Xylanase inhibitors bind to nonstarch polysaccharides.
Identifieur interne : 000352 ( Main/Corpus ); précédent : 000351; suivant : 000353Xylanase inhibitors bind to nonstarch polysaccharides.
Auteurs : Ellen Fierens ; Kurt Gebruers ; Christophe M. Courtin ; Jan A. DelcourSource :
- Journal of agricultural and food chemistry [ 0021-8561 ] ; 2008.
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
Links to Exploration step
pubmed:18092758Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Xylanase inhibitors bind to nonstarch polysaccharides.</title><author><name sortKey="Fierens, Ellen" sort="Fierens, Ellen" uniqKey="Fierens E" first="Ellen" last="Fierens">Ellen Fierens</name><affiliation><nlm:affiliation>Laboratory of Food Chemistry and Biochemistry, Department of Microbial and Molecular Systems, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, Box 2463, 3001 Leuven, Belgium. ellen.fierens@biw.kuleuven.be</nlm:affiliation></affiliation></author><author><name sortKey="Gebruers, Kurt" sort="Gebruers, Kurt" uniqKey="Gebruers K" first="Kurt" last="Gebruers">Kurt Gebruers</name></author><author><name sortKey="Courtin, Christophe M" sort="Courtin, Christophe M" uniqKey="Courtin C" first="Christophe M" last="Courtin">Christophe M. Courtin</name></author><author><name sortKey="Delcour, Jan A" sort="Delcour, Jan A" uniqKey="Delcour J" first="Jan A" last="Delcour">Jan A. Delcour</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18092758</idno><idno type="pmid">18092758</idno><idno type="doi">10.1021/jf0724724</idno><idno type="wicri:Area/Main/Corpus">000352</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000352</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Xylanase inhibitors bind to nonstarch polysaccharides.</title><author><name sortKey="Fierens, Ellen" sort="Fierens, Ellen" uniqKey="Fierens E" first="Ellen" last="Fierens">Ellen Fierens</name><affiliation><nlm:affiliation>Laboratory of Food Chemistry and Biochemistry, Department of Microbial and Molecular Systems, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, Box 2463, 3001 Leuven, Belgium. ellen.fierens@biw.kuleuven.be</nlm:affiliation></affiliation></author><author><name sortKey="Gebruers, Kurt" sort="Gebruers, Kurt" uniqKey="Gebruers K" first="Kurt" last="Gebruers">Kurt Gebruers</name></author><author><name sortKey="Courtin, Christophe M" sort="Courtin, Christophe M" uniqKey="Courtin C" first="Christophe M" last="Courtin">Christophe M. Courtin</name></author><author><name sortKey="Delcour, Jan A" sort="Delcour, Jan A" uniqKey="Delcour J" first="Jan A" last="Delcour">Jan A. Delcour</name></author></analytic><series><title level="j">Journal of agricultural and food chemistry</title><idno type="ISSN">0021-8561</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Endo-1,4-beta Xylanases (antagonists & inhibitors)</term><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></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Endo-1,4-beta Xylanases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Enzyme Inhibitors</term><term>Glucans</term><term>Polysaccharides</term><term>Xylans</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Seeds</term><term>Triticum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrolysis</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18092758</PMID><DateCompleted><Year>2008</Year><Month>04</Month><Day>08</Day></DateCompleted><DateRevised><Year>2008</Year><Month>01</Month><Day>17</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-8561</ISSN><JournalIssue CitedMedium="Print"><Volume>56</Volume><Issue>2</Issue><PubDate><Year>2008</Year><Month>Jan</Month><Day>23</Day></PubDate></JournalIssue><Title>Journal of agricultural and food chemistry</Title><ISOAbbreviation>J Agric Food Chem</ISOAbbreviation></Journal><ArticleTitle>Xylanase inhibitors bind to nonstarch polysaccharides.</ArticleTitle><Pagination><MedlinePgn>564-70</MedlinePgn></Pagination><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></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fierens</LastName><ForeName>Ellen</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Laboratory of Food Chemistry and Biochemistry, Department of Microbial and Molecular Systems, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, Box 2463, 3001 Leuven, Belgium. ellen.fierens@biw.kuleuven.be</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gebruers</LastName><ForeName>Kurt</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Courtin</LastName><ForeName>Christophe M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Delcour</LastName><ForeName>Jan A</ForeName><Initials>JA</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>12</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Agric Food Chem</MedlineTA><NlmUniqueID>0374755</NlmUniqueID><ISSNLinking>0021-8561</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005936">Glucans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011134">Polysaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014990">Xylans</NameOfSubstance></Chemical><Chemical><RegistryNumber>9040-27-1</RegistryNumber><NameOfSubstance UI="C085118">arabinoxylan</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.8</RegistryNumber><NameOfSubstance UI="D043364">Endo-1,4-beta Xylanases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D043364" MajorTopicYN="N">Endo-1,4-beta Xylanases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005936" MajorTopicYN="N">Glucans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012639" MajorTopicYN="N">Seeds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014908" MajorTopicYN="N">Triticum</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014990" MajorTopicYN="N">Xylans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>12</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>4</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>12</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18092758</ArticleId><ArticleId IdType="doi">10.1021/jf0724724</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/ThaumatinV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000352 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 000352 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= ThaumatinV1
|flux= Main
|étape= Corpus
|type= RBID
|clé= pubmed:18092758
|texte= Xylanase inhibitors bind to nonstarch polysaccharides.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Corpus/RBID.i -Sk "pubmed:18092758" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a ThaumatinV1
| This area was generated with Dilib version V0.6.37. |  |