• Journal of Microbiology and Biotechnology
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• v.5 no.6
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• pp.335-340
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• 1995

Two types of Rhizoctonia solani esterases induced by cutin hydrolysate were partially purified by ammonium sulfate precipitation and gel filtration. The esterase I with hydrolyzing activity toward both ${\rho}-ni-trophenyl$ butyrate and ${\rho}-nitrophenyl$ palmitate and the esterase II with hydrolyzing activity toward only ${\rho}-ni-trophenyl$ butyrate were inhibited by ebelactone B, an esterase inhibitor produced by actinomycetes with $IC_{50}$ values of 0.01 and $0.09{\;}\mu\textrm{g}/l$, respectively. Spraying on rice seedling with ebelactone B at a concentration of $30{\;}\mu\textrm{g}/ml$ completely suppressed infection by R. solani. Ebelactone B could not protect the wounded rice seedling and did not show any inhibitory effect on the mycelial growth at a concentration of 1 mg/ml. These results indicate that ebelactone B, an esterase inhibitor protects rice plants from infection with R. solani by inhibition of penetration, not through fungitoxic or fungicidal effect.

• Korean Journal of Microbiology
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• v.27 no.2
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• pp.139-146
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• 1989

The mechanisms and metabolic products involved in the degradation of an organophosphate insecticide, diazinon, were studied in submerged paddy soil under the laboratory condition at $30^{\circ}C$. Diazinon abatement in non-sterilized soil was more rapid than indicating microbial participation in diazinon in soil. One-half of the original applications was lost in 2 days and less than 5% remained after 7 days. During the same period, dizinon applications increased tha microbial populations in accordance with the monooxygenase and esterase activities in soil. These results suggest that the microbiological factors develop in soil following diazinon application. The esterase and monooxygenase-catalyzing degradation products of diazinon were isolated and tentatively identified by mass spectrometryas 2-isopropyle-6-methyl-4-hydroxy pyrimidine, diazoxon, hydroxydiazinon, and sulfotep.

• 한국생물공학회:학술대회논문집
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• 2000.04a
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• pp.501-504
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• 2000

The purification of a thermostable esterase expressed in Escherichia coli was investigated using thermoprecipitation of unclarified cell homogenates followed by after applying the heat-treated lysate to phenyl-sepharose column, and elution with detergent. Heat treatment at $70^{cdot}C$ was capable of removing to E. coli proteins. Specially, the thermoprecipitation with 15% polyethylene glycol 8000 can remove host proteins and nucleic acids efficiently. Various detergents were used to recover the esterase, which was strongly bound to phenyl-sepharose resin. Triton X-100, non-ionic detergent, was found to be the most efficient of all tested detergents.

• The Korean Journal of Ecology
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• v.21 no.6
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• pp.771-777
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• 1998

Aqueous extracts of Pinus rigida changed the electrophoretic patterns of total proteins and of hydrolytic enzymes such as peroxidase, esterase and amylase during the germination of radish (Raphanus sativus var. hortensis for. acanthiformis). When the extract treatment was finished, at the late stage of radish germination, aqueous extracts of P. rigida had suppressed the expression of 24 KD and 60 KD proteins. the extract induced new isozyme bands, indicating concomitant activity of peroxidases, esterase activities were stimulated in the cathodic region. The activity of amylase was enhanced by the extract.

• The Korean Journal of Pesticide Science
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• v.8 no.1
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• pp.16-21
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• 2004

A series of experiments was conducted to determine the toxicities of thiodicarb on the six lepidopterous pests (Pseudaletia separata, Plutella xylostella, Palpita indica, Spodoptera exigua, Helicoverpa assulta, Spodoptera litura) and to elucidate factors insecticidal effects mechanism of thiodicarb. Thiodicarb was very effective against six lepidopterous young larvae, but less effective to the old larvae and it acted slowly. Thiodicarb inhibited acetylcholinesterase and glutathione S-transferase activities, but not inhibit esterase activity.

• Journal of The Korean Society of Grassland and Forage Science
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• v.12 no.1
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• pp.71-76
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• 1992

Starch gel electrophoresis was used to examine the banding pattern of Esterase isozyme in the leaf, root-nodule and seedling of four wild legume species, Trifolim repense, Glycine soja, Phaseolus nipponensis and Vigna uexillata. The number of band, enzyme activity and migrating rate of esterase isozyme varies depending on the species and tissues of legume plants. The isozyme banding pattern in the cotyledon and radicle of T. repense showed same pattern, however, the number of band were varible among the cotyledon of G. soja, P. nipponensis and V. vexzllata, respectively. Est-1 in the leaf of G. soja, V, vexillata. root-nodule of G. soja and seedling of V. vexillata expreesed the highest enzyme activity. The Est-1 showed the rapidest migrating rate among the isozymes.

• KSBB Journal
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• v.15 no.3
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• pp.313-317
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• 2000

In this paper enantioselective production of levofloxacin by porcine liver esterase was investigated, To enhance the produc0-tivity various factors which affect the enzyme activity and the enantioselectivity were optimized, In terms of temperature and pH 45$^{\circ}C$ and 4.8 were found to be the best conditions for enzyme reaction. Addition of ofloxacin butyl ester the substrate at the concentration of 5 g/L was desirable to avoid the product inhibition and the activity of porcine liver esterase was maintained up to 72 hours.In addition to enhance the availability of substrate effect of solvent was also examined. It was found that the application of 5% (v/v) of acetone acetonitrile and dimethylsulfoxide did not increase the conversion of substrate and the presence of 5%(v/v) butanol inhibited the enzyme activity significantly.

• International Journal of Industrial Entomology and Biomaterials
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• v.14 no.1
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• pp.1-7
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• 2007

In order to find out the appropriate parents for the breeding programme, twelve bivoltine and three multivoltine silkworm breeds were evaluated on the basis of multivariate selection index and isozyme analysis. Of which, four [CSR2, D6 (P), SK3, SK4] bivoltine and two multivoltine (Nistari, Cambodge) breeds were selected and breeding initiated to develop higher survival bivoltine silkworm breed suitable for tropical conditions. Among two isozyme (Esterase and acid phosphatase) analyzed, only esterase exhibited polymorphism among the bivoltine breeds. No polymorphism was observed among multivoltine in respect of esterase as well as acid phosphatase.

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

• Journal of Microbiology and Biotechnology
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• v.18 no.12
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• pp.1908-1914
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• 2008

An alkaliphilic bacterium, Bacillus clausii SKAL-16, was isolated from soil that had been contaminated with vegetable oil. The optimal pH and general pH range for bacterial growth was 8, and 7 to 10, respectively. The bacterium could grow on tributyrin and glycerol, but could not grow on acetate and butyrate. The SKAL-16 strain excreted butyric acid during growth on tributyrin, and selectively ingested glycerol during growth on a mixture of butyric acid and glycerol. The SKAL-16 generated intracellular lipase, but did not produce esterase and extracellular lipase. The DNA fragment amplified with the chromosomal DNA of SKAL-16 and primers designed on the basis of the esterase-coding gene of Bacillus clausii KSM-KI6 was not identical with the esterase-coding gene contained in the GenBank database. Pyruvate dehydrogenase, isocitrate dehydrogenase, and malate dehydrogenase activities were detected in the cell-free extract (crude enzyme).