Molecular characterization and solution properties of enzymatically tailored arabinoxylans

Leena Pitkänen*, Päivi Tuomainen, Liisa Virkki, Maija Tenkanen

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

21 Citations (Scopus)


Two α- l-arabinofuranosidases with different substrate specificities were used to modify the arabinose-to-xylose ratio of cereal arabinoxylans: one enzyme (AXH-m) removed the l-arabinofuranosyl substituents from the monosubstituted xylopyranosyl residues and the other (AXH-d3) the (1 → 3)-linked l-arabinofuranosyl units from the disubstituted xylopyranosyl residue. In this study, we noticed that not only the arabinose-to-xylose ratio but also the position of the arabinofuranosyl substituents affects the water-solubility of arabinoxylans. The AXH-d3 treatment had no significant effect on the solution conformation of arabinoxylans, but the density of the arabinoxylan molecules decreased in DMSO solution after AXH-m modification. The possible heterogeneity of arabinoxylans complicated the interpretation of data describing the macromolecular properties of the enzymatically modified samples.

Original languageEnglish
Pages (from-to)963-969
Number of pages7
JournalInternational Journal of Biological Macromolecules
Issue number5
Publication statusPublished - 1 Dec 2011
MoE publication typeA1 Journal article-refereed


  • α-l-Arabinofuranosidase
  • Arabinoxylan
  • Enzymatic modification
  • Hydrodynamic properties
  • Molar mass
  • Size-exclusion chromatography

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