Xylanase inhibitors bind to nonstarch polysaccharides.
Identifieur interne : 000332 ( Main/Exploration ); précédent : 000331; suivant : 000333Xylanase inhibitors bind to nonstarch polysaccharides.
Auteurs : Ellen Fierens [Belgique] ; Kurt Gebruers ; Christophe M. Courtin ; Jan A. DelcourSource :
- Journal of agricultural and food chemistry [ 0021-8561 ] ; 2008.
Descripteurs français
- KwdFr :
- MESH :
- antagonistes et inhibiteurs : Endo-1,4-beta xylanases.
- composition chimique : Graines, Triticum.
- métabolisme : Antienzymes, Glucanes, Polyosides, Xylanes.
- Hydrolyse.
English descriptors
- KwdEn :
- MESH :
- chemical , antagonists & inhibitors : Endo-1,4-beta Xylanases.
- chemical , metabolism : Enzyme Inhibitors, Glucans, Polysaccharides, Xylans.
- chemistry : Seeds, Triticum.
- Hydrolysis.
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:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Enzyme Inhibitors (metabolism)</term>
<term>Glucans (metabolism)</term>
<term>Hydrolysis (MeSH)</term>
<term>Polysaccharides (metabolism)</term>
<term>Seeds (chemistry)</term>
<term>Triticum (chemistry)</term>
<term>Xylans (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Antienzymes (métabolisme)</term>
<term>Endo-1,4-beta xylanases (antagonistes et inhibiteurs)</term>
<term>Glucanes (métabolisme)</term>
<term>Graines (composition chimique)</term>
<term>Hydrolyse (MeSH)</term>
<term>Polyosides (métabolisme)</term>
<term>Triticum (composition chimique)</term>
<term>Xylanes (métabolisme)</term>
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<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Endo-1,4-beta Xylanases</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Enzyme Inhibitors</term>
<term>Glucans</term>
<term>Polysaccharides</term>
<term>Xylans</term>
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<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Endo-1,4-beta xylanases</term>
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<term>Triticum</term>
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<front><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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<Abstract><AbstractText>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.</AbstractText>
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