pH-Dependent structural change in neoculin with special reference to its taste-modifying activity.
Neoculin has pH-dependent taste-modifying activity. This study found that neoculin changed pH-dependently in its tryptophan- and ANS-derived fluorescence spectra, while no such change occurred in a neoculin variant whose histidine residues were replaced with alanine. These results suggest that the sweetness of neoculin depends on structural change accompanying the pH change, with the histidine residues playing a key role.
Morita
Yuji
Y
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.
Nakajima
Ken-ichiro
K
Iizuka
Kisho
K
Terada
Tohru
T
Shimizu-Ibuka
Akiko
A
Ito
Keisuke
K
Koizumi
Ayako
A
Asakura
Tomiko
T
Misaka
Takumi
T
Abe
Keiko
K
D006801:Humans; D006863:Hydrogen-Ion Concentration; D010940:Plant Proteins / Q000737:chemistry* / Q000494:pharmacology*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013649:Taste / Q000187:drug effects* / Q000502:physiology; D014364:Tryptophan
D010940:Plant Proteins; C511659:neoculin protein, Curculigo latifolia; D014364:Tryptophan