Riboflavin-binding protein exhibits selective sweet suppression toward protein sweeteners.
Identifieur interne : 000374 ( Main/Corpus ); précédent : 000373; suivant : 000375Riboflavin-binding protein exhibits selective sweet suppression toward protein sweeteners.
Auteurs : Kenji Maehashi ; Mami Matano ; Azusa Kondo ; Yasushi Yamamoto ; Shigezo UdakaSource :
- Chemical senses [ 0379-864X ] ; 2007.
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
Links to Exploration step
pubmed:17167172Le document en format XML
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<author><name sortKey="Maehashi, Kenji" sort="Maehashi, Kenji" uniqKey="Maehashi K" first="Kenji" last="Maehashi">Kenji Maehashi</name>
<affiliation><nlm:affiliation>Department of Fermentation Science, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Tokyo 156-8502, Japan. maehashi@nodai.ac.jp</nlm:affiliation>
</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>
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<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><nlm:affiliation>Department of Fermentation Science, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Tokyo 156-8502, Japan. maehashi@nodai.ac.jp</nlm:affiliation>
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<author><name sortKey="Matano, Mami" sort="Matano, Mami" uniqKey="Matano M" first="Mami" last="Matano">Mami Matano</name>
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<author><name sortKey="Kondo, Azusa" sort="Kondo, Azusa" uniqKey="Kondo A" first="Azusa" last="Kondo">Azusa Kondo</name>
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<author><name sortKey="Yamamoto, Yasushi" sort="Yamamoto, Yasushi" uniqKey="Yamamoto Y" first="Yasushi" last="Yamamoto">Yasushi Yamamoto</name>
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<author><name sortKey="Udaka, Shigezo" sort="Udaka, Shigezo" uniqKey="Udaka S" first="Shigezo" last="Udaka">Shigezo Udaka</name>
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<series><title level="j">Chemical senses</title>
<idno type="ISSN">0379-864X</idno>
<imprint><date when="2007" type="published">2007</date>
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<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="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" xml:lang="en"><term>Animals</term>
<term>Chickens</term>
<term>Molecular Weight</term>
</keywords>
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<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>
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<Title>Chemical senses</Title>
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<ArticleTitle>Riboflavin-binding protein exhibits selective sweet suppression toward protein sweeteners.</ArticleTitle>
<Pagination><MedlinePgn>183-90</MedlinePgn>
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<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>
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