Zeitschriftenartikel: „Selenomonas ruminantium“

1

Michel, Tomas A., und Joan M. Macy. „Ferredoxin from Selenomonas ruminantium“. Archives of Microbiology 153, Nr. 5 (April 1990): 518–20. http://dx.doi.org/10.1007/bf00248437.

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2

Kalmokoff, M. L., J. W. Austin, M. F. Whitford und R. M. Teather. „Characterization of a major envelope protein from the rumen anaerobeSelenomonas ruminantiumOB268“. Canadian Journal of Microbiology 46, Nr. 4 (01.04.2000): 295–303. http://dx.doi.org/10.1139/w99-149.

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Cell envelopes from the Gram-negative staining but phylogenetically Gram-positive rumen anaerobe Selenomonas ruminantium OB268 contained a major 42 kDa heat modifiable protein. A similarly sized protein was present in the envelopes of Selenomonas ruminantium D1 and Selenomonas infelix. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of Triton X-100 extracted cell envelopes from S. ruminantium OB268 showed that they consisted primarily of the 42 kDa protein. Polyclonal antisera produced against these envelopes cross-reacted only with the 42 kDa major envelope proteins in both S. ruminantium D1 and S. infelix, indicating a conservation of antigenic structure among each of the major envelope proteins. The N-terminus of the 42 kDa S. ruminantium OB268 envelope protein shared significant homology with the S-layer (surface) protein from Thermus thermophilus, as well as additional envelope proteins containing the cell surface binding region known as a surface layer-like homologous (SLH) domain. Thin section analysis of Triton X-100 extracted envelopes demonstrated the presence of an outer bilayer overlaying the cell wall, and a regularly ordered array was visible following freeze-fracture etching through this bilayer. These findings suggest that the regularly ordered array may be composed of the 42 kDa major envelope protein. The 42 kDa protein has similarities with regularly ordered outer membrane proteins (rOMP) reported in certain Gram-negative and ancient eubacteria.Key words: Selenomonas envelope surface SLH domain.

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3

Pristas, Peter, und Maria Piknova. „Underrepresentation of short palindromes in Selenomonas ruminantium DNA: evidence for horizontal gene transfer of restriction and modification systems?“ Canadian Journal of Microbiology 51, Nr. 4 (01.04.2005): 315–18. http://dx.doi.org/10.1139/w05-004.

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Molecular analysis of isolates of the rumen bacterium Selenomonas ruminantium revealed a high variety and frequency of site-specific (restriction) endonucleases. While all known S. ruminantium restriction and modification systems recognize hexanucleotide sequences only, consistently low counts of both 6-bp and 4-bp palindromes were found in DNA sequences of S. ruminantium. Statistical analysis indicated that there is some correlation between the degree of underrepresentation of tetranucleotide words and the number of known restriction endonucleases for a given sequence. Control analysis showed the same correlation in lambda DNA but not in human adenovirus DNA. Based on the data presented, it could be proposed that there is a much higher historical occurrence of restriction and modification systems in S. ruminantium and (or) frequent horizontal gene transfer of restriction and modification gene complexes.Key words: Selenomonas, palindromes, restriction-modification.

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4

Wiryawan, KG, und JD Brooker. „Probiotic control of lactate accumulation in acutely grain-fed sheep“. Australian Journal of Agricultural Research 46, Nr. 8 (1995): 1555. http://dx.doi.org/10.1071/ar9951555.

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When sheep were acutely fed a grain diet, ruminal pH rapidly dropped to less than 5.0, lactic acid exceeded 100 mM and clinical symptoms of acidosis were evident within 24 h. When acute grain feeding was preceeded by inoculation of the rumen with 108 cfu of Selenomonas ruminantium subsp. lactilytica strain JDB201, ruminal lactate was undetectable and ruminal pH was stabilized at 6.3-6.5 for up to 24 h. Inoculation of the rumen with a mixture of 108 cfu each of Selenomonas ruminantium subsp. lactilytica strain JDB201 and Megasphaera elsdenii strain JDB301 was shown to be more effective than Selenomonas ruminantium subsp. lactilytica alone and maintained ruminal stability following acute grain feeding for up to 4 days. A continuous culture model of acidosis was also developed to test the effect of probiotic inoculation in combination with 0.75 8g/mL of Virginiamycin in preventing lactate accumulation and establishing a stable fermentation in vitro. The data suggest that although probiotic treatment is effective, a combination of probiotic and antibiotic may be the best approach to achieve rapid ruminal adaptation during acute grain feeding of sheep.

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5

Haya, Shohei, Yuya Tokumaru, Naoki Abe, Jun Kaneko und Shin-ichi Aizawa. „Characterization of Lateral Flagella of Selenomonas ruminantium“. Applied and Environmental Microbiology 77, Nr. 8 (18.02.2011): 2799–802. http://dx.doi.org/10.1128/aem.00286-11.

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ABSTRACTSelenomonas ruminantiumproduces a tuft of flagella near the midpoint of the cell body and swims by rotating the cell body along the cell's long axis. The flagellum is composed of a single kind of flagellin, which is heavily glycosylated. The hook length ofS. ruminantiumis almost double that ofSalmonella.

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6

Fecskeová, Lívia, Peter Pristaš und Peter Javorský. „Cloning and characterization of cobA, one of vitamin B12 biosynthesis pathway genes from Selenomonas ruminantium“. Nova Biotechnologica et Chimica 10, Nr. 2 (31.08.2021): 131–35. http://dx.doi.org/10.36547/nbc.1122.

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Bacterial biosynthesis of vitamin B12 can occur via either aerobic or anaerobic route. While the aerobic pathway has been fully elucidated and understood, less is known about the anaerobic pathway. Selenomonas ruminantium is thought to be the main producer of this vitamin in rumen environment and must use the anaerobic pathway. In our work we found one of the genes of vitamin B12 biosynthetic pathway of S. ruminantium, encoding for the cobalamin adenosyltransferase, enzyme taking part at the last steps of the synthesis process. Deduced amino acid sequence showed the highest similarity to cobalamin adenosyltransferases of other ruminal anaerobic bacteria and that of species Selenomonas. Phylogenetic comparisons of CobA protein sequences of several anaerobic bacteria of Clostridiale order indicate possible horizontal transfer of this gene.

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7

Nisbet, David J., und Scott A. Martin. „Factors affecting L-lactate utilization by Selenomonas ruminantium“. Journal of Animal Science 72, Nr. 5 (01.05.1994): 1355–61. http://dx.doi.org/10.2527/1994.7251355x.

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8

Williams, D. K., und S. A. Martin. „Xylose uptake by the ruminal bacterium Selenomonas ruminantium.“ Applied and Environmental Microbiology 56, Nr. 6 (1990): 1683–88. http://dx.doi.org/10.1128/aem.56.6.1683-1688.1990.

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9

Brooker, J. D., und B. Stokes. „Monoclonal antibodies against the ruminal bacterium Selenomonas ruminantium.“ Applied and Environmental Microbiology 56, Nr. 7 (1990): 2193–99. http://dx.doi.org/10.1128/aem.56.7.2193-2199.1990.

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10

Kopecny, J., V. Kostyukovsky und K. Fliegerova. „Electroporation of G+ host plasmids into Selenomonas ruminantium“. CrossRef Listing Of Deleted DOIs 45, Suppl. 1 (1996): 356. http://dx.doi.org/10.1051/rnd:19960685.

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11

Cotta, MA, und TR Whitehead. „Xylooligosaccharide utilization by the ruminal bacterium Selenomonas ruminantium“. Reproduction Nutrition Development 37, Suppl. 1 (1997): 51–52. http://dx.doi.org/10.1051/rnd:19970732.

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12

Fliegerová, Benada und Flint. „Large plasmids in ruminal strains of Selenomonas ruminantium“. Letters in Applied Microbiology 26, Nr. 4 (April 1998): 243–47. http://dx.doi.org/10.1046/j.1472-765x.1998.00299.x.

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13

Pristas, P., K. Fliegerova und P. Javorsky. „Two restriction endonucleases in Selenomonas ruminantium subsp. lactilytica“. Letters in Applied Microbiology 27, Nr. 2 (August 1998): 83–85. http://dx.doi.org/10.1046/j.1472-765x.1998.00392.x.

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14

Martin, Scott A. „Hexose Phosphorylation by the Ruminal Bacterium Selenomonas ruminantium“. Journal of Dairy Science 79, Nr. 4 (April 1996): 550–56. http://dx.doi.org/10.3168/jds.s0022-0302(96)76399-3.

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15

Kopecny, J., V. Kostyukovsky und K. Fliegerova. „Electroporation of G+ host plasmids into Selenomonas ruminantium“. Annales de Zootechnie 45, Suppl. 1 (1996): 356. http://dx.doi.org/10.1051/animres:19960685.

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16

de Vries, Wytske, Willemina M. C. van Wijck-Kapteyn und S. K. H. Oosterhuis. „The Presence and Function of Cytochromes in Selenomonas ruminantium, Anaerovibrio lipolytica and Veillonella alcalescens“. Microbiology 81, Nr. 1 (01.01.2000): 69–78. http://dx.doi.org/10.1099/00221287-81-1-69.

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Strains of Selenomonas ruminantium, Anaerovibrio lipolytica and Veillonella alcalescens contained cytochrome b. Peaks corresponding to cytochromes a and a carbon monoxide-binding pigment were also observed. By means of dual-wavelength experiments with crude membrane fractions it was established that cytochrome b functioned in anaerobic electron transport to fumarate. In V. alcalescens and one strain of S. ruminantium which reduced nitrate, anaerobic electron transport to nitrate was found. Glycerol 1-phosphate and NADH were active as hydrogen donors for cytochrome b reduction in glycerol-grown A. lipolytica, lactate and pyruvate were active in lactate-grown V. alcalescens, and NADH was active in lactose-grown S. ruminantium. Oxidative phosphorylation associated with these electron transfer systems might explain the high molar growth yields previously found for these micro-organisms. Fermentation products were measured in supernatant fluids of cultures grown in the presence and absence of nitrate. Nitrate did not influence the fermentation of lactose to lactate by S. ruminantium, and inhibited propionate formation by V. alcalescens.

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17

Matte, Allan, Cecil W. Forsberg und Ann M. Verrinder Gibbins. „Enzymes associated with metabolism of xylose and other pentoses by Prevotella (Bacteroides) ruminicola strains, Selenomonas ruminantium D, and Fibrobacter succinogenes S85“. Canadian Journal of Microbiology 38, Nr. 5 (01.05.1992): 370–76. http://dx.doi.org/10.1139/m92-063.

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Prevotella (Bacteroides) ruminicola strains B14 and S23 and Selenomonas ruminantium strain D used xylose as the sole source of carbohyrate for growth, whereas Fibrobacter succinogenes was unable to metabolize xylose. Prevotella ruminicola strain B14 exhibited transport activity for xylose. In contrast, F. succinogenes lacked typical xylose uptake activity but did exhibit low binding potential for the sugar. Prevotella ruminicola strains B14 and S23 as well as S. ruminantium D showed low xylose isomerase activities but higher xylulokinase activities, using assays that gave high activities for these enzymes in Escherichia coli. Xylose isomerase appeared to be produced constitutively in these ruminal bacteria, but xylulokinase was induced to varying degrees with xylose as the source of carbohydrate. Fibrobacter succinogenes lacked xylose isomerase and xylulokinase. All three species of ruminal bacteria possessed transketolase,xylulose-5-phosphate epimerase, and ribose-5-phosphate isomerase activities. Neither P. ruminicola B14 nor F. succinogenes S85 showed significant phosphoketolase activity. The data indicate that F. succinogenes is unable to either actively uptake or metabolize xylose as a result of the absence of functional xylose permease, xylose isomerase, and xylulokinase activities, although it and both P. ruminicola and S. ruminantium possess the essential enzymes of the nonoxidative branch of the pentose phosphate cycle. Key words: Fibrobacter succinogenes, Prevotella, Selenomonas, xylose metabolism, rumen bacteria, pentose phosphate cycle.

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18

Cotta, Michael A., und Terence R. Whitehead. „Xylooligosaccharide Utilization by the Ruminal Anaerobic Bacterium Selenomonas ruminantium“. Current Microbiology 36, Nr. 4 (01.04.1998): 183–89. http://dx.doi.org/10.1007/s002849900291.

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19

Michel, Tomas A., und Joan M. Macy. „Preparation of spheroplasts from the strict anaerobe Selenomonas ruminantium“. Journal of Microbiological Methods 11, Nr. 1 (Februar 1990): 37–41. http://dx.doi.org/10.1016/0167-7012(90)90045-8.

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20

Evans, J. D., und S. A. Martin. „Factors affecting lactate and malate utilization by Selenomonas ruminantium.“ Applied and environmental microbiology 63, Nr. 12 (1997): 4853–58. http://dx.doi.org/10.1128/aem.63.12.4853-4858.1997.

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21

Bishop, Richard, Moses Obura, David Odongo und Agnes Odenyo. „Specific PCR Assay for a Tannin-Tolerant Selenomonas ruminantium Isolate, Derived from Helicase Coding Sequences“. Applied and Environmental Microbiology 70, Nr. 5 (Mai 2004): 3180–82. http://dx.doi.org/10.1128/aem.70.5.3180-3182.2004.

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ABSTRACT Sequences from a tannin-tolerant Selenomonas ruminantium isolate (EAT2) that hydrolyzes gallic acid were identified. Two exhibited identity to helicases with a wide phylogenetic distribution. PCR amplification by using primers from one helicase gene detected 2,000 to 5,000 EAT2 genome equivalents but did not amplify total gastrointestinal microbial DNA of nine other ungulate species.

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22

D'Silva, C. G., H. D. Bae, L. J. Yanke, K. J. Cheng und L. B. Selinger. „Localization of phytase in Selenomonas ruminantium and Mitsuokella multiacidus by transmission electron microscopy“. Canadian Journal of Microbiology 46, Nr. 4 (01.04.2000): 391–95. http://dx.doi.org/10.1139/w00-001.

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The localization of phytase (myo-inositol-hexaphosphate phosphohydrolase) in the ruminal bacteria, Selenomonas ruminantium JY35 and Mitsuokella multiacidus 46/5(2), was determined with transmission electron microscopy. Phosphate produced from the enzymatic dephosphorylation of the calcium salt of phytic acid is precipitated as calcium phosphate. The calcium is then replaced with lead to produce electron-dense lead phosphate. This deposition of lead phosphate localized phytase in S. ruminantium JY35 and M. multiacidus 46/5(2) to the outer membrane, and confirmed intracellular expression of the enzyme in Escherichia coli pSrP.2, the recombinant clone which possesses the gene (phyA) encoding phytase (phyA) in S. ruminantium.Key words: phytase, localization, ruminal bacteria, transmission electron microscopy.

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23

Caldwell, Daniel R. „Effects of methanol on the growth of gastrointestinal anaerobes“. Canadian Journal of Microbiology 35, Nr. 2 (01.02.1989): 313–17. http://dx.doi.org/10.1139/m89-047.

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The effects of methanol on the growth of representative, predominant, anaerobic gut bacteria were studied. Growth yields and rates were determined in a base medium to which methanol was added to produce media with methanol concentrations varying, in twofold steps, over a concentration range of 0.01 to 25%, by volume. The growth of many of the organisms was completely inhibited by a methanol concentration equal to, or less than, 6.2%. Isolates representing cellulolytic species were completely inhibited at a methanol concentration of 3.1%, and inhibitory effects on the yield of some cellulolytic isolates were found at a methanol concentration as small as 0.01%. Although most of the organisms studied were inhibited at relatively small methanol concentrations, isolates of Selenomonas ruminantium, Bacteroides ovatus, and Fusobacterium necrophorum were relatively methanol resistant. A methanol concentration of 12.5% was required to completely inhibit S. ruminantium. Substantial growth of B. ovatus was obtained in media containing 12.5% methanol, and for F. necrophorum, substantial growth occurred in media containing 25% methanol. The yields of F. necrophorum strain B85 and S. ruminantum strain PC18 were enhanced by relatively small methanol concentrations and reduced with further methanol concentration increase. Anaerobic, nonsporing gut bacteria exhibit a diversity of responses to methanol.Key words: methanol, growth, bacteria, anaerobic, gastrointestinal.

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Piña-Gónzalez, Laura, Juan Miranda-Ríos, Rogelio Alejandro Alonso-Morales, Otoniel Maya, Luis Corona und Claudia Cecilia Márquez-Mota. „PSXIV-15 Metagenomic sequencing of rumen microorganisms of cattle fed a corn stover-based diet“. Journal of Animal Science 97, Supplement_3 (Dezember 2019): 441–44. http://dx.doi.org/10.1093/jas/skz258.873.

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Abstract Worldwide, there is a need to discover new microorganisms that efficiently degrade lignocellulosic complexes that would help to improve the digestibility of low-quality agricultural byproducts. The aim of the study was to evaluate the effects of a corn stover-based diet (CSD) on rumen bacteria. Ruminal fluid of 6 Holstein cows (595 ± 96 kg) was collected during two periods. During first period, animals were consuming a diet based on corn silage and oat hay (DB), mineral premix and water ad libitum (50:50, DM). In second period, animals were provided a CSD (100% DM), mineral premix and water ad libitum for 45 days. Ruminal fluid was collected through esophageal tube, filtered and stored at -80°C until DNA extraction. Rumen microorganisms were identified by sequencing the 16SrRNA gene using the Illumina Miseq platform and primers for V3 and V4 regions. Data were analyzed by QIIME 1.9. Analysis of variance was performed for a completely randomized design using the MIXED procedure of SAS 9.1. The taxonomic affiliation showed that both populations were mainly composed of Firmicutes, Bacteroidetes and Proteobacteria. The most abundant bacteria species in both diets were Ruminococcus flavefaciens, Prevotella copri, Prevotella ruminicola, Fibrobacter succinogenes, Bacillus coagulans, Bacteroides uniformis and Selenomonas ruminantium. Feeding a CSD, increased the relative abundance of Prevotella ruminicola (from 6.1 to 20.9%, P < 0.01), Streptococcus luteciae (from 0.05 to 0.78%, P < 0.01), Clostridium aminophilum (0.45 to 3.1%, P < 0.01), Selenomonas ruminantium (5.2 to 21.8%, P < 0.02) and Pantoea agglomerans (0.7 to 3.9%, P < 0.01) and decreased Propionibacterium acnes (0.7 to 0.1%, P < 0.02) and Bacteroides ovatus (0.9 to 0.1%, P < 0.01). Feeding cattle with a diet with a more lignified forage like CSD led to the proliferation of bacteria such as Prevotella ruminicula, Streptococcus luteciae, Clostridium aminophilum, Selenomonas ruminantium and Pantoea agglomerans.

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25

Takatsuka, Yumiko, Yoshihiro Yamaguchi, Minenobu Ono und Yoshiyuki Kamio. „Gene Cloning and Molecular Characterization of Lysine Decarboxylase from Selenomonas ruminantiumDelineate Its Evolutionary Relationship to Ornithine Decarboxylases from Eukaryotes“. Journal of Bacteriology 182, Nr. 23 (01.12.2000): 6732–41. http://dx.doi.org/10.1128/jb.182.23.6732-6741.2000.

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ABSTRACT Lysine decarboxylase (LDC; EC 4.1.1.18 ) from Selenomonas ruminantium comprises two identical monomeric subunits of 43 kDa and has decarboxylating activities toward both l-lysine andl-ornithine with similar Km andVmax values (Y. Takatsuka, M. Onoda, T. Sugiyama, K. Muramoto, T. Tomita, and Y. Kamio, Biosci. Biotechnol. Biochem. 62:1063–1069, 1999). Here, the LDC-encoding gene (ldc) of this bacterium was cloned and characterized. DNA sequencing analysis revealed that the amino acid sequence of S. ruminantium LDC is 35% identical to those of eukaryotic ornithine decarboxylases (ODCs; EC 4.1.1.17 ), including the mouse,Saccharomyces cerevisiae, Neurospora crassa,Trypanosoma brucei, and Caenorhabditis elegansenzymes. In addition, 26 amino acid residues, K69, D88, E94, D134, R154, K169, H197, D233, G235, G236, G237, F238, E274, G276, R277, Y278, K294, Y323, Y331, D332, C360, D361, D364, G387, Y389, and F397 (mouse ODC numbering), all of which are implicated in the formation of the pyridoxal phosphate-binding domain and the substrate-binding domain and in dimer stabilization with the eukaryotic ODCs, were also conserved inS. ruminantium LDC. Computer analysis of the putative secondary structure of S. ruminantium LDC showed that it is approximately 70% identical to that of mouse ODC. We identified five amino acid residues, A44, G45, V46, P54, and S322, within the LDC catalytic domain that confer decarboxylase activities toward bothl-lysine and l-ornithine with a substrate specificity ratio of 0.83 (defined as thek cat/Km ratio obtained with l-ornithine relative to that obtained withl-lysine). We have succeeded in converting S. ruminantium LDC to form with a substrate specificity ratio of 58 (70 times that of wild-type LDC) by constructing a mutant protein, A44V/G45T/V46P/P54D/S322A. In this study, we also showed that G350 is a crucial residue for stabilization of the dimer in S. ruminantium LDC.

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Martin, S. A., und R. G. Dean. „Characterization of a plasmid from the ruminal bacterium Selenomonas ruminantium.“ Applied and Environmental Microbiology 55, Nr. 12 (1989): 3035–38. http://dx.doi.org/10.1128/aem.55.12.3035-3038.1989.

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27

Gilmour, M., H. J. Flint und W. J. Mitchell. „Multiple lactate dehydrogenase activities of the rumen bacterium Selenomonas ruminantium“. Microbiology 140, Nr. 8 (01.08.1994): 2077–84. http://dx.doi.org/10.1099/13500872-140-8-2077.

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Pristas, P., I. Vanat, N. Kostrabova und P. Javorsky. „Variability of endonucleolytic activity within natural population of Selenomonas ruminantium“. Reproduction Nutrition Development 37, Suppl. 1 (1997): 75–76. http://dx.doi.org/10.1051/rnd:19970759.

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MARTIN, S. A., und J. B. RUSSELL. „Mechanisms of Sugar Transport in the Rumen Bacterium Selenomonas ruminantium“. Microbiology 134, Nr. 3 (01.03.1988): 819–27. http://dx.doi.org/10.1099/00221287-134-3-819.

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30

Chu, Hsing-Mao, Rey-Ting Guo, Ting-Wan Lin, Chia-Cheng Chou, Hui-Lin Shr, Hui-Lin Lai, Tsung-Yin Tang, Kuo-Joan Cheng, Brent L. Selinger und Andrew H. J. Wang. „Structures of Selenomonas ruminantium Phytase in Complex with Persulfated Phytate“. Structure 12, Nr. 11 (November 2004): 2015–24. http://dx.doi.org/10.1016/j.str.2004.08.010.

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31

Al-Khaldi, Sufian F., Lawren L. Durocher und Scott A. Martin. „Deoxyribonuclease Activity in Selenomonas ruminantium , Streptococcus bovis , and Bacteroides ovatus“. Current Microbiology 41, Nr. 3 (13.09.2000): 182–86. http://dx.doi.org/10.1007/s002840010115.

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Yamaguchi, Yoshihiro, Yumiko Takatsuka und Yoshiyuki Kamio. „Two Segments in Bacterial Antizyme P22 Are Essential for Binding and Enhance Degradation of Lysine/Ornithine Decarboxylase in Selenomonas ruminantium“. Journal of Bacteriology 190, Nr. 1 (26.10.2007): 442–46. http://dx.doi.org/10.1128/jb.01429-07.

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ABSTRACT In Selenomonas ruminantium, a strictly anaerobic and gram-negative bacterium, the degradation of lysine/ornithine decarboxylase (LDC/ODC) by ATP-requiring protease(s) is accelerated by the binding of P22, which is a ribosomal protein of this strain. Amino acid sequence alignment of S. ruminantium P22 with the L10 ribosomal proteins of gram-positive and -negative bacteria showed that P22 has a 5-residue K101NKLD105 segment and an 11-residue G160VIRNAVYVLD170 segment, both of which are lacking in L10 in any other gram-positive and gram-negative bacteria reported. To elucidate whether the two segments are involved in P22 function, a series of mutant genes of P22 were constructed and expressed in Escherichia coli. The proteins were isolated and assayed for their function with respect to S. ruminantium LDC/ODC and mouse ODC. The results indicated that the two segments of P22 are crucial for P22 binding to both enzymes and also accelerated degradation of both decarboxylases.

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Heinrichová, Kveta, Július Heinrich, Mária Dzúrová und Alexander Ziolecki. „Mode of Action and Partial Purification of the Active Centre of exo-Poly-α-D-galacturonosidase from Selenomonas ruminantium“. Collection of Czechoslovak Chemical Communications 58, Nr. 3 (1993): 681–92. http://dx.doi.org/10.1135/cccc19930681.

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In the presented paper are summarized results of the study of the mode of action, dimensions and arrangement of the active centre of the exo-poly-α-D-galacturonosidase, (poly(1,4-α-D-galactosiduronate) digalacturonohydrolase, E.C. 3.2.1.82) produced by the bacteria Selenomonas ruminantium. With this aim we determined experimentally values of Michaelis constants and limiting rates for the catalytic hydrolysis of linear oligo(D-galactosiduronates) of the degree of polymeration in the range of 3 to 8, at pH 7.0 and the temperature 30 °C. We calculated molecular activities k0 and parameters k0/Km from these values. From the dependence of logk0 and logk0/Km on the degree of polymerization five subsites of the active centre were determined, with the catalytic site being situated between the second and third one. Kinetic data were used for the calculation of the affinities of the fourth and fifth subsites A4 and A5 in accordance with the theory of Hiromi. Product analysis of non-labelled oligo(D-galactosiduronates) and compounds labelled with [1-3H] at the reducing end anabled to ascertain approximately the value for the first subsite A1 of the active centre and to study the mode of action of the exo-poly-α-D-galacturonosidase from Selenomonas ruminantium.

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Grochowska, Sylwia, Włodzimierz Nowak, Małgorzata Lasik-Kurdyś, Robert Mikuła und Jacek Nowak. „The effect of Saccharomyces cerevisiae on in vitro growth and fermentation of Selenomonas ruminantium and Megasphaera elsdenii“. Roczniki Naukowe Polskiego Towarzystwa Zootechnicznego 13, Nr. 3 (29.09.2017): 9–22. http://dx.doi.org/10.5604/01.3001.0010.5453.

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Stimulation of lactate utilization by Selenomonas ruminantium and Megasphaera elsdenii may help in reducing problems associated with rumen acidosis. The objective of this study was to determine the effect of a Saccharomyces cerevisiae live culture and Saccharomyces cerevisiae fermentation products on in vitro growth and fermentation of lactate-utilizing ruminal bacteria, S. ruminantium (ATCC 19205) and M. elsdenii (ATCC 25940). The cultures were run for 0, 6, 12, 24 and 48 h under anaerobic conditions on a growth medium supplemented with a yeast live culture (SC) or with yeast fermentation products (SCFP) and, as reference, on the same medium without supplementation (CON). Neither SC nor SCFP had a significant effect on the growth of S. ruminantium after 6, 12 and 24 h of incubation, but the live yeast culture significantly (P≤0.05) improved the growth of these bacteria after 48 h of incubation. The yeast fermentation products significantly (P≤0.05) decreased pH and increased lactate synthesis by S. ruminantium. The Saccharomyces cerevisiae live culture significantly improved the growth of M. elsdenii after 12 and 24 h of incubation, and the S. cerevisiae fermentation products increased its growth after 48 h. The After 24 and 48 h of incubation the Saccharomyces cerevisiae live culture reduced the concentration of total volatile fatty acids (VFA), while caproate was the main product of in vitro fermentation of M. elsdenii (P≤0.05). Saccharomyces cerevisiae live cultures may improve microbial fibre fermentation in the rumen by maintaining optimal pH conditions.

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Cotta, M. A. „Utilization of nucleic acids by Selenomonas ruminantium and other ruminal bacteria.“ Applied and Environmental Microbiology 56, Nr. 12 (1990): 3867–70. http://dx.doi.org/10.1128/aem.56.12.3867-3870.1990.

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Silley, P., und D. G. Armstrong. „Metabolism of the rumen bacterium Selenomonas ruminantium grown in continuous culture“. Letters in Applied Microbiology 1, Nr. 3 (März 1985): 53–55. http://dx.doi.org/10.1111/j.1472-765x.1985.tb01488.x.

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Dean, R. G., S. A. Martin und C. Carver. „Isolation of plasmid DNA from the ruminal bacterium Selenomonas ruminantium HD4“. Letters in Applied Microbiology 8, Nr. 2 (Februar 1989): 45–48. http://dx.doi.org/10.1111/j.1472-765x.1989.tb00220.x.

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Pristas, Peter, Jozef Ivan und Peter Javorsky. „Structural instability of small rolling circle replication plasmids from Selenomonas ruminantium“. Plasmid 64, Nr. 2 (September 2010): 74–78. http://dx.doi.org/10.1016/j.plasmid.2010.04.005.

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Nakamura, Mutsumi, Takafumi Nagamine, Koretsugu Ogata, Kiyoshi Tajima und Rustem I. Aminov. „Sequence Analysis of Small Cryptic Plasmids Isolated from Selenomonas ruminantium S20“. Current Microbiology 38, Nr. 2 (01.02.1999): 107–12. http://dx.doi.org/10.1007/s002849900412.

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Jordan, Douglas B., Xin-Liang Li, Christopher A. Dunlap, Terence R. Whitehead und Michael A. Cotta. „β-d-Xylosidase from Selenomonas ruminantium of glycoside hydrolase family 43“. Applied Biochemistry and Biotechnology 137-140, Nr. 1-12 (April 2007): 93–104. http://dx.doi.org/10.1007/s12010-007-9042-6.

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Ricke, S. C., und D. M. Schaefer. „An ascorbate-reduced medium for nitrogen metabolism studies with Selenomonas ruminantium“. Journal of Microbiological Methods 11, Nr. 3-4 (Juli 1990): 219–27. http://dx.doi.org/10.1016/0167-7012(90)90058-e.

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Skene, I. K., und J. D. Brooker. „Characterization of Tannin Acylhydrolase Activity in the Ruminal Bacterium Selenomonas Ruminantium“. Anaerobe 1, Nr. 6 (Dezember 1995): 321–27. http://dx.doi.org/10.1006/anae.1995.1034.

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43

Fliegerova, Katerina, Sylvie Pazoutova, Peter Pristas und Harry J. Flint. „Highly Conserved DNA Sequence Present in Small Plasmids from Selenomonas ruminantium“. Plasmid 44, Nr. 1 (Juli 2000): 94–99. http://dx.doi.org/10.1006/plas.2000.1464.

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Ghali, M. B., P. T. Scott, G. A. Alhadrami und R. A. M. Al Jassim. „Identification and characterisation of the predominant lactic acid-producing and lactic acid-utilising bacteria in the foregut of the feral camel (Camelus dromedarius) in Australia“. Animal Production Science 51, Nr. 7 (2011): 597. http://dx.doi.org/10.1071/an10197.

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The camel is emerging as a new and important animal in the Australian livestock industry. However, little is known regarding the microbial ecosystem of the gastrointestinal tract of this ruminant-like animal. This study was carried out to determine the diversity of lactic acid-producing and lactic acid-utilising bacteria in the foregut of the feral camel (Camelus dromedarius) in Australia. Putative lactic acid bacteria were isolated from the foregut contents of camels by culturing on De Man, Rogosa, Sharpe and lactic acid media. Identification of representative isolates was based on the analysis of 16S rRNA gene sequences. Fermentation end products of glucose (i.e. volatile fatty acids and lactate) were also measured in vitro. The key predominant bacteria identified in this study were closely related to Streptococcus bovis, Selenomonas ruminantium, Butyrivibrio fibrisolvens, Lachnospira pectinoschiza and Prevotella ruminicola. The main L-lactate producers were those isolates closely related to S. bovis, S. ruminantium and Lactococcus garvieae, while the efficient lactate utilisers were S. ruminantium-related isolates. D-lactate was produced by isolates closely related to either L. pectinoschiza or S. ruminantium. The predominant bacteria isolated and characterised in this study are identical and/or closely related to those typically found in true ruminants (e.g. S. ruminantium, B. fibrisolvens, S. bovis). In addition, some of the bacteria isolated represent novel species of Lachnospira and Clostridium in the context of lactic acid bacteria from a large herbivorous host. The results from this study have contributed to our understanding and provide opportunities to reduce foregut acidosis in the camel.

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Rasmussen, M. A. „Isolation and characterization of Selenomonas ruminantium strains capable of 2-deoxyribose utilization.“ Applied and Environmental Microbiology 59, Nr. 7 (1993): 2077–81. http://dx.doi.org/10.1128/aem.59.7.2077-2081.1993.

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Gilmour, M., W. J. Mitchell und H. J. Flint. „Genetic transfer of lactate-utilizing ability in the rumen bacterium Selenomonas ruminantium“. Letters in Applied Microbiology 22, Nr. 1 (Januar 1996): 52–56. http://dx.doi.org/10.1111/j.1472-765x.1996.tb01107.x.

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Sawanon, Suriya, Satoshi Koike und Yasuo Kobayashi. „Evidence for the possible involvement of Selenomonas ruminantium in rumen fiber digestion“. FEMS Microbiology Letters 325, Nr. 2 (21.10.2011): 170–79. http://dx.doi.org/10.1111/j.1574-6968.2011.02427.x.

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Terrasan, César Rafael Fanchini, Caio Casale Aragon, Douglas Chodi Masui, Benevides Costa Pessela, Gloria Fernandez-Lorente, Eleonora Cano Carmona und Jose Manuel Guisan. „β-xylosidase from Selenomonas ruminantium: Immobilization, stabilization, and application for xylooligosaccharide hydrolysis“. Biocatalysis and Biotransformation 34, Nr. 4 (03.07.2016): 161–71. http://dx.doi.org/10.1080/10242422.2016.1247817.

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Sprincova, Adriana, Peter Javorsky und Peter Pristas. „pSRD191, a new member of RepL replicating plasmid family from Selenomonas ruminantium“. Plasmid 54, Nr. 1 (Juli 2005): 39–47. http://dx.doi.org/10.1016/j.plasmid.2004.11.004.

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Hausinger, R. P. „Purification of a nickel-containing urease from the rumen anaerobe Selenomonas ruminantium.“ Journal of Biological Chemistry 261, Nr. 17 (Juni 1986): 7866–70. http://dx.doi.org/10.1016/s0021-9258(19)57483-x.

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