Sugarcane bagasse derived xylooligosaccharides produced by an arabinofuranosidase/xylobiohydrolase from Bifidobacterium longum in synergism with xylanases

Caio Cesar de Mello Capetti, Ornella Ontañon, Laura E Navas, Eleonora Campos, Rachael Simister, Adam Dowle, Marcelo Vizoná Liberato, Vanessa de Oliveira Arnoldi Pellegrini, Leonardo D Gómez, Igor Polikarpov

Research output: Contribution to journalArticlepeer-review

Abstract

Arabinoxylan is a major hemicellulose in the sugarcane plant cell wall with arabinose decorations that impose steric restrictions on the activity of xylanases against this substrate. Enzymatic removal of the decorations by arabinofuranosidases can allow a more efficient arabinoxylan degradation by xylanases. Here we produced and characterized a recombinant Bifidobacterium longum arabinofuranosidase from glycoside hydrolase family 43 (BlAbf43) and applied it, together with GH10 and GH11 xylanases, to produce xylooligosaccharides (XOS) from wheat arabinoxylan and alkali pretreated sugarcane bagasse. The enzyme synergistically enhanced XOS production by GH10 and GH11 xylanases, being particularly efficient in combination with the latter family of enzymes, with a degree of synergism of 1.7. We also demonstrated that the enzyme is capable of not only removing arabinose decorations from the arabinoxylan and from the non-reducing end of the oligomeric substrates, but also hydrolyzing the xylan backbone yielding mostly xylobiose and xylose in particular cases. Structural studies of BlAbf43 shed light on the molecular basis of the substrate recognition and allowed hypothesizing on the structural reasons of its multifunctionality.

Original languageEnglish
Article number122248
Number of pages13
JournalCARBOHYDRATE POLYMERS
Volume339
Early online date11 May 2024
DOIs
Publication statusPublished - 1 Sept 2024

Keywords

  • Oligosaccharides/chemistry
  • Glycoside Hydrolases/metabolism
  • Glucuronates/metabolism
  • Endo-1,4-beta Xylanases/metabolism
  • Xylans/metabolism
  • Saccharum/chemistry
  • Cellulose/chemistry
  • Bifidobacterium longum/enzymology
  • Hydrolysis
  • Substrate Specificity
  • Recombinant Proteins/metabolism
  • Disaccharides

Cite this