• 한국미생물·생명공학회지
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• 제47권1호
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• pp.87-95
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• 2019

Esterase produced by Acinetobacter sp. B1 (strain B1) was optimized by means of one-variable-at-a-time and response surface methodologies. Results of the one-variable-at-a-time experiment showed that Tween 80 significantly increased esterase production of strain B1. The addition of Tween 80 to the culture medium increased the biomass and esterase activity of strain B1, stimulated content of total extracellular protein, and enhanced the oleic acid (C18:1) composition in the cell membrane of strain B1. The influence of eight culture variables on esterase production was evaluated by Plackett-Burman design. Results showed that Tween 80, pH, and $K_2HPO_4$ significantly affected the esterase production of strain B1. Tween 80, pH, and $K_2HPO_4$ were further optimized by central composite design. Under the optimized conditions (w/v, soluble starch 2.5%, tryptone 1.5%, Tween 80 0.8%, $K_2HPO_4$ 0.5%, NaCl 0.5%, pH 8.0, inoculum size 1%, and inoculum age 24 h), the maximum esterase activity of strain B1 was 152.13 U/ml, which was 10-fold higher than that of non-optimization after 36 h cultivation.

• International Journal of Industrial Entomology and Biomaterials
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• 제9권1호
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• pp.59-63
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• 2004

By using PAGE, a study was made on the nonspecific esterase spectra of female genital organs and eggs in Bombyx mori L. The expression of 11 esterase bands was detected during ontogenesis of races and inter-races hybrids kept in Bulgaria. The gene activity of 9 esterase loci was assumed. Esterases specific for the spectrum of diapausing eggs were observed. In two esterase zones, intra- and inter-breed polymorphism was found. Based on the same breed specific expression, the existence of correspondence between esterase bands from spectra of different silkworm tissues and organs was suggested. Stage-specific expression of esterases in female genital glands, indicative of differentiated gene activity during ontogenesis, was established.

• 한국초지조사료학회지
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• 제11권3호
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• pp.158-161
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• 1991

Horizontal starch gel electrophoresis, follow by enzyrne-specific staining, separate and visualize several legume esterase isozyme. Using extracts prepared from cotyledon, radicle and plumule of legume seedlings germinated 5 days. The results were as follows. 1. The number and staining intensity of esterase isozyme bands varies depending on the plant species. tissues and developmental stage. 2. Bands in the cotyledon of field bean seedling expressed 4 and 1 in radicle. 3. In soybean cultivars, cotyledon of IIwangkum-kong had 3 bands and 1 band in the examined tissues of Paldal-kong and Jangkyung-kong seedling. 4. The cotyledon and radicle of french bean seedling had 3 bands, respectively. 5. The highest esterase isozyme activity appears to be expressed in the cotyledon and radicle of french bean, as indicated by intensity of stain, with the Paldal-kong particulary active.

• 한국인쇄학회지
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• 제26권1호
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• pp.17-28
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• 2008

The wood-pulp is treated with the three enzymes; Endo-xylanase, exo-xylanase and acetyl-esterase. The maximum value of relative activity appeared 0.95 in acetyl-esterase at $40^{\circ}C$, 0.9 in exo-xylanase at $40^{\circ}C$, and 0.8 in endo-xylanase at $50^{\circ}C$, respectively. And it has measured 0.8 in endo-xylanase, 0.95 in acetyl-esterase at pH 6 and 0.9 in exo-xylanase at pH 5, while the maximum value of relative activity does not rely on reaction time for three enzymes treatment, and the value was about 0.9, respectively. We have watched that decreased Kappa number and increased brightness. And it turned out that the three enzyme produced a lot of reducing sugar with wood-pulp treatment.

• Parasites, Hosts and Diseases
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• 제31권2호
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• pp.165-168
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• 1993

서울주걱흡충의 냉동절편에서 효소조직화학법을 이용하여 조직융해구(trlbocytic organ)와 맹장에 acid phosphatase, non-specific esterase 활성도가 있음을 알 수 있었다. 이 두 기관이 표피 이외에 중요한 흡수기관일 것이다. 이 흡충의 우리말 이름을, 이미 회원들에 의해 제안된 "쥐주걱흉충"은 쥐만 적절한 숙주로 생각할 수 있으므로 발견 장소가 학명에 포함된 것을 감안하여 "서울주걱흡충"이라고 고쳐 쓰고 싶다. 준말로 쓸 때는 "서울흡충"이 나을 것이다.

• 한국미생물·생명공학회지
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• 제21권6호
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• pp.542-548
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• 1993

Bacillus stearothermophilus was shown to express multiple xylanolytic enzymes including acetyl xylan esterase. Genomic DNA of the strain partially digested with HindIII was ligated into the HindIII site of pBR322, and expressed in E. coli HB101 cells in order to clone the gene for acetyl xylan esterase. One transformant among 4000 screened formed a clear zone around its colony on the LB agar supplemented with 1.0% tributyrin. The functional clone harbored the recombinant plasmid pKMG5 with an insert of 5.1kb.

• 한국동물학회지
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• 제31권2호
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• pp.147-155
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• 1988

1986년 12월부터 87년 11월까지 채집된 애응애과 응애를 분류학적으로 정리한 바 Brevipalpus속의 B.californicus와 B.ovovatus 2종과 다음의 한국4미기록종을 얻었다: Aegyptobia nothus Pritchard and Baker,Pentomerismus taxi Hailer, P. oregonensis McGregor,Brevipalpus lewisi McGregor. 따라서, 한국산 애응애과 응애는 Tenuipalpus속의 T.zhizhilashiliae(감나무애응애)를 포함하여 4속 7종이 보고되는 셈이다. 또한 P. oregonensis,B.californicus,B.ovovatus 및 B.lewisi에 대하여 polyacrylamide slab gel electrophoresis로 esterase와 alkaline phosphatase pattern을 조사한 바 esterase는 band수와 이동도에서 종과 속간에 뚜렷한 차이를 보였다.

• 한국균학회지
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• 제25권2호통권81호
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• pp.85-90
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• 1997

표고버섯(Lentinula edodes)의 동위효소 양상을 표고 연구의 기초 연구의 일환으로 실시하였다. 균사체의 Tris-HCl 완충액에 용해되는 세포내 효소를 nondenaturing polyacrylamide gel 전기영동 법으로 분리후, peroxidase, esterase, superoxide dismutase, acid phosphatase, alkaline phosphatase, alcohol dehydrogenase, ${\alpha}-amylase$ 효소 활성을 측정하였다. 표고는 peroxidase, esterase, superoxide dismutase, acid phosphatase 활성이 검출되었으며, 본 연구에서 사용한 방법으로 alkaline phosphatase, alcohol dehydrogenase, ${\alpha}-amylase$ 효소 활성은 검출되지 않았다. 표고버섯의 peroxidase, esterase band는 배양 기간에 따라 큰 차이가 없이 안정하였으며, 동위효소는 표고의 유전적 연구 및 원형질체 융합 후 융합체의 특성 연구에 중요하다.

• Journal of Applied Biological Chemistry
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• 제51권3호
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• pp.95-101
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• 2008

The gene encoding a putative esterase of Xanthomonas oryzae pv. oryzae was cloned using PCR technique. The gene was expressed with His6 tag in E. coli. One-step purification of the recombinant esterase with Ni-NTA resin resulted in one band by SDS-PAGE analysis. The purified enzyme showed a molecular weight of 30 kDa, as expected, therefore the enzyme was a mononer. The enzyme was the most active toward p-nitrophenyl (p-NP) acetate and p-NP-butyrate to a lesser extent. However, the enzyme could not hydrolyze p-NP-myristate, palmitate, and stearate. Therefore, the enzyme is considered as an esterase, very different from lipase. The purified esterase had optimal pH at around 8.0 and was stable in a broad range of pH values. The optimal temperature ranged from 30 to $40^{\circ}C$, and the residual activity observed after heat treatment at $55^{\circ}C$ for 20 min was 72 % of the initial activity. The activity was inhibited by the presence of copper and cobalt ions.

• 한국미생물·생명공학회지
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• 제25권1호
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• pp.23-29
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• 1997

The nucleotide sequence of the estI gene encoding acetylxylan esterase I of Bacillus stearothermophilus was determined and analyzed. The estI gene was found to consist of a 810 base pair open reading frame coding for a polypeptide of 270 amino acids with a deduced molecular weight of 30 kDa. This was in well agreement with the molecular weight (29 kDa) estimated by SDS-PAGE of the purified esterase. The coding sequence was preceded by a putative ribo some binding site 10 bp upsteam of the ATG codon. Further 53 bp upstream, the transcription initiation signals were identified. The putative $_{-}$10 sequence (TCCAAT) and $_{-}$35 seqence (TTGAAT) corresponded closely to the respective consensus sequences for the Bacillus subtiis major RNA polymerase. The G+C content of the coding region of the estI was 51% whereas that of the third position of codone was 60.2%. The N-terminal amino acid sequence of the EstI deduced from the nucleotide sequence perfectly matched the corresponding region of the purified esterase described previously. Comparison with the amino acid sequence of other esterases and lipases reported so far allowed us to identify a sequence, GLSMG at positions 123 to 127 of the EstI which was reported to be the highly conserved active site sequence for those enzymes. The nucleotide sequence of the estI revealed 55.7% homology to that of the xylC coding for the acetylxylan esterase of Caldocellum saccharolyticum.