• The Korean Journal of Pesticide Science
• /
• v.4 no.2
• /
• pp.63-68
• /
• 2000

This study was conducted to investigate insecticidal mechanisms of the new insecticides DBI-1015 and DBI-3204 with label compounds of chitin precursors, [$^{14}C$] N-acetylglucosamine and [$^{14}C$] UDP-N-acetylglucosamine in Spodoptera litura. The concentrations of the insecticides for incorporation of chitin precursors into chitin were founded to be functional relationship. The result of in vivo test, $I_{50}$ (ppm) of the DBI-1015, DBI-3024 and diflubenzuron to [$^{14}C$] N-acetylglucosamine were 0.57, 0.89 and 0.26 ppm respectively, and to [$^{14}C$] UDP-N-acetylglucosaminen were 0.99, 0.53 and 0.45 ppm respectively. in vitro test of DBI-1015, DBI-3024 and diflubenzuron by integument fragments, the incorporation rate in the cuticle were low, however, $40{\sim}60%$ inhibitions were observed at $2{\mu}M$ when compared to the untreated control.

• KSBB Journal
• /
• v.7 no.1
• /
• pp.15-20
• /
• 1992

The use of Jerusalem artichoke containing $\beta$-1, 2-fructose oligomer in the production of sorbitol that is used as food additives and precursor for the L-sorbose has been studied. Coimmobilization of both inulinase and oxidoreductase was considered for the simultaneous reaction for hydrolysis of inulin and conversion of glucose and fructose liberated from inulin to sorbitol. Both inulinase and oxidoreductase were immobilized in chitin(5%, w/v) and K-carrageenan(4%, w/v), The activity of oxidoreductase was specified by permeabilization of Zymomonas mobilis cell with 0.2% CTAB(Cetyltrimethylammonlumbromide). The use of inulinase for hydrolysis of inulin resulted in 36.65g/l of glucose and 85.32g/1 of fructose respectively. These are valuable substrates for sorbitol production. Using these hydrolyzates, accumulation of 35.64g/l for sorbitol occurred at $38^{\circ}C$ and pH6.2. When permeabilized cells and inulinase were coimmobilized, sorbitol produced at 30.15g/l although it is low compared with 35.64g/l in separated reactor system.