Efficient decontamination of zearalenone, the mycotoxin of cereal pathogen, by transgenic yeasts through the expression of a synthetic lactonohydrolase gene

Appl Microbiol Biotechnol. 2005 Jun;67(6):838-44. doi: 10.1007/s00253-004-1816-y. Epub 2005 Jan 4.

Abstract

Zearalenone (ZEN), an estrogenic mycotoxin produced by several Fusarium species, is converted to a non-estrogenic product by a detoxifying enzyme of Clonostachys rosea. Previously, we investigated whether recombinant Saccharomyces cerevisiae carrying this detoxification gene, zhd101, can remove 2 microg ml(-1) of ZEN in a liquid culture. Although the transgenic yeasts eliminated most of the ZEN, they also converted a significant amount to a poor substrate, beta-zearalenol, which remained in the medium. In this study, we synthesized a codon-optimized zhd101 gene and investigated whether the transgenic yeast strain can overcome the problem of insufficient detoxification of ZEN. Importantly, within 48 h of incubation at 28 degrees C or 8 h of incubation at 37 degrees C, the transgenic yeasts completely eliminated 2 microg ml(-1) of ZEN in the medium without accumulating even a trace amount of beta-zearalenol. The result suggests that incomplete ZEN detoxification attributed to the action of an endogenous yeast beta-reductase can be overcome by simply increasing the expression of the detoxifying gene.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biodegradation, Environmental
  • Decontamination / methods
  • Molecular Sequence Data
  • Plasmids
  • Protein Engineering*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / pharmacology
  • Saccharomyces cerevisiae / growth & development
  • Saccharomyces cerevisiae / metabolism*
  • Sequence Alignment
  • Zearalenone / antagonists & inhibitors*
  • Zeranol / analogs & derivatives
  • Zeranol / metabolism

Substances

  • Recombinant Proteins
  • zearalenol
  • Zearalenone
  • Zeranol