Developments in biotechnological production of sweet proteins.
Identifieur interne : 000393 ( Main/Exploration ); précédent : 000392; suivant : 000394Developments 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
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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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></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17189164</PMID><DateCompleted><Year>2007</Year><Month>01</Month><Day>17</Day></DateCompleted><DateRevised><Year>2006</Year><Month>12</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1389-1723</ISSN><JournalIssue CitedMedium="Print"><Volume>102</Volume><Issue>5</Issue><PubDate><Year>2006</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Journal of bioscience and bioengineering</Title><ISOAbbreviation>J Biosci Bioeng</ISOAbbreviation></Journal><ArticleTitle>Developments in biotechnological production of sweet proteins.</ArticleTitle><Pagination><MedlinePgn>375-89</MedlinePgn></Pagination><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></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kitabatake</LastName><ForeName>Naofumi</ForeName><Initials>N</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Japan</Country><MedlineTA>J Biosci Bioeng</MedlineTA><NlmUniqueID>100888800</NlmUniqueID><ISSNLinking>1347-4421</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013549">Sweetening Agents</NameOfSubstance></Chemical><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></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001419" MajorTopicYN="N">Bacteria</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001709" MajorTopicYN="Y">Biotechnology</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D030821" MajorTopicYN="N">Plants, Genetically Modified</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><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><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>04</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>06</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>12</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>1</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>12</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17189164</ArticleId><ArticleId IdType="pii">S1389-1723(06)70680-6</ArticleId><ArticleId IdType="doi">10.1263/jbb.102.375</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région du Kansai</li></region><settlement><li>Kyoto</li></settlement><orgName><li>Université de Kyoto</li></orgName></list><tree><noCountry><name sortKey="Kitabatake, Naofumi" sort="Kitabatake, Naofumi" uniqKey="Kitabatake N" first="Naofumi" last="Kitabatake">Naofumi Kitabatake</name></noCountry><country name="Japon"><region name="Région du Kansai"><name sortKey="Masuda, Tetsuya" sort="Masuda, Tetsuya" uniqKey="Masuda T" first="Tetsuya" last="Masuda">Tetsuya Masuda</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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