Butyrivibrio fibrisolvens

14,000,000 Leading Edge Experts on the ideXlab platform

Scan Science and Technology

Contact Leading Edge Experts & Companies

Scan Science and Technology

Contact Leading Edge Experts & Companies

The Experts below are selected from a list of 231 Experts worldwide ranked by ideXlab platform

Robert J. Stack - One of the best experts on this subject based on the ideXlab platform.

Lennart Kenne - One of the best experts on this subject based on the ideXlab platform.

  • Structural studies of the extracellular polysaccharide produced by Butyrivibrio fibrisolvens strain H10b.
    Carbohydrate research, 2003
    Co-Authors: Lars Andersson, Michael A. Cotta, Lennart Kenne
    Abstract:

    The extracellular polysaccharide produced by Butyrivibrio fibrisolvens strain H10b, when grown under strictly anaerobic conditions with glucose as carbohydrate source, has been studied by chemical and spectroscopic techniques. The results demonstrate that the polysaccharide consists of hexasaccharide repeating units with the following structure: [structure: see text] The isolated polysaccharide was found to be approximately 65% acetylated at O-2 of the 3-O-[(S)-1-carboxyethyl]-beta-D-Glcp residue. The absolute configuration of the 1-carboxyethyl groups was determined by circular dichroism.

  • structural studies of the extracellular polysaccharide produced by Butyrivibrio fibrisolvens strain h10b
    Carbohydrate Research, 2003
    Co-Authors: Lars Andersson, Michael A. Cotta, Lennart Kenne
    Abstract:

    Abstract The extracellular polysaccharide produced by Butyrivibrio fibrisolvens strain H10b, when grown under strictly anaerobic conditions with glucose as carbohydrate source, has been studied by chemical and spectroscopic techniques. The results demonstrate that the polysaccharide consists of hexasaccharide repeating units with the following structure: Download : Download full-size image The isolated polysaccharide was found to be ∼65% acetylated at O-2 of the 3-O-[(S)-1-carboxyethyl]-β- d -Glcp residue. The absolute configuration of the 1-carboxyethyl groups was determined by circular dichroism.

  • Structural studies of the extracellular polysaccharide from Butyrivibrio fibrisolvens strain CF3
    Carbohydrate Research, 1997
    Co-Authors: Fernando Ferreira, Lennart Kenne, Michael A. Cotta, Robert J. Stack
    Abstract:

    Abstract The capsular polysaccharide from Butyrivibrio fibrisolvens strain X6C61 has been investigated using NMR spectroscopy, mass spectrometry, methylation methylation analysis, and partial acid hydrolysis as the main methods. The polysasccharide is composed of hexasaccharide repeating units having the following structure. The polysaccharide also contains O-acetyl groups, of which ≈70% are substituted to O-3 of the β- d -GlcpA residue.

  • Structural studies of the extracellular polysaccharide from Butyrivibrio fibrisolvens strain CF3.
    Carbohydrate research, 1997
    Co-Authors: Fernando Ferreira, Lennart Kenne, Michael A. Cotta, Robert J. Stack
    Abstract:

    The structure of the Butyrivibrio fibrisolvens strain CF3 capsular polysaccharide has been investigated mainly by sugar and methylation analyses, Smith degradation, NMR spectroscopy, and mass spectrometry. The results indicate that the polysaccharide is composed of pentasaccharide repeating units having the following structure: -->4)-beta-L-Altp-(1-->4)-beta-D-Glcp-(1-->3)-4-O-[(R)-1-carboxyet hyl]-beta- D-Glcp-(1-->4)-6-O-[(R)-1-carboxyethyl]-alpha-D-Galp-(1--> 2 increases 1 beta-D-Glcp.

  • Structural studies of the extracellular polysaccharide from Butyrivibrio fibrisolvens strain 49.
    Carbohydrate research, 1995
    Co-Authors: Fernando Ferreira, Lennart Kenne, Michael A. Cotta, M Andersson, Robert J. Stack
    Abstract:

    The structure of Butyrivibrio fibrisolvens strain 49 capsular polysaccharide has been investigated mainly by sugar and methylation analysis, partial chemical degradations, NMR spectroscopy, and mass spectrometry. The results suggest that the polysaccharide is composed of pentasaccharide repeating units having the following structure. [formula: see text] The polysaccharide contains O-acetyl groups, one of which is substituted to O-3 of the 4-substituted alpha-D-Galp residue, while others occur in non-stoichiometric amounts at other locations.

Gang-ping Xue - One of the best experts on this subject based on the ideXlab platform.

  • Transformation and expression of an anaerobic fungal xylanase in several strains of the rumen bacterium Butyrivibrio fibrisolvens.
    Journal of applied microbiology, 2002
    Co-Authors: Kari S. Gobius, Brian P. Dalrymple, Yolande Swadling, Gang-ping Xue, James H. Aylward, Christopher S. Mcsweeney, Denis Krausé
    Abstract:

    To obtain reliable transformation of a range of Butyrivibrio fibrisolvens strains and to express a Neocallimastix patriciarum xylanase gene in the recipients. Eight strains (H17c, E14, LP1309, LP1028, AR11a, OB156, LP210B and LP461A) of Bu. fibrisolvens were transformed by the Gram-positive vector pUB110. A xylanase expression/secretion cassette containing Bu. fibrisolvens promoter and signal peptide elements fused to catalytic domain II of the N. patriciarum xylanase A cDNA (xynANp) was inserted into pUB110 to create the plasmid pUBxynA. pUBxynA was used to transform seven of the Bu. fibrisolvens strains transformed by pUB110. In strain H17c pUBxynA, which produced native xylanase, 2.46 U mg-1 total xylanase activity was produced with 45% extracellular xylanase. In strain H17c pUMSX, 0.74 U mg-1 total xylanase activity was produced with 98% extracellular xylanase. H17c pUBxynA exhibited increased (28.7%) degradation of neutral detergent fibre compared with unmodified H17c; however, progressive loss of pUBxynA was observed in long-term cultivation. A stable transformation system was developed that was applicable for a range of Bu. fibrisolvens strains and high levels of expression of a recombinant xylanase were obtained in H17c which lead to increased fibre digestion. This stable transformation system with the accompanying recombinant plasmids will be a useful tool for further investigation aimed at improving ruminal fibre digestion.

  • Distribution and evolution of the xylanase genes xynA and xynB and their homologues in strains of Butyrivibrio fibrisolvens.
    Applied and environmental microbiology, 1999
    Co-Authors: Brian P. Dalrymple, Yolande Swadling, Ingrid Layton, Kari S. Gobius, Gang-ping Xue
    Abstract:

    The ruminal bacterium Butyrivibrio fibrisolvens is being engineered by the introduction of heterologous xylanase genes in an attempt to improve the utilization of plant material in ruminants. However, relatively little is known about the diversity and distribution of the native xylanase genes in strains of B. fibrisolvens. In order to identify the most appropriate hosts for such modifications, the xylanase genotypes of 28 strains from the three 16S ribosomal DNA (rDNA) subgroups of Butyrivibrio fibrisolvens have been investigated. Only 4 of the 20 strains from 16S rDNA group 2 contained homologues of the strain Bu49 xynA gene. However, these four xynA-containing strains, and two other group 2 strains, contained members of a second xylanase gene family clearly related to xynA (subfamily I). Homologues of xynB, a second previously described xylanase gene from B. fibrisolvens, were identified only in three of the seven group 1 strains and not in the group 2 and 3 strains. However, six of the group 1 strains contained one or more members of the two subfamilies of homologues of xynA. The distribution of genes and the nucleotide sequence relationships between the members of the two xynA subfamilies are consistent with the progenitor of all strains of B. fibrisolvens having contained a xynA subfamily I gene. Since many xylanolytic strains of B. fibrisolvens did not contain members of either of the xynA subfamilies or of the xynB family, at least one additional xylanase gene family remains to be identified in B. fibrisolvens.

  • Cloning of a gene encoding cinnamoyl ester hydrolase from the ruminai bacterium Butyrivibrio fibrisolvens E14 by a novel method
    FEMS microbiology letters, 1996
    Co-Authors: Brian P. Dalrymple, Yolande Swadling, D. H. Cybinski, Gang-ping Xue
    Abstract:

    A gene (cinI) encoding a cinnamoyl ester hydrolase (CEH) has been isolated from the ruminal bacterium, Butyrivibrio fibrisolvens E14, using a model substrate, MUTMAC [4-methylumbelliferoyl (p-trimethylammonium cinnamate chloride)]. CinI has significant amino-acid similarities with members of a large and diverse family of hydrolases with a serine/aspartic acid/histidine catalytic triad. Our analyses identified two previously unclassified amino acid sequences, the amino-terminal domain of unknown function in XynZ from Clostridium thermocellum and XynC, an acetylxylan esterase from Caldicellulosiruptor saccharolyticus, as members of the same family of hydrolases. A previously described esterase with CEH activity, XylD from Pseudomonas fluorescens ssp. cellulosa, is not similar to CinI. CinI was expressed at high levels in the periplasmic fraction of E. coli TOPP2 and released ferulic acid from Fara [5-O-(trans-feruloyl)-arabinofuranose] prepared from wheat bran.

Harry J. Flint - One of the best experts on this subject based on the ideXlab platform.

Karen P. Scott - One of the best experts on this subject based on the ideXlab platform.