Fate of Cry1Ab protein in agricultural systems under slurry management of cows fed genetically modified maize (Zea mays L.) MON810: a quantitative assessment

J Agric Food Chem. 2011 Jul 13;59(13):7135-44. doi: 10.1021/jf200854n. Epub 2011 Jun 8.

Abstract

The objective of the study was to track the fate of recombinant Cry1Ab protein in a liquid manure field trial when feeding GM maize MON810 to dairy cows. A validated ELISA was applied for quantification of Cry1Ab in the agricultural chain from GM maize plants, feed, liquid manure and soil to crops grown on manured fields. Starting with 23.7 μg of Cry1Ab g(-1) dry weight GM maize material, a rapid decline of Cry1Ab levels was observed as 2.6% and 0.9% of Cry1Ab from the GM plant were detected in feed and liquid manure, respectively. Half of this residual Cry1Ab persisted during slurry storage for 25 weeks. After application to experimental fields, final degradation of Cry1Ab to below detectable levels in soil was reported. Cry1Ab exhibited a higher rate of degradation compared to total protein in the agricultural processes. Immunoblotting revealed a degradation of the 65 kDa Cry1Ab into immunoreactive fragments of lower size in all analyzed materials.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agriculture / methods
  • Animal Feed / analysis*
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / analysis*
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / pharmacokinetics
  • Endotoxins / analysis*
  • Endotoxins / metabolism
  • Endotoxins / pharmacokinetics
  • Hemolysin Proteins / analysis*
  • Hemolysin Proteins / metabolism
  • Hemolysin Proteins / pharmacokinetics
  • Manure / analysis*
  • Plants, Genetically Modified / genetics*
  • Recombinant Proteins / analysis*
  • Soil / analysis
  • Zea mays / genetics*
  • Zea mays / growth & development

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Endotoxins
  • Hemolysin Proteins
  • Manure
  • Recombinant Proteins
  • Soil
  • insecticidal crystal protein, Bacillus Thuringiensis