• 한국응용곤충학회지
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• 제29권3호
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• pp.170-175
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• 1990

점박이응애(Tetranychus urticae Koch)의 살비제저항성 기작을 구명하기 위한 기초시험으로서, 유기인계 carbophenothion과 ethion, 유기염소계 dicofol, 유기주석계 cyhexatin 및 합성 pyrethroid계 biphenthrin으로 누대도태한 각 저항성계통과 감수성계통을 공시하여, esterase isozyme의 영동대 차이점 (polyacrylamide gel electrophoresis)을 비교한 결과, carbophenothion 저항성계통은 감수성계통에서 나타나지 않은 Est. 1, Est. 3이 검출되었고, ethion과 cyhexatin 저항성계통에서는 각각 Est. 3이, dicofol 저항성계통에서는 Est. 1, Est. 3, Est. 7이, biphenthrin 저항성계통은 Est. 3, Est. 7이 검출되었다. 이러한 영동대와 기질분해량의 차이점으로 미루어 보아 공시살비제들의 저항성발달에는 esterase가 관여하는 것으로 나타났다.

• 한국균학회지
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• 제16권2호
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• pp.95-100
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• 1988

한국에 자생하는 느타리버섯 균주중 지역별로 기주가 다른 균주들을 수집하여 Esterase 동위효소와 Leucine amino peptidase 동위효소를 등전점 전기영동으로 균사와 자실체 부위별로 비교하였다. Pleurotus ostreatus의 Esterase 밴드 패턴은 균사와 자실체가 많은 차이가 있었으나 자실체중 Primordia, 갓, 줄기 등의 isozyme 패턴은 유사하였다. P. ostreatus, P. cornucopiae, P. florida의 Esterase 밴드 패턴에 많은 차이가 있어 종간 균주구별이 가능하였다. Leucine Amino Peptidase 밴드는 P. ostreatus, P. cornucopiae, P. florida 간에 뚜렷이 구별지을 수 없었으며, 균사와 자실체 간에는 약간의 밴드 패턴의 차이가 있었다.

• Journal of Plant Biology
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• 제36권1호
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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.

• 대한소아치과학회지
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• 제34권2호
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• pp.285-291
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• 2007

상아질-레진 접착강도에 대한 collagenase와 esterase의 영향을 살펴보기 위해, 소구치의 교합면 상아질에 Single Bond 2와 Clearfil SE Bond로 접착을 시행하고 미세 시편을 제작하여 PBS collagenase 용액, esterase 용액에 4주간 보관한 후 미세인장결합강도를 측정, 비교하여 다음과 같은 결론을 얻었다. 1. 모든 보관 용액에서 Single Bond 2의 미세인장결합강도는 Clearfil SE Bond보다 유의하게 낮았다(p<0.05). 2. Single Bond 2의 미세인장결합강도는 collagenase군이 PBS군, esterase군보다 낮았다(p>0.05). 3. Clearfil SE Bond의 미세인장결합강도는 esterase군이 PBS군에 비해 낮았으나(p>0.05), collagenase군보다는 높았다(p>0.05). Collagenase군은 PBS군에 비해 유의하게 낮은 미세인장결합강도를 보였다(p<0.05).

• 대한수의학회지
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• 제4권1호
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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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• 제40권4호
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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.

• 한국균학회지
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• 제14권2호
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• pp.93-99
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• 1986

영지(靈芝)버섯(Ganoderma lucidum (Fr.) Karst.)의 16개 균주간(菌株關) 특성을 전기영동법(電氣泳動法)을 사용(使用)하여 단백질(蛋白質) pattern과 esterase, LAP의 동립효소(同位酵素) pattern에 의해 비교(比較) 관찰하여 다음과 같은 결과를 얻었다. 1. 자실체(子實體)의 esterase의 band pattern은 각(各) 균주간(菌株間) 특정 band의 유 무(有 無)와 위치(位置) 등에 의해 분류(分類) 할 수 있었으며 자실체(子實體)의 형태(形態)가 유사한 것은 band pattern에서도 유사하였다. 2. 동일균주(同一菌株)에서 편각(扁角)과 녹각형태(鹿角形態)로 형성(形成)된 자실체(子實體)의 esterase band pattern은 서로 동일(同一)한 pattern을 보였다. 3. 균주간(菌株間) 유연관계인 유사도 지수는 12.5%에서 100%의 변이 폭을 보였다. 특히 6과 7번의 두 균주간(菌株間)과 13,14,15,16번의 4균주간(菌株間)은 유사도지수가 100%이므로 유전적(遺傳的)으로 동일(同一)한 균(菌)이라 사료(思料)된다. 4. 균사(菌絲)의 단백질(蛋白質)과 esterase의 band pattern은 자실체(子實體)의 pattern과는 달랐으며 자실체(子實體)에서 동일(同一)한 pattern을 보였던 균주간(菌株間)에서도 균주간(菌株間) 특성을 가장 잘 보여 주었으므로 영지(靈芝)버섯 분류(分類)에는 균사(菌絲)의 esterase pattern이 가장 적합하다.

• Journal of Microbiology and Biotechnology
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• 제30권2호
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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.

• 한국응용곤충학회지
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• 제30권2호
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• pp.117-123
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• 1991

벼멸구의 살충제 저항성 기구를 구명하고자 fenobucarb, carbofuran 및 diazinon으로 벼멸구를 14~18세대 누대 도태하여 얻어진 벼멸구를 대상으로 저항성 기구를 조사하였으며, 얻어진 결과중 acetylcholinesterase(AChE)와 esterase의 활성 변화에 대하여 보고하고자 한다. AChE활성은 fenobucarb선발 계통에서 1.6배 증가하였으나 타 계통에서는 차이가 없었고, 세포내 분포도 mitochondrial fraction에서 70% 이상으로 계통간 차이가 없었다. 반면, AChE감수성은 fenobucarb와 carbofuran선발 계통에서 각각의 공시 살충제에 대하여 12.2배, 5.6배 감소하였으나 diazinon선발 계통에서는 diazoxon에 대하여 1.7배 감소에 그쳤다. Esterase활성은 fenobucarb선발계통에서 5.6~6.8배, carbofuran선발계통에서 6.4~7.8배, diazinon선발계통에서 4.0~4.4배 증가하였다. 벼멸구의 저항성 증가에 다른 요인이 관련됨을 배제할 수 없으나, 본 실험 결과 esterase 활성증가와 AChE감수성 저하라는 두 요인이 상승적으로 작용하여 벼멸구 저항성을 유발하였음을 확인하였다.

• 한국미생물·생명공학회지
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• 제22권5호
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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.