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RISS 인기검색어
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- 저자 : 임재윤(Jai-Yun Lim) (검색결과 20 건)
- 무료
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Glutary 7-Aminodeacetoxycephalosporanis Acid Acylase 생산균의 분리 및 동정
이윤진,임재윤,Lee, Yun-Jin,Lim, Jai-Yun 한국미생물학회 1994 미생물학회지 Vol.32 No.3
Glutaryl 7-aminodeacetoxycephalosporanic acid(GL-7-ADCA)로부터 7-aminodeacetoxycephalosporanic acid(7-ADCA)를 생성하는 GL-7-ADCA acylase생산균을 자연계에서 폭넓게 검색하여 한균주를 선정하고 분리균의 형태 및 생리적 성질들을 조사하여 Alcaligenes sp.로 동정하였다. 분리균의 효소생산을 위한 배양조건을 검토한 결과 탄소원으로는 glucose, 질소원으로는 yeast extract, monosodium L-glutamate가 우수하였다. 효소의 작용최적 pH는 8.0이며, pH7.0~pH11.0 번위에서 비교적 안정하였다. 5l jar fermentor에서 배양경과를 조사한 결과 효소이 활성은 $37^{\circ}C$, 교반속도 300rpm, 통기량 1vvm 조건에서 20시간~30시간 배양시 가장 높았다. Microorganism producing glutaryl 7-aminodeacetoxycephalosporanic acid (GL-7-ADCA) acylase was screened from soil. The microorganism was identified as Alcaligenes sp. J-421 by its morphology and biochemical properties. Cultural conditions of Alcaligenes sp. J-421 were investigated for the production of GL-7-ADCA acylase. Optimum medium composition was 1% glucose, 1% beef extract, 0.5% yeast extract, 0.2% monosodium L-glutamate, 0.1% glutaric acid, 0.2% NaCl, 0.5% $K_2$ $HPO_4$, and 0.05% $CuSO _4{\cdot}5H_2O$. Optimum cultivation conditions for the production of the enzyme in 5 l jar fermentor were $37^{\circ}C$, tip speed 300 rpm, aeration 1 vvm. Optimum reaction pH of the enzyme was 8.0 and the enzyme was stable at pH7.0-11.0.
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Alcaligenes sp. J-482 로부터 분리한 제한효소 AspJI의 특성
이정택,조태주,임재윤,Lee, Jeong-Taek,Lim, Jai-Yun 한국미생물학회 1994 미생물학회지 Vol.32 No.4
자연계에서 새로운 제한효소 생산균을 검색하여 한 균주를 선발하고, 형태학적, 생리학적, 생화학적 특성들을 조사하여 Alcaligenes sp.로 동정하고 제한효소의 특성을 조사하였다. Alcaligenes sp. J-482가 생산하는 제한효소를 AspJI으로 명명하였다. AspJI은 pBR322, Adenovirus 2-DNA, ${lambda}$ DNA 등에 대한 절단양식이 AatII와 같아 AatII의 isoschizomer로 추정 되었으며, 효소활성에 12.5mM 이상의 $MgCl_2$를 필요로 하였으며, NaCl에 의하여 저해되었다. AspJI의 반응 최적 온도는 $37^{circ}C$, 최적 pH는 7.5로 확인 되었으며, 내열성을 조사한 결과 $85^{circ}C$이상에서 15분처리 할 때 안전히 실활되는 것으로 관찰되었다. About 500 bacterial and fungal strains from a wide variety of natural habitats were screened for a new type II restriction endonuclease. Among the 500 species, we selected one species that produced a new restriction endonuclease. This strain has an optimum temperature of $30^{circ}C$ for growth. Morphological, cultural, and physiological characteristics were examined for identification of the isolated strain J-482. This strain was found to belong to the genus Alcaligenes. The restriction endonuclease was named as AspJI and partially purified from Alcaligenes sp. J-482 by DEAE-Sephadex A-50 column chromatography and gel filtration. Most of other nucleases were removed by the purification steps. The AspJI has a substrate specificity to ${lambda}$ DNA, pBR322 and Adenovirus-2 DNA. For its maximal activity, the isolated enzyme requires $MgCl_2$, which should be at least 12.5 mM and it does not need any other cofactors. It is maximally active in the absence of NaCl and is completely inactivated at 100 mM NaCl. The pH and temperature optima for activity were pH 7.5 and $37^{circ}C$, respectively. The DNA fragments generated by digesting ${lambda}$ DNA, pBR322, and Adenovirus-2 DNA with AspJI were the same as that produced by AatII. This suggests that AspJI is an isoschizomer of AatII.
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Penicillium sp. KJ81이 생산하는 Erythritol 4-Phosphate Dehydrogenase의 특성
윤나래,박상희,임재윤,Yun, Na-Rae,Park, Sang-Hee,Lim, Jai-Yun 한국미생물학회 2009 미생물학회지 Vol.45 No.2
Erythritol 생합성에 중요한 효소인 erythritol 4-phosphate dehydrogenase를 Penicillium sp. KJ81로부터 분리 정제하여 효소의 특성을 조사한 결과 다음과 같은 결론을 얻었다. Erythritol 4-phosphate dehydrogenase의 최적 생산 조건은 30% sucrose, 0.5% yeast extract, 0.5% $(NH_4)_2SO_4$, 0.1% $KH_2PO_4$ 그리고 0.05% $MgCl_2$ (pH 7.0) 배지에서 1 vvm aeration, 교반속도 200 rpm, $37^{\circ}C$로 Penicillium sp. KJ81을 배양한 결과 8일 배양 시 최대의 생산량을 보였다. Penicillium sp. KJ81주의 균체 추출액으로부터 ultrafiltration, 조제용 disc gel electrophoresis를 이용하여 erythritol 4-phosphate dehydrogenase를 분리 정제하였다. 최종 수율은 33%이었으며 정제배수는 39.5였다. 정제된 효소의 pI값은 4.6으로, erythrose 4-phosphate에 특이적으로 반응하였으며, Km값은 1.07mM이었다. Native-PAGE에서 single band를 보인 효소의 분자량은 약 1,500 kDa이었다. 효소활성의 최적 pH와 온도는 pH 7.0, $30^{\circ}C$였으며, 효소는 pH 4.0~9.0, 그리고 $30^{\circ}C$까지 안정하였다. 다양한 금속이온 중 $Cu^{2+}$, $Zn^{2+}$에 의하여 효소의 활성이 저해되었다. 다양한 아미노산 반응 잔기 변형시약 중 iodine과 NBS에 의해 효소의 활성이 저해되는 것을 확인하였다. In this study, the characterization of purified erythritol 4-phosphate dehydrogenase, key enzyme of erythritol biosynthesis, produced by Penicillium sp. KJ81 was investigated. Optimum production conditions of erythritol 4-phosphate dehydrogenase was 1 vvm areration, 200 rpm agitation, at $37^{\circ}C$ for 8 days in the medium containing 30% sucrose, 0.5% yeast extract, 0.5% $(NH_4)_2SO_4$, 0.1% $KH_2PO_4$, and 0.05%$MgCl_2$. Erythritol 4-phosphate dehydrogenase was purified through ultrafiltration and preparative gel electrophoresis from cell extract of Penicillium sp. KJ81. This enzyme was especially active on erythrose 4-phosphate with 1.07 mM of Km value. It gave a single band on native polyacrylamide gel electrophoresis and an isoelectric point of 4.6. The enzyme had an optimal activity at pH 7.0 and $30^{\circ}C$. It was stable between pH 4.0 and 9.0, and also below $30^{\circ}C$. The enzyme activity was completely inhibited by 1mM $Cu^{2+}$ and 1 mM $Zn^{2+}$, but was not significantly affected by other cations tested. This enzyme was inactivated by treatment of tyrosine specific reagent, iodine and tryptophan specific reagent, N-bromosuccinimide. The substrate of the enzyme, erythrose 4-phosphate showed protective effect on the inactivation of the enzyme by both reagents. These results suggest that tryptophan and tyrosine residues are probably located at or near active site of the enzyme.
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재조합균주 E. coli CK1092가 생산하는 2,3-Dihydroxybiphenyl Dioxygenase의 정제 및 특성
박효남,김영수,김영창,김치경,임재윤,Park, Hyo-Nam,Kim, Young-Soo,Kim, Young-Chang,Kim, Chi-Kyung,Lim, Jai-Yun 한국미생물 · 생명공학회 1996 한국미생물·생명공학회지 Vol.24 No.3
2,3-DHBP dioxygenase was purified from E. coli CK1092 carrying the pcbC gene, which was cloned from 4-chlorobiphenyl-degrading Pseudomonas sp. P20. Purification of this enzyme was done by acetone precipitation, DEAE- Sephadex A-25 ion exchange chromatography, and preparative gel electrophoresis. The molecular weight of subunit was 34 kDa determined by SDS-PAGE, and that of native enzyme was about 270 kDa. It suggests that this enzyme consist of eight identical subunits. This enzyme was specifically active against only 2,3-DHBP as a substrate with 18 $\mu$M of Km value, but not catechol, 3-methylcatechol, 4-methylcatechol and 4-chlorocatechol. The optimal pH and temperature of 2,3-DHBP dioxygenase were pH 8.0 and 40-60$\circ$C. The enzyme was inhibited by Cu$^{2+}$, Fe$^{2+}$ and Fe$^{3+}$ ions, and was inactivated by H$_{2}$0$_{2}$2 and EDTA. The lower concentrations of some organic solvents such as acetone and ethanol don't stabilize the activity of 2,3-DHBP dioxygenase. The enzyme was completely inactivated by adding the reagents such as N-bromosuccinimide, iodine and p- diazobenzene sulfonic acid.
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이기성,오태엽,박영식,김영수,김영창,임재윤,민경희,김치경 ( Ki Sung Lee,Tae Youp Oh,Young Sik Park,Young Soo Kim,Young Chang Kim,Jai Yun Lim,Kyung Hee Min,Chi Kyung Kim ) 한국하천호수학회 1995 생태와 환경 Vol.28 No.3
This study was designed to elucidate the bio-degradability and self-clarification upon agricultural chemicals in the Kum river area including the field, rice paddy, green houses, the Daechung Reservoir Lake, and Kap-chun etc. First, we checked the size of bacterial populations degrading recalcitant agricultural chemicals, upon 12 different sites around Kum River area in December, 1993 and in May 1994. These recalcitrant chemicals included glyphosate(GPS), butachlor(BUT) as herbicide, cartap(CAP), diazinon(DIA) as insecticide and iprobenfos(IPR) as fungicide. Of these bacteria, the actively degradable bacteria upon agricultural chemicals were selected and isolated, for checking the growth curve and biodegradability using thin layer chromatography and U, V. spectroscopy. In winter, the densities of agricultural chemical degrading bacteria were high. As the results, the distributions and population densities of agricultural chemical degrading bacteria were very different seasonally and spatially. The order (of dominant bacterial population comprising the higher biodegradabilty upon recalcitrant agricultural chemical)was GPS→CAR→DIA→BUT→IPR, respectively. On the other hand, in spring, the order was CAR→BUT→GPS→DIA→IPR, respectively. In 6 days after each of chemicals(DIA, BUT, IPR) was
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2,3-Dihydroxybiphenyl Dioxygenase 생산을 위한 E. coli CK1092의 배양조건
이정영,김영수,이기성,민경희,김영창,김치경,임재윤,Lee, Jung-Young,Kim, Youngsoo,Lee, Ki-Sung,Min, Kyung-Hee,Kim, Young-Chang,Kim, Chi-Kyung,Lim, Jai-Yun 한국미생물학회 1998 미생물학회지 Vol.34 No.1
PCBs를 분해하는 Pseudomonas sp. P20 균주의 pcbC gene이 재조합 된 E. coli CK1092 균주를 이용하여 2,3-dihydroxybiphenyl dioxygenase 생산에 미치는 배양조건을 검토하였다. E. coli CK1092를 2% sucrose가 포함된 LB 배지를 기본배지로 하여 질소원, 금속이온 등의 영향을 조사한 결과, $Fe^{3+}$와 $Fe^{2+}$이 $10^{-5}M$의 농도일때 효소생산이 증가되었으며 배양최적온도는 $37^{\circ}C$, 배양초기 pH 7.0일때 효소생산이 우수하였다. 배양조에서의 배양조건은 초기 pH 7.0, 통기량 1 v/v/m, 교반속도 200rpm에서 가장 효소생성이 우수하였다. To obtain higher yield of 2,3-dihydroxybiphenyl(2,3-DHBP) dioxygenase by recombinant E. coli CK1092 carrying pcbC gene of Pseudomonas sp. P20, the environmental and physiological factors were investigated and the cultural conditions using jar fermentor were studied. E. coli CKl092 was grown in LB medium supplemented with 2% sucrose, as a basal medium. The effect of various metal ions on the enzyme production was investigated. In particular, the enzyme production increased in the presence of $Fe^{3+}$ and $Fe^{2+}$, and showed the maxium at the concentration of $10^{-5}M$. The enzyme production was increased by 55% in the medium containing $Fe^{3+}$ ($10^{-5}M$) ion. The optimal temperature and initial pH for cell growth were $37^{\circ}C$ and 7.0, respectively. In the culture using a fermentor at $37^{\circ}C$, the optimal conditions for the enzyme production were obtained at the initial pH 7.0, 1 v/v/m of aeration rate, 200 rpm of agitation speed. It was found that enzyme activity was higher when cultivated without pH control than with pH control.
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