Degradation of complex arabinoxylans by human colonic Bacteroidetes

Nat Commun. 2021 Jan 19;12(1):459. doi: 10.1038/s41467-020-20737-5.

Abstract

Some Bacteroidetes and other human colonic bacteria can degrade arabinoxylans, common polysaccharides found in dietary fiber. Previous work has identified gene clusters (polysaccharide-utilization loci, PULs) for degradation of simple arabinoxylans. However, the degradation of complex arabinoxylans (containing side chains such as ferulic acid, a phenolic compound) is poorly understood. Here, we identify a PUL that encodes multiple esterases for degradation of complex arabinoxylans in Bacteroides species. The PUL is specifically upregulated in the presence of complex arabinoxylans. We characterize some of the esterases biochemically and structurally, and show that they release ferulic acid from complex arabinoxylans. Growth of four different colonic Bacteroidetes members, including Bacteroides intestinalis, on complex arabinoxylans results in accumulation of ferulic acid, a compound known to have antioxidative and immunomodulatory properties.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • Bacterial Proteins / ultrastructure
  • Bacteroides / enzymology*
  • Bacteroides / genetics
  • Colon / microbiology
  • Coumaric Acids / metabolism
  • Crystallography, X-Ray
  • Dietary Fiber / metabolism
  • Enzyme Assays
  • Esterases / genetics
  • Esterases / isolation & purification
  • Esterases / metabolism*
  • Esterases / ultrastructure
  • Gastrointestinal Microbiome / physiology*
  • Humans
  • Intestinal Mucosa / microbiology
  • Molecular Dynamics Simulation
  • Multigene Family / genetics
  • Substrate Specificity
  • Xylans / chemistry
  • Xylans / metabolism*

Substances

  • Bacterial Proteins
  • Coumaric Acids
  • Dietary Fiber
  • Xylans
  • arabinoxylan
  • ferulic acid
  • Esterases