This study aimed to investigate the residues, kinetics and dissipation patterns of kresoxim-methyl, (E)-methoxyimino[α-(o-tolyloxy)-o-tolyl]acetate, and trifloxystrobin, methyl(E)-methoxyimino-{(E)-α[1-(α,α,α-trifluoro-m-tolyl)ethylideneaminooxy]-o-tolyl}acetate". A simple and sensitive liquid chromatography-ultraviolet detection (LC-UV) method combined with the 'Quick Easy Cheap Effective Rugged and Safe' (QuEChERS) protocol was developed to quantify the levels of kresoxim-methyl and trifloxystrobin residues in citrus. More than 97% of the kresoxim-methyl and trifloxystrobin deposists gradually dissipated from the citrus peels within 15 days. The half-lives of kresoxim-methyl and trifloxystrobin in the peels were in the ranges of 2.63-2.66 d and 3.12-3.15 d, respectively, and the pattern of decline in the peels followed first-order kinetics. The kresoxim-methyl and trifloxystrobin residues in the pulp dissipated below the detectable level of 0.01 mg kg(-1) after 9 days. Kresoxim-methyl and trifloxystrobin were easily decomposed (T1/2 < 30 d), and the observed dissipation patterns could support the application of these two fungicides in the postharvest storage of citrus fruits.

The production of xylanase (TrxA) byTrichoderma reeseiJL-1 in solid-state fermentation (SSF) was optimized by response surface methodology (RSM). Results revealed that factors of concentration of added ammonium sulfate, and moisture content had significant effect on the TrxA production (P<0.05). The maximum xylanase activity (485.0 U/g U/g dry fermentation product) was obtained at 2.9% the ammonium sulfate by employing wheat bran as the solid substrate, 61.6% moisture content and 59.5-h fermentation, which was close to the predicted one, and was 1.8 times as high as that of the basic medium. The optimum temperature and pH for TrXA activity were 45°C and pH 5.0, respectively. Over 90% of xylanase activity was retained after treatment of the enzyme by preincubation over a pH range of 3.0-5.0 for 1 h at 25°C. TrxA exhibitedKmandVmaxvalues of 1.458mg/mL and 25.316 μmol/min/ml, respectively. In the presences of metal ions such as Mn2+the activity of the enzyme increased. Whereas strong inhibition of the enzyme activity was observed in the presences of Fe3+and Ca2+.

No abstract