Molecular characterization and solution properties of enzymatically tailored arabinoxylans

Research output: Contribution to journalArticleScientificpeer-review

Researchers

Research units

  • University of Helsinki

Abstract

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.

Details

Original languageEnglish
Pages (from-to)963-969
Number of pages7
JournalInternational Journal of Biological Macromolecules
Volume49
Issue number5
Publication statusPublished - 1 Dec 2011
MoE publication typeA1 Journal article-refereed

    Research areas

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

ID: 30819546