Riboflavin-binding protein exhibits selective sweet suppression toward protein sweeteners.
Identifieur interne : 000362 ( Main/Exploration ); précédent : 000361; suivant : 000363Riboflavin-binding protein exhibits selective sweet suppression toward protein sweeteners.
Auteurs : Kenji Maehashi [Japon] ; Mami Matano ; Azusa Kondo ; Yasushi Yamamoto ; Shigezo UdakaSource :
- Chemical senses [ 0379-864X ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Goût (effets des médicaments et des substances chimiques), Masse moléculaire (MeSH), Poulets (MeSH), Protéines d'oeuf (isolement et purification), Protéines d'oeuf (pharmacologie), Protéines de transport membranaire (isolement et purification), Protéines de transport membranaire (pharmacologie), Récepteurs de surface cellulaire (physiologie), Seuil du goût (effets des médicaments et des substances chimiques), Édulcorants (pharmacologie).
- MESH :
- effets des médicaments et des substances chimiques : Goût, Seuil du goût.
- isolement et purification : Protéines d'oeuf, Protéines de transport membranaire.
- pharmacologie : Protéines d'oeuf, Protéines de transport membranaire, Édulcorants.
- physiologie : Récepteurs de surface cellulaire.
- Animaux, Masse moléculaire, Poulets.
English descriptors
- KwdEn :
- Animals (MeSH), Chickens (MeSH), Egg Proteins (isolation & purification), Egg Proteins (pharmacology), Membrane Transport Proteins (isolation & purification), Membrane Transport Proteins (pharmacology), Molecular Weight (MeSH), Receptors, Cell Surface (physiology), Sweetening Agents (pharmacology), Taste (drug effects), Taste Threshold (drug effects).
- MESH :
- chemical , isolation & purification : Egg Proteins, Membrane Transport Proteins.
- chemical , pharmacology : Egg Proteins, Membrane Transport Proteins, Sweetening Agents.
- chemical , physiology : Receptors, Cell Surface.
- drug effects : Taste, Taste Threshold.
- Animals, Chickens, Molecular Weight.
Abstract
Riboflavin-binding protein (RBP) is well known as a riboflavin carrier protein in chicken egg and serum. A novel function of RBP was found as a sweet-suppressing protein. RBP, purified from hen egg white, suppressed the sweetness of protein sweeteners such as thaumatin, monellin, and lysozyme, whereas it did not suppress the sweetness of low molecular weight sweeteners such as sucrose, glycine, D-phenylalanine, saccharin, cyclamate, aspartame, and stevioside. Therefore, the sweet-suppressing activity of RBP was apparently selective to protein sweeteners. The sweet suppression by RBP was independent of binding of riboflavin with its molecule. Yolk RBP, with minor structural differences compared with egg white RBP, also elicited a weaker sweet suppression. However, other commercially available proteins including ovalbumin, ovomucoid, beta-lactogloblin, myoglobin, and albumin did not substantially alter the sweetness of protein sweeteners. Because a prerinse with RBP reduced the subsequent sweetness of protein sweeteners, whereas the enzymatic activity of lysozyme and the elution profile of lysozyme on gel permeation chromatography were not affected by RBP, it is suggested that the sweet suppression is caused by an interaction of RBP with a sweet taste receptor rather than with the protein sweeteners themselves. The selectivity in the sweet suppression by RBP is consistent with the existence of multiple interaction sites within a single sweet taste receptor.
DOI: 10.1093/chemse/bjl048
PubMed: 17167172
Affiliations:
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uniqKey="Kondo A" first="Azusa" last="Kondo">Azusa Kondo</name></author><author><name sortKey="Yamamoto, Yasushi" sort="Yamamoto, Yasushi" uniqKey="Yamamoto Y" first="Yasushi" last="Yamamoto">Yasushi Yamamoto</name></author><author><name sortKey="Udaka, Shigezo" sort="Udaka, Shigezo" uniqKey="Udaka S" first="Shigezo" last="Udaka">Shigezo Udaka</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17167172</idno><idno type="pmid">17167172</idno><idno type="doi">10.1093/chemse/bjl048</idno><idno type="wicri:Area/Main/Corpus">000374</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000374</idno><idno type="wicri:Area/Main/Curation">000374</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000374</idno><idno type="wicri:Area/Main/Exploration">000374</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Riboflavin-binding protein exhibits selective sweet suppression toward protein sweeteners.</title><author><name sortKey="Maehashi, Kenji" sort="Maehashi, Kenji" uniqKey="Maehashi K" first="Kenji" last="Maehashi">Kenji Maehashi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Fermentation Science, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Tokyo 156-8502, Japan. maehashi@nodai.ac.jp</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Fermentation Science, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Tokyo 156-8502</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Matano, Mami" sort="Matano, Mami" uniqKey="Matano M" first="Mami" last="Matano">Mami Matano</name></author><author><name sortKey="Kondo, Azusa" sort="Kondo, Azusa" uniqKey="Kondo A" first="Azusa" last="Kondo">Azusa Kondo</name></author><author><name sortKey="Yamamoto, Yasushi" sort="Yamamoto, Yasushi" uniqKey="Yamamoto Y" first="Yasushi" last="Yamamoto">Yasushi Yamamoto</name></author><author><name sortKey="Udaka, Shigezo" sort="Udaka, Shigezo" uniqKey="Udaka S" first="Shigezo" last="Udaka">Shigezo Udaka</name></author></analytic><series><title level="j">Chemical senses</title><idno type="ISSN">0379-864X</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Chickens (MeSH)</term><term>Egg Proteins (isolation & purification)</term><term>Egg Proteins (pharmacology)</term><term>Membrane Transport Proteins (isolation & purification)</term><term>Membrane Transport Proteins (pharmacology)</term><term>Molecular Weight (MeSH)</term><term>Receptors, Cell Surface (physiology)</term><term>Sweetening Agents (pharmacology)</term><term>Taste (drug effects)</term><term>Taste Threshold (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Goût (effets des médicaments et des substances chimiques)</term><term>Masse moléculaire (MeSH)</term><term>Poulets (MeSH)</term><term>Protéines d'oeuf (isolement et purification)</term><term>Protéines d'oeuf (pharmacologie)</term><term>Protéines de transport membranaire (isolement et purification)</term><term>Protéines de transport membranaire (pharmacologie)</term><term>Récepteurs de surface cellulaire (physiologie)</term><term>Seuil du goût (effets des médicaments et des substances chimiques)</term><term>Édulcorants (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Egg Proteins</term><term>Membrane Transport Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Egg Proteins</term><term>Membrane Transport Proteins</term><term>Sweetening Agents</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Receptors, Cell Surface</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Taste</term><term>Taste Threshold</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Goût</term><term>Seuil du goût</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines d'oeuf</term><term>Protéines de transport membranaire</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Protéines d'oeuf</term><term>Protéines de transport membranaire</term><term>Édulcorants</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Récepteurs de surface cellulaire</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Chickens</term><term>Molecular Weight</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Masse moléculaire</term><term>Poulets</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Riboflavin-binding protein (RBP) is well known as a riboflavin carrier protein in chicken egg and serum. A novel function of RBP was found as a sweet-suppressing protein. RBP, purified from hen egg white, suppressed the sweetness of protein sweeteners such as thaumatin, monellin, and lysozyme, whereas it did not suppress the sweetness of low molecular weight sweeteners such as sucrose, glycine, D-phenylalanine, saccharin, cyclamate, aspartame, and stevioside. Therefore, the sweet-suppressing activity of RBP was apparently selective to protein sweeteners. The sweet suppression by RBP was independent of binding of riboflavin with its molecule. Yolk RBP, with minor structural differences compared with egg white RBP, also elicited a weaker sweet suppression. However, other commercially available proteins including ovalbumin, ovomucoid, beta-lactogloblin, myoglobin, and albumin did not substantially alter the sweetness of protein sweeteners. Because a prerinse with RBP reduced the subsequent sweetness of protein sweeteners, whereas the enzymatic activity of lysozyme and the elution profile of lysozyme on gel permeation chromatography were not affected by RBP, it is suggested that the sweet suppression is caused by an interaction of RBP with a sweet taste receptor rather than with the protein sweeteners themselves. The selectivity in the sweet suppression by RBP is consistent with the existence of multiple interaction sites within a single sweet taste receptor.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17167172</PMID><DateCompleted><Year>2007</Year><Month>03</Month><Day>27</Day></DateCompleted><DateRevised><Year>2007</Year><Month>02</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0379-864X</ISSN><JournalIssue CitedMedium="Print"><Volume>32</Volume><Issue>2</Issue><PubDate><Year>2007</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Chemical senses</Title><ISOAbbreviation>Chem Senses</ISOAbbreviation></Journal><ArticleTitle>Riboflavin-binding protein exhibits selective sweet suppression toward protein sweeteners.</ArticleTitle><Pagination><MedlinePgn>183-90</MedlinePgn></Pagination><Abstract><AbstractText>Riboflavin-binding protein (RBP) is well known as a riboflavin carrier protein in chicken egg and serum. A novel function of RBP was found as a sweet-suppressing protein. RBP, purified from hen egg white, suppressed the sweetness of protein sweeteners such as thaumatin, monellin, and lysozyme, whereas it did not suppress the sweetness of low molecular weight sweeteners such as sucrose, glycine, D-phenylalanine, saccharin, cyclamate, aspartame, and stevioside. Therefore, the sweet-suppressing activity of RBP was apparently selective to protein sweeteners. The sweet suppression by RBP was independent of binding of riboflavin with its molecule. Yolk RBP, with minor structural differences compared with egg white RBP, also elicited a weaker sweet suppression. However, other commercially available proteins including ovalbumin, ovomucoid, beta-lactogloblin, myoglobin, and albumin did not substantially alter the sweetness of protein sweeteners. Because a prerinse with RBP reduced the subsequent sweetness of protein sweeteners, whereas the enzymatic activity of lysozyme and the elution profile of lysozyme on gel permeation chromatography were not affected by RBP, it is suggested that the sweet suppression is caused by an interaction of RBP with a sweet taste receptor rather than with the protein sweeteners themselves. The selectivity in the sweet suppression by RBP is consistent with the existence of multiple interaction sites within a single sweet taste receptor.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Maehashi</LastName><ForeName>Kenji</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Fermentation Science, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Tokyo 156-8502, Japan. maehashi@nodai.ac.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matano</LastName><ForeName>Mami</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Kondo</LastName><ForeName>Azusa</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Yamamoto</LastName><ForeName>Yasushi</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Udaka</LastName><ForeName>Shigezo</ForeName><Initials>S</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>2006</Year><Month>12</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Chem Senses</MedlineTA><NlmUniqueID>8217190</NlmUniqueID><ISSNLinking>0379-864X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004527">Egg Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026901">Membrane Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011956">Receptors, Cell Surface</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013549">Sweetening Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C019079">riboflavin-binding protein</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002645" MajorTopicYN="N">Chickens</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004527" MajorTopicYN="N">Egg Proteins</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D026901" MajorTopicYN="N">Membrane Transport Proteins</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011956" MajorTopicYN="N">Receptors, Cell Surface</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013549" MajorTopicYN="N">Sweetening Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013649" MajorTopicYN="N">Taste</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013652" MajorTopicYN="N">Taste Threshold</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>12</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>3</Month><Day>28</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>12</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17167172</ArticleId><ArticleId IdType="pii">bjl048</ArticleId><ArticleId IdType="doi">10.1093/chemse/bjl048</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement></list><tree><noCountry><name sortKey="Kondo, Azusa" sort="Kondo, Azusa" uniqKey="Kondo A" first="Azusa" last="Kondo">Azusa Kondo</name><name sortKey="Matano, Mami" sort="Matano, Mami" uniqKey="Matano M" first="Mami" last="Matano">Mami Matano</name><name sortKey="Udaka, Shigezo" sort="Udaka, Shigezo" uniqKey="Udaka S" first="Shigezo" last="Udaka">Shigezo Udaka</name><name sortKey="Yamamoto, Yasushi" sort="Yamamoto, Yasushi" uniqKey="Yamamoto Y" first="Yasushi" last="Yamamoto">Yasushi Yamamoto</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Maehashi, Kenji" sort="Maehashi, Kenji" uniqKey="Maehashi K" first="Kenji" last="Maehashi">Kenji Maehashi</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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