Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

FEBS Lett. 2004 Aug 27;573(1-3):135-8. doi: 10.1016/j.febslet.2004.07.073.

Abstract

Curculin from Curculigo latifolia is a unique sweet protein that exhibits both sweet-tasting and taste-modifying activities. We isolated a gene that encodes a novel protein highly homologous to curculin. Using cDNAs of the previously known curculin (designated as curculin1) and the novel curculin isoform (curculin2), we produced a panel of homodimeric and heterodimeric recombinant curculins by Escherichia coli expression systems. It was revealed that sweet-tasting and taste-modifying activities were exhibited solely by the heterodimer of curculin1 and curculin2.

Publication types

  • Clinical Trial
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • Cloning, Molecular
  • Curculigo / chemistry*
  • Curculigo / genetics*
  • Dimerization
  • Disulfides / metabolism
  • Humans
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Plant Proteins / chemistry*
  • Plant Proteins / genetics
  • Plant Proteins / pharmacology*
  • Protein Structure, Quaternary
  • Protein Subunits / chemistry
  • Protein Subunits / genetics
  • Protein Subunits / pharmacology
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / pharmacology
  • Sweetening Agents / chemistry*
  • Sweetening Agents / pharmacology*
  • Taste / drug effects*
  • Taste / physiology

Substances

  • Disulfides
  • Plant Proteins
  • Protein Subunits
  • Recombinant Proteins
  • Sweetening Agents
  • curculin