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Four quinolone alkaloids, 2-heptyl-4-quinolone (1), 2-nonyl-4-quinolone (2), 2-undecyl-4-quinolone (3), and 2- undecen-1′-yl-4-quinolone (4), together with two nitrogen derived benzoic acid derivatives, N-acetylanthranilic acid (5) and oacetamidobenzamide (6) have been isolated from the Arctic bacterial strain, Pseudomonas aeruginosa. The structures of the compounds were determined by 1D and 2D NMR, and MS experiments, as well as by comparison of their data with published values. To the best of our knowledge, compounds 3-6 were isolated for the first time from P. aeruginosa.
본 연구에서 탄소원이 고갈된 후 용존산소농도로 epothilone 의 합성을 조절할 수 있음을 증명하였다. 선행연구로써, soluble starch를 탄소원으로 결정하였고, lactose와 yeast extract의 최적농도가 각각 4 g/L, 0 g/L임을 알 수 있었다. 탄소원이 고갈된 환경에서 산소농도가 낮을 경우 균체가 epothilone을 다량으로 합성하였다. 산소 공급을 조절할 수 없는 flask의 경우 배양이 진행되면서 균체농도가 증가하고 자연적으로 산소 농도도 감소하므로 epothilone 이 합성되지만, 생물반응기의 경우 탄소원의 고갈 후 산소농도를 최대한 낮게 유지시키는 것이 epothilone의 생산을 증가시켰다 The biological production of a potent anticancer agent, epothilone, by Sorangium cellulosum was carried out using flask and fermentor cultures. Soluble starch was selected as the main carbon source and the concentrations of lactose and yeast extract were optimized at 4 and 0 g/L, respectively, when using the flask cultures. In the fermentor cultures, the cells were cultivated at a high DO level of more than 80% of air saturation in the growth stage and then the DO level was controlled at about 50, 20 or 1-2% when the carbon source was exhausted. The epothilone production increased with decreasing DO level after the exhaustion of the carbon source, and the maximum concentration of epothilone was 5.4 mg/L. It was found that the DO level had significant regulation effects on the epothilone production.
This research was to examine the effects of various cyclodextrins on the solubility and stability of prodigiosin in seawater. Among them, β-cyclodextrin was found to have the best efficiency and formation of the inclusion complex was saturated when prodigiosin and β-cyclodextrin were mixed in a ratio of 1:8 and shaken at 25℃ and pH 8.0 for 6 h. The maximum algicidal activity against Chattonella antiqua using the inclusion complex stored at 4℃ for 5 weeks of culture was obtained, 52.28 ± 3.41%, which was about 5.0 fold higher than that of control. Our results suggest that inclusion complexes of prodigiosin and β-cyclodextrin could serve as effective algicidal agents.
본 논문에서는 반응표면분석법을 이용한 Arthrobacter sp. PAMC 25486의 carotenoids 생산 배지의 최적화를 수행하였다. Placket-Burman 방법을 이용하여 yeast extract, MgSO4, dextrose가 carotenoids의 생산에 영향을 미치는 주요인자인 것을 확인하였다. 반응표면분석 방법을 이용하여 최대 carotenoids 생산 농도를 갖는 yeast extract, MgSO4, dextrose의 농도를 계산한 결과 1 g/L yeast extract, 0.0879 g/L MgSO4 and 1 g/L dextrose의 농도에서 최대 307 mg/L 의 carotenoids 농도가 예측됐으며, 실제 배양 결과 288 mg/L carotenoids가 얻어졌다. 얻어진 농도 값은 최적화 이전의 값에 비하여 200% 이상 증가하였다. 이러한 결과로부터 미생물 배양에 의한 carotenoids 생산을 증가시키기 위한 배지최적화 방법으로서 반응표면분석법의 유용성을 확인할 수 있었다. This study was conducted to optimize the medium composition for carotenoid production in Arthrobacter sp. PAMC 25486 through response surface methodology (RSM). Using a Placket-Burman design, from which yeast extract, MgSO4 and dextrose were identified as the significant factors affecting carotenoids production. RSM studies for carotenoids production by Arthrobacter sp. PAMC 25486 have been carried out for three parameters of yeast extract, MgSO4 and dextrose concentrations. These significant factors were optimized by experiments and RSM, as 1 g/L yeast extract, 0.0879 g/L MgSO4 and 1 g/L dextrose. The experimentally obtained concentration of carotenoid was 288 mg/L, and it became 2-fold increase on concentration before optimization.
본 논문에서는 저온활성 protease의 생산을 최적화하기 위하여 극지 미생물인 Enterobacteriaceae sp. PAMC 25617의 반응표면분석법을 이용한 배지의 최적화를 수행하였다. One-factor-at-a-time 방법을 이용하여 yeast extract, TritonX-100이 protease의 생산에 영향을 미치는 주요인자인 것을 확인하였다. 물리적인 환경 요인으로 pH를 추가하여 반응표면분석 방법을 이용한 최대 protease 생산 농도를 갖는 각 인자들의 농도를 확인한 결과 5 g/L peptone, 3 g/L malt extract, 10 g/L C6H12O6, 6.690 g/L yeast extract, 0.018 g/L TritonX-100의 농도에 pH 6.777의 조건에서 미생물을 배양하였을 경우, 최대 10.049 U/L의 protease가 생산될 수 있는 것으로 예측되었다. 실제 배양 결과 8.03 U/L의 protease가 얻어졌으며, 최적화 이전의 생산농도와 비교하여 150% 이상의 증가를 이루었다. 결과적으로 배지최적화를 통한 protease 생산량의 증가에 반응표면분석법의 적용이 유용하다는 것을 확인할 수 있는다. 이러한 결과로부터, 배지 최적화를 이용한 극지 미생물 유래 cold-adapted protease 생산량의 증가가 여러 산업 분야에서 유용하게 이용될 수 있을 것으로 생각된다. This study was conducted to optimize the medium composition for cold-adaptive protease production of Enterobacteriaceae sp. by response surface methodology (RSM). Yeast extract, and TritonX-100 were identified as the significant factors affecting protease from one-factor-at-a-time method. RSM studies for optimizing protease production of Enterobacteriaceae sp. have been carried out for three parameters including yeast extract concentration, TritonX-100 concentration, and culture pH. These significant factors were optimized as 6.690 g/L yeast extract, 0.018 g/L Triton™ X-10, and pH 6.677. The experimentally obtained protease activity was 8.03 U /L, and it became 1.5-fold increase before optimization.
Antifreeze proteins (AFP) inhibit growth and recrystallization of ice, and permit organisms to survive in cold environments. The AFP from an Antarctic bacterium, Flavobacterium frigoris PS1, FfIBP (Flavobacterium frigoris icebinding protein), was produced in E. coli using a cold shock induction system. The culture temperature was shifted from 37°C to 15°C and a 20 L culture scale was used. The final weights of dried cell and FfIBP were estimated to be 126 g and 8.4 g, respectively. The thermal hysteresis (TH) activity (1.53°C) of the produced FfIBP was 3.6-fold higher than that of the LeIBP (Leucosporidium ice-binding protein) produced in Picha. The current study demonstrates that large-scale production of FfIBP was successful and the result could be extended to further application studies using recombinant AFPs.
Antifreeze proteins (AFPs) have a unique feature to bind to ice nuclei, and are referred to ice-binding protein (IBP). The AFP, expressed in the cells of some polar organisms, controls cell damage in subzero temperature environments by inhibiting the ice growth and recrystallization. In this study, recombinant LeIBP (Leucosporidium ice-binding protein) from the arctic yeast Glaciozyma sp. (former known as Leucosporidium sp.) was produced in E. coli using a cold shock induction system. The final cell density and concentration of the purified LeIBP were measured to be 8.2 g/L and 1.1 g/L, respectively. The thermal hysteresis (TH) activity of LeIBP was 0.39±0.02°C at 13.25 mg/mL, which means that the scaleup was successfully performed for the production of recombinant LeIBP in heterologous bacterial expression system.
본 연구에서는 극지 연구소로부터 분양 받은 Arthrobacter sp. PAMC 27388 균주에서 생산되는 아밀라아제(amylase)를 물리적 요인(physical factor)들의 변화를 통하여 생산배지 최적화를 수행하였다. 한천 배지 상에서 lugol solution을 이용한 클린환의 확인을 통하여 아밀라아제가 생산됨을 확인하였으며, 16S rDNA를 이용하여 동정한 결과 Arthrobacter sp. 임을 확인할 수 있었다. 최적화 이전의 아밀라아제 생산량은 1.66 mU/L로 확인되었다. 최적화 결과, 2.49 mL의 접종부피, pH 6.85, 42.87 mL의 배지 부피의 조건에서 가장 많은 양의 아밀라아제가 생산될 것으로 예상되었으며, 생산량은 2.84 mU/L로 예상되었다. 확인 실험을 통하여 최적화 이전과 비교하여 생산량이 약 150% 증가한 2.50 mU/L의 아밀라아제가 생산됨을 확인할 수 있었다. In this study, the physical factors for amylase production by Arthrobacter sp. were optimized using response surface methodology(RSM). Antarctic microorganism Arthrobacter sp. PAMC 27388 was obtained from the Polar and Alpine Microbial Collection(PAMC) at the Korea Polar Research Institute. This microorganism was confirmed for the excretion of amylase with Lugol`s solution. The amylase activity was after flask culture was as low as 1.66 mU/L before optimization. The physical factors including the inoculum volume, the initial culture pH, and the medium volume were chosen to be optimized for the enhanced amylase production. The calculated results using RSM indicate that the optimal physical factors were 2.49 mL inoculum volume, 6.85 pH and 42.87 mL medium volume with a predicted amylase production of 2.84 mU/L. The experimentally obtained amylase activity was 2.50 mU/L, which was a 150% increase compared to the level before optimization.
Antifreeze proteins (AFP) inhibit ice growth to permit the survival of polar organisms in the cold environments. The recombinant AFP from an Antarctic bacterium, Flavobacterium frigoris PS1, FfIBP (Flavobacterium frigoris icebinding protein), was produced using Pichia pastoris expression system. The optimum fermentation temperature (30℃) and pH (5) for FfIBP production were determined using a fedbatch culture system. The maximal cell density and purified FfIBP were 112 g/L and 70 mg/L, respectively. The thermal hysteresis (TH) activity (0.85) of FfIBP obtained using a glycerol-methanol fed-batch culture system was 2-fold higher than that of the LeIBP (Leucosporidium ice-binding protein). This work allows for large-scale production of FfIBP, which could be extended to further application studies using recombinant AFPs.