pH-Dependent structural change in neoculin with special reference to its taste-modifying activity

Biosci Biotechnol Biochem. 2009 Nov;73(11):2552-5. doi: 10.1271/bbb.90524. Epub 2009 Nov 7.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Humans
  • Hydrogen-Ion Concentration
  • Plant Proteins / chemistry*
  • Plant Proteins / pharmacology*
  • Spectrometry, Fluorescence
  • Spectrophotometry, Ultraviolet
  • Taste / drug effects*
  • Taste / physiology
  • Tryptophan

Substances

  • Plant Proteins
  • neoculin protein, Curculigo latifolia
  • Tryptophan