• Korean Journal of Environmental Agriculture
• /
• v.9 no.2
• /
• pp.97-103
• /
• 1990

In order to determine the major biochemical degradation factors of the two organophosphorus insecticides, diazinon and dursban, the activities of monooxygenase(m. o.) and ${\alpha}$, ${\beta}-esterase$ were studied in submerged soil under laboratory conditions at $30{\pm}1^{\circ}C$ The degradation rate of diazinon by microorganism showed 1.5 times higher than dursban. The m. o. activity increased from 12hrs and 3days after application of diazinon and dursban, respectively. But the ${\beta}-esterase$ activity showed maximum at one day after application of dursban and $5{\sim}8$ days after diazinon application. Also, the ${\beta}-esterase$ activity was about 10 times higher than ${\alpha}-esterase$. Hence, it was concluded that the biological degradation of diazinon was mainly attributed to m. o. activity and the degradation of dursban to ${\beta}-esterase$ activity.

• Korean journal of applied entomology
• /
• v.32 no.3
• /
• pp.265-270
• /
• 1993

The German cockroach(Blattelia germanica) population~ were successIVely selected with ch\orpyrifos and permethrin during the six generations. The resulting resistant $R_{chtorpenfos}$(Rc) and $R_{permethnn}$(Rp) stra.ins were studied to investigate the esterase activity by spectrophotometer, filter parper test, and electrophoresis. Esterase-$\alpha$ activities by filter paper test showed 2.65 and LBZ times higher in the Rc and Rp strains than the susceptible strain, respectively. ln the spectrophoLometer method, the esterase activit18s to $\alpha$-and $\beta$-naphthyl acetate were increased 2.34 and 5.28 times in the Rc than susceptible strain, and 1.48 and 2.92 times in the Rp Limn susceptible stram, respectlvely. Zymogram patterns of eslerase isozyme by agarose gel electrophoresis showed totally five bands. The Rc and Rp strains showed two additive bands as, Est-2 and Est-3, which were not shown in the susceptible strain. but the Rp strain dId not show Est-5 bands which was COlumon in the Rc and susceptible strams.

• The Korean Journal of Pesticide Science
• /
• v.11 no.3
• /
• pp.179-185
• /
• 2007

Esterase isozymes were investigated from digestive juice of M. saltuarius adults after pesticide treatment. Twelve esterase isozymes were separated on 12% native-PAGE gel and stained with three different substrates(${\alpha}$-naphthyl acetate, ${\beta}$-naphthyl acetate, and ${\alpha}$-naphthyl butyrate). Interestingly, the isozyme of Est1(${\alpha}$-naphthyl acetate) was strongly inhibited by the carbofuran and methomyl. The Est1 activity was completely inhibited by the chlorpyrifos and partially inhibited by methidation about 70 %. In addition, eserine suppressed esterase isozyme activities of Est1 about 70% and isozyme activities of Est2, Est3, and Est4 were weakly inhibited. ${\alpha}$-pinene did not suppressed esterase isozyme activities but activities of esterases were very weakly inhibited in camphor and bornyl acetate.

• The Korean Journal of Mycology
• /
• v.25 no.2 s.81
• /
• pp.85-90
• /
• 1997

The Isozyme activities of Lentinula edodes were studied as a preliminary study for genetic analysis after protoplast fusion. The presence of peroxidase, esterase, superoxide dismutase, acid phosphatase, alkaline phosphatase, alcohol dehydrogenase and ${\alpha}-amylase$ was examined. An intracellular buffer-soluble protein from the mycelia was used for enzyme analysis on nondenaturing polyacrylamide gels. The auxotrophs of Lentinula edodes were positive for peroxidase, esterase, superoxide dismutase and acid phosphatase. However, alkaline phosphatase, alcohol dehydrogenase and ${\alpha}-amylase$ were not detected. The esterase and peroxidase were not affected by the various culture age. Isozyme identification may be a useful tool after protoplast fusion.

• The Korean Journal of Pesticide Science
• /
• v.11 no.3
• /
• pp.171-178
• /
• 2007

Esterase isozymes were extracted from final instar larvae of M. saltuarius treated with selective diets and inhibitors. Twenty esterase isozymes were separated on 12% native-PAGE gel and stained with three different substrates(${\alpha}$-naphthyl acetate, ${\beta}$-naphthyl acetate, or ${\alpha}$-naphthyl butyrate). Interestingly, the isozymes of Est7(${\alpha}$-naphthyl acetate and ${\alpha}$-naphthyl butyrate) and Est6(${\beta}$-naphthyl acetate) were specifically activated in final instar larvae fed with the bark of Pinus koraiensis. However, we could not find any band from substrate ${\beta}$-naphthyl stearate. The esterase activities of Est3, Est6, and Est7 were inhibited by organophosphate and carbamate insecticides. In addition, The esterase activities of Est4, Est6, and Est7 were also inhibited by eserine. However, inhibition of esterase activities in methoprene, bornyl acetate, linal, cineol, and citral was not observed. However, It is necessary to reconfirm these results in vivo.

• Journal of the Korean Society of Tobacco Science
• /
• v.21 no.1
• /
• pp.49-56
• /
• 1999

Classification of esterase isozymes of the apterous green peach aphids (Myzus persicae Sulzer) collected in tobacco fields were investigated by the native polyacrylamide gel electrophoresis (PAGE). A total of twelve esterase bands were identified in adult apterous aphid, and the difference of enzyme band activity in the clones was observed at the first and second bands group. Esterases of green peach aphids reacted with specific substrate were more stained $\alpha$-naphthyl acetate than $\alpha$-naphthyl propionate, and $\alpha$-naphthyl acetate more than $\beta$-naphthyl acetate. Twelve esterases on the basis of inhibition by the three types of inhibitors (organophosphates: 2.5$\times$10$^{-3}$ M paraoxon, 4$\times$10$^{-3}$ M DFP; eserine sulfate : 2$\times$10$^{-3}$ M eserin; sulfhydryl reagents: 2$\times$10$^{-3}$ M p-HMB) were classified into three class, namely, cholinesterase (ChE) I, II, carboxylesterase (CE) and arylesterase (ArE), and these classes contained 3, 4, 3 and 2 isozymes, respectively.

• The Korean Journal of Zoology
• /
• v.39 no.2
• /
• pp.190-197
• /
• 1996

The optimal conditions and substrate specificity of whole body esterase (EST) activity, effects of inhibitors (Eserine, Paraoxon, p-HMB, DDVP, DFP) on the enzyme, and ontogenv of the isozymes were determined in Lucilio ilfustris Meisen. The optimal temperature was $45^{\circ}C$ regardless of kind of reacted substrate, $\alpha-naphthyl$ acetate $(\alpha-Nal,$ a.naphthvl butylate $(\alpha-N),$ and Pnaphthyl acetate $(\beta-Na),$ but the optimal pH showed some regioselectivitv to naphthvl group of the esters; PH 7.0 for Iform, pH 7.5 for a-form. The maximum reaction rate was recorded at about 2.5 $\times$ 10's M of PNa and etNa, but 1.0 $\times$ 10'S M of $\alpha-Nb.$ Among the five EST inhibitors tested, DDVP was the most powerful. However, distinction of the relative specificity of inhibitors between three body parts, head, thorax, and abdomen, was shouts, representing differences in the distribution and activity of isozvmes. Of 12 carboxyl-esterases (CE), 8 cholinesterases (ChE) and 2 arvlesterases (ArE) identified based on their inhibitor specificity throughout the development, two larval and prepupal stage specific ChEs, no pupal specific, and 2 CEs.2ChEs. and one ArE adult specific isozvmes were confirmed.

• Journal of Microbiology and Biotechnology
• /
• v.20 no.11
• /
• pp.1521-1523
• /
• 2010

Bioassay-guided fractionation of a methanol extract of Ganoderma lucidum gave a pure cholesterol esterase inhibitor. On the basis of spectroscopic analysis and comparison with data from the literature, the structure of this compound was identified as $5{\alpha},8{\alpha}$-epidioxyergosta-6,22-dien-$3{\bet}$-ol (compound I). This compound inhibited cholesterol esterase activity with an $IC_{50}$ value of $42{\mu}M$. Lineweaver-Burk plot analysis revealed that compound I is a noncompetitive inhibitor. The findings of this study suggest that compound I may be the active principle of the hypocholesterolemic effect of Ganoderma lucidum.

• The Korean Journal of Pesticide Science
• /
• v.11 no.2
• /
• pp.117-124
• /
• 2007

Esterase activity was observed after pesticides treatment in eggs of H. axyridis to select low toxicity pesticide. Egg esterases of H. axyridis were examined using an esterase substrate(${\alpha}$-naphthyl acetate). Three esterase isozymes were detected and the activities were inhibited by organophosphorus insecticide (Chlorpyrifos and Phenthoate), organochlorine insecticide(Methidation), triazole fungicide(Hexaconazole and Triflumizole), and pyrimidine fungicide(Nuarlmol). Fecundity and hatchability in adults and eggs of H. axyridis were examined on selected pesticides. Fecundity and hatchability were significantly reduced from H. axyridis adults and eggs treated with the pesticides and the fungicides showed strong inhibition of esterase isozymes activities. However, we also observed the pesticides and the fungicides showed low or non-inhibition of esterase isozymes activities affected on fecundity and hatchability in adults and eggs.

• Microbiology and Biotechnology Letters
• /
• v.30 no.4
• /
• pp.305-311
• /
• 2002

Acetyl xylan esterase gene (AXE) from Aspergillus ficuum was cloned and its Pichia expression plasmid, pPICZ$\alpha$C-AXE (4.6 kb), was constructed, in which the AXE gene was under the control of the AOXI promoter and connected downstream of mating factor u-1 signal sequence. The plasmid linearized by Sacl was integrated into the 5'AOXI region of the chromosomal DNA of P. pastoris. In the flask batch culture of P. pastoris transformant on methanol medium, the cell concentration and total AXEase activity reached at 6.0 g-dry cell weight/1 and 77 unit/ml after 36 h cultivation, respectively. In the fed-batch culture employing the optimized methanol and histidine feeding strategy, the cell concentration and total AXEase activity were significantly increased to about 97 g-dry cell weight/1 and 930 unit/ml. Most of AXEase activity (>90%) was found in the extracellular medium and the majority of extracellular protein (>80%) was AXEase enzyme (33.5 kDa). This result means that about 9.8 g/1 of AXEase protein was produced in the extracellular medium.