Enhancement of volatile thiol release of Saccharomyces cerevisiae strains using molecular breeding

Appl Microbiol Biotechnol. 2013 Jul;97(13):5893-905. doi: 10.1007/s00253-013-4739-7. Epub 2013 Feb 20.

Abstract

Cysteine-conjugated volatile thiols are powerful aromatic compounds that contribute to the fruity notes of many white wines and especially Sauvignon Blanc. Genetic selection programs of wine yeast starters able to produce more volatile thiols constitute, therefore, an important goal for the wine industry. Recent investigations on yeast metabolism suggested that the ß-lyase Irc7p and the control of its gene expression by nitrogen catabolite repression constitute a rational way for yeast genetic improvement. This work demonstrates that the use of a natural ure2 mutation can be used to design wine starters with an enhanced capacity of volatile thiols production. By applying backcrosses driven by molecular markers, this allelic form was introduced in different starter backgrounds. Our investigations demonstrate that the ure2 inheritance is able to enhance the production of 4MMP (recently renamed 4MSP) and 3MH (recently renamed 3SH). For 4MMP, this effect depends of the presence of the allele IRC7LT encoding a long form of the Irc7 protein. Moreover, a correlation in between the expression level of this allelic form and 4MMP production was found within industrial starters. All together, these results emphasised the use of molecular breeding for improving quantitative traits of industrial strains without the use of genetically modifying strategies.

MeSH terms

  • Crosses, Genetic
  • DNA Shuffling*
  • Glutathione Peroxidase / genetics
  • Metabolic Engineering / methods*
  • Metabolic Networks and Pathways / genetics*
  • Prions / genetics
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / genetics
  • Sulfhydryl Compounds / metabolism*

Substances

  • Prions
  • Saccharomyces cerevisiae Proteins
  • Sulfhydryl Compounds
  • Glutathione Peroxidase
  • URE2 protein, S cerevisiae