Title: Xylanase inhibitors bind to nonstarch polysaccharides
Authors: Fierens, Ellen ×
Gebruers, Kurt
Courtin, Christophe
Delcour, Jan #
Issue Date: Jan-2008
Publisher: Amer chemical soc
Series Title: Journal of Agricultural and Food Chemistry vol:56 issue:2 pages:564-570
Abstract: This study is an in-depth investigation of the interaction between polysaccharides and the proteinaceous xylanase inhibitors, Triticum aestivum xylanase inhibitor (TAXI), xylanase inhibitor protein (XIP), and thaumatin-like xylanase inhibitor (TLXI). The binding affinities of all three known types of xylanase inhibitors from wheat are studied by measuring the residual xylanase inhibition activity after incubation of the inhibitors in the presence of different polysaccharides, such as beta-glucans and (arabino)xylans. The binding affinities of all three xylanase inhibitors for (arabino)xylans increased with a decreasing arabinose/xylose ratio (A/X ratio). This phenomenon was observed both with water-extractable and water-unextractable (arabino)xylans. The inhibitors also interacted with different soluble and insoluble beta-glucans. None of the inhibitors tested had the ability to hydrolyze the polysaccharides investigated. The present findings contribute to the unraveling of the function of xylanase inhibitors in nature and to the prediction of the effect of added xylanases in cereal-based biotechnological processes, such as bread making and gluten-starch separation.
ISSN: 0021-8561
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Centre for Food and Microbial Technology
× corresponding author
# (joint) last author

Files in This Item:
File Description Status SizeFormat
Fierens 2008 J Agric Food Chem 56 564-570.pdf Published 382KbAdobe PDFView/Open Request a copy
Manuscript final version.pdf Published 370KbAdobe PDFView/Open Request a copy

These files are only available to some KU Leuven Association staff members


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science