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Xylanase inhibitors bind to nonstarch polysaccharides.

Identifieur interne : 000332 ( Main/Exploration ); précédent : 000331; suivant : 000333

Xylanase inhibitors bind to nonstarch polysaccharides.

Auteurs : Ellen Fierens [Belgique] ; Kurt Gebruers ; Christophe M. Courtin ; Jan A. Delcour

Source :

RBID : pubmed:18092758

Descripteurs français

English descriptors

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.

DOI: 10.1021/jf0724724
PubMed: 18092758


Affiliations:


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Le document en format XML

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<term>Endo-1,4-beta Xylanases (antagonists & inhibitors)</term>
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<term>Glucans (metabolism)</term>
<term>Hydrolysis (MeSH)</term>
<term>Polysaccharides (metabolism)</term>
<term>Seeds (chemistry)</term>
<term>Triticum (chemistry)</term>
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<term>Glucanes (métabolisme)</term>
<term>Graines (composition chimique)</term>
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<term>Polyosides (métabolisme)</term>
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<term>Xylanes (métabolisme)</term>
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<div type="abstract" xml:lang="en">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.</div>
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