Sulfur aroma precursor present in S-glutathione conjugate form: identification of S-3-(hexan-1-ol)-glutathione in must from Vitis vinifera L. cv. Sauvignon blanc

J Agric Food Chem. 2002 Jul 3;50(14):4076-9. doi: 10.1021/jf020002y.

Abstract

When Sauvignon blanc or Gros Manseng grape must was percolated through an immobilized gamma-glutamyltranspeptidase column, there was a significant increase in the concentration of S-3-(hexan-1-ol)-L-cysteine, the precursor of 3-mercaptohexan-1-ol, a compound that contributes to the varietal aroma of wines made from these grapes. Low- and high-resolution liquid secondary ion mass sepectrometry (LSIMS) analyses established the presence of S-3-(hexan-1-ol)-glutathione in Sauvignon blanc must. The identification of this compound suggests that the S-3-(hexan-1-ol)-L-cysteine in grapes is produced by the catabolism of S-3-(hexan-1-ol)-glutathione. As is the case in other plant or animal organisms, S-glutathione conjugates may be involved in certain detoxification systems in vines.

MeSH terms

  • Chromatography, Liquid
  • Enzymes, Immobilized
  • Glutathione / analogs & derivatives
  • Glutathione / analysis*
  • Glutathione / chemistry*
  • Mass Spectrometry
  • Odorants*
  • Sulfur / chemistry*
  • Vitis / chemistry*
  • Wine / analysis*
  • gamma-Glutamyltransferase

Substances

  • Enzymes, Immobilized
  • S-3-(hexan-1-ol)gluathione
  • Sulfur
  • gamma-Glutamyltransferase
  • Glutathione