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.
| Original language | English |
|---|---|
| Pages (from-to) | 963-969 |
| Number of pages | 7 |
| Journal | International Journal of Biological Macromolecules |
| Volume | 49 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 1 Dec 2011 |
| MoE publication type | A1 Journal article-refereed |
Funding
The authors thank Ndegwa Maina for help with the monosaccharide composition analysis of commercial wheat and rye arabinoxylans and Olli Aitio for assistance with NMR spectroscopy. The Academy of Finland (Valowheat project, Contract No 132150 ), the University of Helsinki Research Funds and the Finnish Cultural Foundation are gratefully acknowledged for funding this study.
Keywords
- α-l-Arabinofuranosidase
- Arabinoxylan
- Enzymatic modification
- Hydrodynamic properties
- Molar mass
- Size-exclusion chromatography
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