2010 Fiscal Year Final Research Report
Structural analysis and protein engineering for clarifying the molecular mechanism of the taste-modifying activity of neoculin
Project/Area Number |
21880015
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Research Category |
Grant-in-Aid for Research Activity Start-up
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Allocation Type | Single-year Grants |
Research Field |
Food science
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Research Institution | The University of Tokyo |
Principal Investigator |
NAKAJIMA Kenichiro The University of Tokyo, 大学院・農学生命科学研究科, 特任助教 (70554492)
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Project Period (FY) |
2009 – 2010
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Keywords | 味覚修飾活性 / ヒスチジン / NMR |
Research Abstract |
Neoculin is a sweet protein with taste-modifying activity converting sourness into sweetness. In this study, I performed a mutational analysis of neoculin to identify the important residue(s) for this pH-dependent activity. It revealed that one histidine residue in neoculin was critical for the activity. NMR analysis also performed to evaluate the structural-activity relationship of neoculin. It was found that the neoculin structurally changed between neutral and acidic pH.
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Research Products
(6 results)
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[Journal Article] Identification and Modulation of the Key Amino Acid Residue Responsible for the pH Sensitivity of Neoculin, a Taste-modifying Protein2011
Author(s)
Ken-ichiro Nakajima, Kanako Yokoyama, Taichi Koizumi, Ayako Koizumi, Tomiko Asakura, Tohru Terada, Katsuyoshi Masuda, Keisuke Ito, Akiko Shimizu-Ibuka, Takumi Misaka, Keiko Abe
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Journal Title
Peer Reviewed
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[Journal Article] Non-acidic Compounds Induce the Intense Sweet Taste of Neoculin, a Taste-modifying Protein2011
Author(s)
Ken-ichiro Nakajima, Ayako Koizumi, Kisho Iizuka, Keisuke Ito, Yuji Morita, Taichi Koizumi, Tomiko Asakura, Akiko Shimizu-Ibuka, Takumi Misaka, Keiko Abe
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Journal Title
Biosci.Biotechnol.Biochem. under review
Peer Reviewed
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