Developments in biotechnological production of sweet proteins.
Identifieur interne : 000373 ( Main/Curation ); précédent : 000372; suivant : 000374Developments in biotechnological production of sweet proteins.
Auteurs : Tetsuya Masuda [Japon] ; Naofumi KitabatakeSource :
- Journal of bioscience and bioengineering [ 1389-1723 ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
- biosynthèse : Protéines recombinantes, Protéines végétales.
- métabolisme : Bactéries, Champignons.
- Biotechnologie, Relation structure-activité, Végétaux génétiquement modifiés, Édulcorants.
English descriptors
- KwdEn :
- MESH :
- chemical , biosynthesis : Plant Proteins, Recombinant Proteins.
- metabolism : Bacteria, Fungi.
- Biotechnology, Plants, Genetically Modified, Structure-Activity Relationship, Sweetening Agents.
Abstract
Most proteins are tasteless and flavorless, while some proteins elicit a sweet-taste response on the human palate. Six proteins, thaumatin, monellin, mabinlin, brazzein, egg lysozyme, and neoculin (previously considered as curculin) have been identified as sweet-tasting proteins. However, no common features among them have been observed. Herein, recent advances in the research of sweet-tasting proteins and the production of such proteins by biotechnological approaches are reviewed. Information on the structure-sweetness relationship for these proteins would help not only in the clarification of the mechanism of interaction of sweet-tasting proteins with their receptors, but also in the design of more effective low-calorie sweeteners.
DOI: 10.1263/jbb.102.375
PubMed: 17189164
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pubmed:17189164Le document en format XML
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<author><name sortKey="Masuda, Tetsuya" sort="Masuda, Tetsuya" uniqKey="Masuda T" first="Tetsuya" last="Masuda">Tetsuya Masuda</name>
<affiliation wicri:level="1"><nlm:affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.</nlm:affiliation>
<country xml:lang="fr">Japon</country>
<wicri:regionArea>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011</wicri:regionArea>
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<author><name sortKey="Kitabatake, Naofumi" sort="Kitabatake, Naofumi" uniqKey="Kitabatake N" first="Naofumi" last="Kitabatake">Naofumi Kitabatake</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacteria (metabolism)</term>
<term>Biotechnology (MeSH)</term>
<term>Fungi (metabolism)</term>
<term>Plant Proteins (biosynthesis)</term>
<term>Plants, Genetically Modified (MeSH)</term>
<term>Recombinant Proteins (biosynthesis)</term>
<term>Structure-Activity Relationship (MeSH)</term>
<term>Sweetening Agents (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Bactéries (métabolisme)</term>
<term>Biotechnologie (MeSH)</term>
<term>Champignons (métabolisme)</term>
<term>Protéines recombinantes (biosynthèse)</term>
<term>Protéines végétales (biosynthèse)</term>
<term>Relation structure-activité (MeSH)</term>
<term>Végétaux génétiquement modifiés (MeSH)</term>
<term>Édulcorants (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Plant Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
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<term>Protéines végétales</term>
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<term>Champignons</term>
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<term>Plants, Genetically Modified</term>
<term>Structure-Activity Relationship</term>
<term>Sweetening Agents</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Biotechnologie</term>
<term>Relation structure-activité</term>
<term>Végétaux génétiquement modifiés</term>
<term>Édulcorants</term>
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<front><div type="abstract" xml:lang="en">Most proteins are tasteless and flavorless, while some proteins elicit a sweet-taste response on the human palate. Six proteins, thaumatin, monellin, mabinlin, brazzein, egg lysozyme, and neoculin (previously considered as curculin) have been identified as sweet-tasting proteins. However, no common features among them have been observed. Herein, recent advances in the research of sweet-tasting proteins and the production of such proteins by biotechnological approaches are reviewed. Information on the structure-sweetness relationship for these proteins would help not only in the clarification of the mechanism of interaction of sweet-tasting proteins with their receptors, but also in the design of more effective low-calorie sweeteners.</div>
</front>
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<DateCompleted><Year>2007</Year>
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<Day>17</Day>
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<DateRevised><Year>2006</Year>
<Month>12</Month>
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<Issue>5</Issue>
<PubDate><Year>2006</Year>
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<Title>Journal of bioscience and bioengineering</Title>
<ISOAbbreviation>J Biosci Bioeng</ISOAbbreviation>
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<ArticleTitle>Developments in biotechnological production of sweet proteins.</ArticleTitle>
<Pagination><MedlinePgn>375-89</MedlinePgn>
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<Abstract><AbstractText>Most proteins are tasteless and flavorless, while some proteins elicit a sweet-taste response on the human palate. Six proteins, thaumatin, monellin, mabinlin, brazzein, egg lysozyme, and neoculin (previously considered as curculin) have been identified as sweet-tasting proteins. However, no common features among them have been observed. Herein, recent advances in the research of sweet-tasting proteins and the production of such proteins by biotechnological approaches are reviewed. Information on the structure-sweetness relationship for these proteins would help not only in the clarification of the mechanism of interaction of sweet-tasting proteins with their receptors, but also in the design of more effective low-calorie sweeteners.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Masuda</LastName>
<ForeName>Tetsuya</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.</Affiliation>
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<Author ValidYN="Y"><LastName>Kitabatake</LastName>
<ForeName>Naofumi</ForeName>
<Initials>N</Initials>
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<Language>eng</Language>
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<MedlineJournalInfo><Country>Japan</Country>
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<ISSNLinking>1347-4421</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D013549">Sweetening Agents</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C090521">brazzein protein, Pentadiplandra brazzeana</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C002541">monellin protein, Dioscoreophyllum cumminsii</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>53850-34-3</RegistryNumber>
<NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance>
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<MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013549" MajorTopicYN="Y">Sweetening Agents</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<NumberOfReferences>152</NumberOfReferences>
</MedlineCitation>
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