod-shaped bacteria antigenically related to Methanobacterium thermoautotrophicum GC1 and delta H was highest with no Mg2+ present, and their numbers decreased with increasing concentrations of the cation. These quantitative data, obtained by counting cells in suspensions made from disrupted granules, were confirmed by microscopic observation of the methanogenic subpopulations in thin histologic sections of the granules. Images

31 citations

Journal ArticleDOI
TL;DR: It is reported here that cell extracts of the archaeon catalyze the formation of methyl-coenzyme M from coen enzyme M and tetramethylammonium and coen enzymatic activity was dependent on the presence of Ti(III) citrate and ATP, and was rapidly lost under oxic conditions.
Abstract: A methanogen (strain NaT1) that belongs to the family of Methanosarcinaceae and that can grow on tetramethylammonium as the sole energy source has recently been isolated. We report here that cell extracts of the archaeon catalyze the formation of methyl-coenzyme M from coenzyme M and tetramethylammonium. The activity was dependent on the presence of Ti(III) citrate and ATP, and was rapidly lost under oxic conditions. Anoxic chromatography on DEAE-Sepharose revealed that two fractions, fractions 3 and 4, were required for activity. A 50-kDa protein that together with fraction 3 catalyzed methyl-coenzyme M formation from tetramethylammonium and coenzyme M was purified from fraction 4. From fraction 3, a 22-kDa corrinoid protein and a 40-kDa protein exhibiting methylcobalamin:coenzyme M methyltransferase (MT2) activity were purified. The N-terminal amino acid sequences of these purified proteins were determined. The 40-kDa protein showed sequence similarity to MT2 isoenzymes from Methanosarcina barkeri. Cell extract of strain NaT1 grown on trimethylamine rather than on tetramethylammonium did not exhibit tetramethylammonium:coenzyme M methyltransferase activity. The strain was identified as belonging to the genus of Methanococcoides, its closest relative being Methanococcoides methylutens.

31 citations

Journal ArticleDOI
TL;DR: A gas-vacuolate strain of Methanosarcina barkeri formed protoplast in substrate-depleted cultures and gas vesicles were isolated from the protoplasts and were shown by electron microscopy to have a rib spacing of 4.8 nm.
Abstract: SUMMARY: A gas-vacuolate strain of Methanosarcina barkeri formed protoplasts in substrate-depleted cultures and gas vesicles were isolated from the protoplasts. Vacuolate protoplasts were separated from unvacuolate ones by flotation and the protoplast membrane was removed by Tween 20, liberating the gas vesicles. The gas vesicles were purified by flotation after initial passage through a 0.45 μm filter to remove contaminating material. Gas vesicle membranes were purified by isopycnic gradient centrifugation and were shown by electron microscopy to have a rib spacing of 4.8 nm.

31 citations

Journal ArticleDOI
TL;DR: Bacterial species dominated in the chemostat as a function of their enhanced substrate uptake and growth kinetic properties, and the substrate uptake kinetic properties displayed by the mixed che mostat population were equivalent to those of individual species measured in pure culture.
Abstract: Changes in lactose concentration and feed rate altered bacterial growth and population levels in a whey-processing chemostat. The bacterial population and methane production levels increased in relation to increased lactose concentrations comparable to those in raw whey (6%) and converted over 96% of the substrate to methane, carbon dioxide, and cells. Sequential increases in the chemostat dilution rate demonstrated excellent biomethanation performance at retention times as low as 25 h. Retention times shorter than 25 h caused prevalent bacterial populations and methane production to decrease, and intermediary carbon metabolites accumulated in the following order: acetate, butyrate, propionate, lactate, ethanol, and lactose. Bacterial species dominated in the chemostat as a function of their enhanced substrate uptake and growth kinetic properties. The substrate uptake kinetic properties displayed by the mixed chemostat population were equivalent to those of individual species measured in pure culture, whereas the growth kinetic properties of species in mixed culture were better than those measured in pure culture. A designed starter culture consisting of Leuconostoc mesenteroides, Desulfovibrio vulgaris, Methanosarcina barkeri, and Methanobacterium formicicum displayed biomethanation performance, which was similar to that of a diverse adapted mixed-culture inoculum, in a continuous contact digestor system to which 10 g of dry whey per liter was added. Preserved starter cultures were developed and used as inocula for the start-up of a continuous anaerobic digestion process that was effective for biomethanation of raw whey at a retention time of 100 h.

31 citations

Journal ArticleDOI
TL;DR: The immunological approach demonstrates that aminoacyl-tRNA synthetases do not belong to the group of enzymes in gene expression with high structural conservation and achieve the necessary fidelity by post-transfer proofreading, a corrective hydrolytic event after transfer to tRNAPhe.

30 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20237
202212
202112
202012
20197
201818