Studies on the elicitation of sweetness of sweet-tasting proteins.

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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