Degradation and utilization of xylans by the rumen anaerobe Prevotella bryantii (formerly P-ruminicola subsp brevis) B(1)4

K Miyazaki, J C Martin, R Marinsek-Logar, H J Flint

Research output: Contribution to journalArticle

121 Citations (Scopus)

Abstract

Freshly harvested whole cells from cultures of P. bryantii B(1)4 grown with oat spelt xylan (OSX) as an energy source showed less than 25% of the enzyme activity against OSX, and less than 15% of the activity against birchwood xylan (BWX) and carboxymethylcellutose, that was detectable in sonicated cell preparations. This indicates that much of this hydrolytic activity is either periplasmic, membrane-associated or intracellular and may be concerned with the processing of transported oligosaccharides. P. bryantii B(1)4 cultures were able to utilise up to 45% and 51% of the total pentose present in OSX and BWX, respectively, after 24 h, but could utilize 84% of a water-soluble fraction of BWX. Analysis of the xylan left undegraded after incubation with P. bryantii showed that while xylose and arabinose were removed to a similar extent, uronic acids were utilized to a greater extent than xylose. Predigestion of xylans with two cloned xylanases from the cellulolytic rumen anaerobe Ruminococcus flavefaciens gave Little increase in overall pentose utilization suggesting that external P. bryantii xylanases are as effective as the cloned X. flavefaciens enzymes in releasing products that can be utilised by P. bryantii cells. The xylanase system of P. bryantii is able to efficiently utilise not only xylo-oligosaccharides but also larger water-soluble xylan fragments. (C) 1997 Academic Press.

Original languageEnglish
Pages (from-to)373-381
Number of pages9
JournalAnaerobe
Volume3
Issue number6
Publication statusPublished - Dec 1997

Keywords

  • xylanase
  • Prevotella bryantii
  • Prevotella ruminicola
  • Ruminococcus flavefaciens
  • rumen
  • enzyme localization
  • BACTEROIDES-RUMINICOLA
  • RUMINAL BACTERIA
  • STRAINS
  • GENE
  • EXPRESSION
  • SEQUENCE
  • ENZYMES

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