, 2005). It is thus expected that the incorporation of this detoxification mechanism into highly Fusarium susceptible cultivars will lead to

an increase of the D3G/DON ratio also in natural infection. A DON-glucosyltransferase gene from barley has been recently identified check details ( Schweiger et al., 2010), which might be utilized in transgenic approaches to increase Fusarium resistance by overexpression of this gene. Yet, the fate of D3G after digestion by mammals is largely unknown, and the concern is that this compound may be cleaved to DON and glucose (reviewed by Berthiller et al., 2009b). Another conjugated Fusarium mycotoxin, zearalenone-14-β-d-glucoside (Z-14-G), was shown to produce zearalenone (ZEN) in the digestive tract of swine ( Gareis et al., 1990). This reaction was believed to be largely due to the activity of the gut microbiota of animals ( Gareis, 1994). In this work, the stability of D3G towards hydrochloric acid, artificial stomach juice, artificial non-microbial gut juice, a variety of enzymes and intestinal bacteria is evaluated and discussed. D3G was isolated from wheat plants treated with DON at anthesis, as previously described

(Berthiller et al., 2005). The mycotoxin DON was purchased from Romer Labs (Tulln, Austria) as calibrant in acetonitrile. HPLC grade find more methanol was purchased from J.T. Baker (Deventer, The Netherlands), MS grade ammonium

acetate from Sigma–Aldrich (St. Louis, MO, USA). Resveratrol LC grade water was produced with a Millipore Milli-Q plus system (Molsheim, France) after reverse osmosis. Possible hydrolysis of D3G to DON was tested with the following solutions: (1) purified water; (2) 0.02 M HCl (pH approx. 1.7); (3) 0.2 M HCl (pH approx. 0.7); (4) artificial stomach juice (540 mg Helo-acid, Rösch und Handel, Wien, Austria, containing pepsin, in 0.02 M HCl); (5) artificial, non-microbial, gut juice (70 mg Kreon 40,000, Solvay Pharma, Klosterneuburg, Austria, containing 40 mg pancreatin (4000 lipase units, 2500 amylase units, 160 protease units) in 1 g/L NaHCO3, pH 8.0); (6) almond β-glucosidase (EC 3.2.1.21, Sigma–Aldrich G4511, 1 U/mL in 0.1 N sodium acetate buffer, pH-value 5.0); (7) β-glucuronidase (EC 3.2.1.31, isolated from Helix pomatia, Sigma–Aldrich G7396, 10 U/mL in 0.1 N sodium acetate buffer, pH 5.0); (8) cellulase (EC 3.2.1.4, from Trichoderma reesei, Sigma–Aldrich C8546, 1 U/mL in 0.1 N sodium acetate buffer, pH 5.0); (9) cellobiase (EC 3.2.1.21, isolated from Aspergillus niger, Sigma–Aldrich 49291, 130 mU/mL in 50 mM sodium phosphate buffer containing 5 mM EDTA, pH 6.0).