2009 Fiscal Year Final Research Report
Studies on the elicitation of sweetness of sweet-tasting proteins.
| Project/Area Number |
19780074
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
MASUDA Tetsuya Kyoto University, 大学院・地球環境学堂, 助教 (80311744)
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| Project Period (FY) |
2007 – 2009
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| Keywords | 甘味タンパク質 / ソーマチン / 結晶構造解析 |
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| Research Abstract |
Thaumatin is an intensely sweet-tasting protein. To clarify the structure-sweetness relationships in thaumatin, we performed high resolution crystal structure analysis. The results showed that overall structures of these mutants are identical to that of plant thaumatin. However the subtle conformational changes in the main chain of K67 were induced by mutation of R82. The surface electric potential on the cleft containing side of the thaumatin was dramatically changed by the mutation at R82. These results demonstrated that the strict surface electrostatic potentials at the specific site formed by R82 and K67 are required for thaumatin sweetness
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[Journal Article] Cloning of the thaumatin I cDNA and characterization of recombinant thaumatin I secreted Pichia pastoris2007
Author(s)
Ide, N., Kaneko, R., Wada, R., Metha, A., Tamaki, S., Tsuruta, T., Fu j ita, Y., Masuda, T., Kitabatake, N.
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Journal Title
Biotechnol. prog 23
Pages: 1023-1030
Peer Reviewed
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