Chrysosporium lucknowense C1 arabinofuranosidases are selective in releasing arabinose from either single or double substituted xylose residues in arabinoxylans

L.A.M. Pouvreau, R. Joosten, S.W.A. Hinz, H. Gruppen, H.A. Schols

Research output: Contribution to journalArticleAcademicpeer-review

24 Citations (Scopus)

Abstract

Two novel arabinofuranosidases, Abn7 and Abf3 from Chrysosporium lucknowense (C1), belonging to the glycoside hydrolase family 43 and 51 were purified and characterized. Abn7 is exclusively able to hydrolyze arabinofuranosyl residues at position O-3 of double substituted xylosyl residues in arabinoxylan-derived oligosaccharides, an activity rarely found thus far. Abf3 is able to release arabinose from position O-2 or O-3 of single substituted xyloses. Both enzymes performed optimal at pH 5.0 and 40 °C. Combining Abn7 and Abf3 resulted in a synergistic increase in arabinose release from arabinoxylans. This synergistic effect is due to the action of Abf3 on the remaining arabinose residues at position O-2 on single substituted xylosyl residues resulting from the action of Abn7 on double substituted xylosyl residues. Arabinose release was further increased when an endo-1,4-ß-xylanase was present during digestion. The efficiency of these arabinohydrolases from C1 on insoluble arabinoxylan substrates is discussed.
Original languageEnglish
Pages (from-to)397-403
JournalEnzyme and Microbial Technology
Volume48
Issue number4-5
DOIs
Publication statusPublished - 2011

Keywords

  • maize bran
  • lignocellulosic materials
  • aspergillus-awamori
  • wheat arabinoxylan
  • side-chains
  • cell-walls
  • oligosaccharides
  • complex
  • ethanol
  • purification

Fingerprint

Dive into the research topics of 'Chrysosporium lucknowense C1 arabinofuranosidases are selective in releasing arabinose from either single or double substituted xylose residues in arabinoxylans'. Together they form a unique fingerprint.

Cite this