• Korean journal of applied entomology
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• v.29 no.3
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• pp.170-175
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• 1990

These studies were conducted to examine the mechanism of acaricidal resistance in the twospotted spider mite (Tetranychus urticae Koch). The resistant strains were obtained by succssive selection of five acaricides including carbonphenothion and ethion of organophosphorus compound, dicofol of organochlorine compound, cyhexatin of compound and biphenthrin of synthetic pyrethroid. Esterase isozymes were separated by polyacrlyamide gel susceptible strains. The differences of the esterase isozymes of the resistant strains were Est. 1, Est. 3 in the carbonphenothion-selected strain, Est. 3 in the ethion- and the cyhexatin-selected strains, Est. 1, Est. 3, Est. 7 in the dicofol-selected strain, Est. 7 in the biphenthrin-selected strain as compared to the susceptible strain. With the difference of electrophoretic bands and their activities, esterases were related to the resistant mechanism of tested acaricides.

• The Korean Journal of Mycology
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• v.16 no.2
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• pp.95-100
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• 1988

Isozyme band patterns were investigated by isoeletric focusing Esterase and Leucine amino peptidase of Pleurotus spp. in Korea. Esterase patterns of mycelia and fruitbody were distinquished. However, those of primordia, cap and stem were similar. Interspecies differences of Pleurotus ostreatus, P. cornucopiae and P. florida of Esterase zymogram were found. Species identification by electrophoretic zymogram may be a role as an additional taxonomic tool.

• Journal of Plant Biology
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• v.36 no.1
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• pp.51-57
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• 1993

The microtuber was efficiently formed on SH medium containing 9% sucrose from the in vitro propagated shoot of potato (Solanum tuberosum cv. Sumi). In order to investigate gene expression depending on the development stage of microtuber, we examined the changes of peroxidase and esterase activities, and their isozyme patterns as well. Peroxidase and esterase activities were the highest at the 7 day-culture of the microtuber and subsequently decreased on the stage of microtuberization, whereas esterase activity increased at the stage of 60 day-culture. However, their activities in the ordinary tuber were higher than those of 60 day-cultured microtuber. In addition, in the peroxidase isozyme pattern two new bands of pI 7.05 and pI 4.65 were appeared at the 15- day and 60 day-cultures, respectively, as shown by isoelectric focusing. Various bands in the sterase isozyme pattern were shown at the 7 day-culture, and the band patterns were a large difference, comparing those of shoot and tuber. New bands in the esterase isozyme pattern also appeared at the 15 day- (pI4.52) and 60 day-cultures (pI 4.48). These results suggest that the changes of peroxidase and esterase activities and isozyme patterns are an important factor in the differentiation and development of potato.

• Journal of the korean academy of Pediatric Dentistry
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• v.34 no.2
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• pp.285-291
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• 2007

The purpose of this study was to evaluate the effect of collagenase and esterase on the microtensile bond $strength({\mu}TBS)$ in dentin bonding. After resin composites were bonded to occlusal dentin. ${\mu}TBS$ specimens were formed and stored in PBS, collagenase, or esterase solution After 4-week storage, ${\mu}TBS$ was determined and, the results were as follows : 1. ${\mu}TBS$ values of Single Bond 2 were lower than those of Clearfil SE Bond for all storage medium (p<0.05). 2. In Single Bond 2 group, collagenase solution lowered bond strength more than PBS and esterase solution (p>0.05). 3. In Clearfil SE Bond group, esterase solution lowered bond strength more than PBS(p>0.05). Collagenase solution lowered bond strength more than esterase solution(p>0.05) and PBS(p<0.05).

• Korean Journal of Veterinary Research
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• v.4 no.1
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• pp.15-17
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• 1964

Scabby burley collected in Kyong Sang Nam Do fed to healthy dogs, age less than 2 years, old and determined the Choline-Esterase Activity in blood of dogs. The results obtained in this investigation are summarized as follows. 1. Choline-Esterase Activity in the blood of dogs fed Scabby barley has been decreased. 2. The poisionous component of the Scabby barley thought to be Anticholinesterase.

• BMB Reports
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• v.40 no.4
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• pp.588-594
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• 2007

A novel hot spring thermophile, Anoxybacillus gonensis A4 (A. gonensis A4) was investigated in terms of capability of tributyrin degradation and characterization of its thermostable esterase activity by the hydrolysis of p-nitrophenyl butyrate (PNPB). It was observed that A. gonensis A4 has an esterase with a molecular weight of 62 kDa. The extracellular crude preparation was characterized in terms of substrate specificity, pH and temperature optima and stability, kinetic parameters and inhibition/activation behaviour towards some chemicals and metal ions. Tributyrin agar assay showed that A. gonensis A4 secreted an esterase and $V_{max}$ and $K_m$ values of its activity were found to be 800 U/L and 176.5 ${\mu}M$, respectively in the presence of PNPB substrate. The optimum temperature and pH, for A. gonensis A4 esterase was $60-80^{\circ}C$ and 5.5, respectively. Although the enzyme activity was not significantly changed by incubating crude extract solution at $30-70^{\circ}C$ for 1 h, the enzyme activity was fully lost at $80^{\circ}C$ for same incubation period. The pH-stability profile showed that original crude esterase activity increased nearly 2-fold at pH 6.0. The effect of some chemicals on crude esterase activity indicated that A. gonensis A4 produce an esterase having serine residue in active site and -SH groups were essential for its activity.

• The Korean Journal of Mycology
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• v.14 no.2
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• pp.93-99
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• 1986

Isozyme patterns of leucine aminopeptidase, esterase and protein from 16 isolates of Ganoderma lucidum were observed by electrophoresis for characterization of the isolates. Even in the same isolate, the patterns of the isozymes from mycelium and cap were different. The esterase patterns from the mycelium could differentiate the isolates. Of 16 isolates, four isolates showed identical patterns. It was assumed that these had the same genetic background.

• Journal of Microbiology and Biotechnology
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• v.30 no.2
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• pp.216-225
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• 2020

An esterase gene, estA1, was cloned from Alteromonas sp. 39-G1 isolated from the Beaufort Sea. The gene is composed of 1,140 nucleotides and codes for a 41,190 Da protein containing 379 amino acids. As a result of a BLAST search, the protein sequence of esterase EstA1 was found to be identical to Alteromonas sp. esterase (GenBank: PHS53692). As far as we know, no research on this enzyme has yet been conducted. Phylogenetic analysis showed that esterase EstA1 was a member of the bacterial lipolytic enzyme family IV (hormone sensitive lipases). Two deletion mutants (Δ20 and Δ54) of the esterase EstA1 were produced in Escherichia coli BL21 (DE3) cells with part of the N-terminal of the protein removed and His-tag attached to the C-terminal. These enzymes exhibited the highest activity toward p-nitrophenyl (pNP) acetate (C₂) and had little or no activity towards pNP-esters with acyl chains longer than C₆. Their optimum temperature and pH of the catalytic activity were 45℃ and pH 8.0, respectively. As the NaCl concentration increased, their enzyme activities continued to increase and the highest enzyme activities were measured in 5 M NaCl. These enzymes were found to be stable for up to 8 h in the concentration of 3-5 M NaCl. Moreover, they have been found to be stable for various metal ions, detergents and organic solvents. These salt-tolerant and chemical-resistant properties suggest that the enzyme esterase EstA1 is both academically and industrially useful.

• Korean journal of applied entomology
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• v.30 no.2
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• pp.117-123
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• 1991

Acetylcholinesterase(AChE) and esterase activities as mechanisms of resistance to fenobucarb, carbofuran and diazinon in the insecticide-selected brown planthopper strains were investigated. Although there was no significant difference in AChE activity from suscept tible and resistant strains, AChE insensitivity was highly increased in the carbam없e insecticide-selected strains. On the other hand, esterase activity was moderately increa잃d in all the s selected strains. It is concluded that the cross-resistance and the level of resistance in the b brown planthopper can be explained by the combination of altered AChE and high esterase a activity, although a possible involvement of other factor(s) can not be excluded.

• Microbiology and Biotechnology Letters
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• v.22 no.5
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• pp.507-514
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• 1994

Acetyl xylan esterase was produced by E. coli HB101 harboring a recombinant plasmid pKMG6 which contained the estI gene of Bacillus stearothermophilus. The maximum production was observed when the E. coli strain was grown at 37$\circC for 12 hours in the medium containing 0.5% acetyl xylan, 1.0% tryptons, 1.0% sodium chloride, and 0.5% yeast extract. The esterase produced was purified to homogeneity using a combination of ammonium sulfate fractionation, DEAE Sepharose CL-6B ion exchange chromatography and Sephacryl S-200 gel filtration. The native enzyme had an apparent molecular mass of 60 kd and was composed of two identical subunits of 29 kd. The N-terminal amino acid sequence of the polypeptide was Ala-X-Leu-Gln- Ile-Gln-Phe-X-X-Gln. The acetyl esterase displayed a pH optimum of 6.5 and a temperature opti- mum of 45$\circC. The heavy metal ions such as Ag$^{++}$, Hg$^{++}$ and Cu$^{++}$ inhibited nearly completely the activity of the esterase, and no specific metal ion was found to be required for the enzyme activity. The enzyme readily cleaved MAS, $\beta$-D-glucose pentaacetate, $\alpha$-naphthyl acetate, $\rho$-nitrophenyl acetate as well as acetyl xylan, but had no activity on $\rho$-nitrophenyl propionate, $\beta$-nitrophenyl butyrate or $\beta$-nitrophenyl valerate. The Km and Vmax values for MAS were 2.87 mM and 11.55 $\mu$mole/min, respectively. Synergistic behavior was demonstrated with a combination of xylanase and esterase from B. stearothermophilus in hydrolyzing acetyl xylan.