• Korean Journal of Food Science and Technology
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• v.36 no.3
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• pp.440-447
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• 2004

Characteristics of human ${\beta}-carotene$ 15,15'-dioxygenase isolated by recombinant DNA technology was elucidated. Optimal pH and temperature were 9.0 and $40^{\circ}C$, respectively. Enzyme activity was temperature-sensitive. Enzyme was stable at pH 6.0-9.0 for 24 hr and under $5^{\circ}C$. Half-life of enzyme at $35^{\circ}C$ was 40 min. Crude preparations of enzyme were inhibited by ferrous ion-chelating agent and sulfhydryl-binding agent. GSH offsets inhibitory effect of PCMB. With increasing substrate concentrations, enzyme activity gave typical Michaelis-Menten curve, Based on Hanes-Woolf plot of data, $K_{m}\;and\;V_{max$ were $3.39{\times}10^{6}\;M\;and\;1.2\;pmol/mg$ protein/min, respectively.

• Korean Journal of Materials Research
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• v.26 no.3
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• pp.117-122
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• 2016

White organic light-emitting diodes with a structure of indium-tin-oxide [ITO]/N,N-diphenyl-N,N-bis-[4-(phenylm-tolvlamino)-phenyl]-biphenyl-4,4-diamine [DNTPD]/[2,3-f:2, 2-h]quinoxaline-2,3,6,7,10,11-hexacarbonitrile [HATCN]/1,1-bis(di-4-poly-aminophenyl) cyclo -hexane [TAPC]/emission layers doped with three color dopants/4,7-diphenyl-1,10-phenanthroline [Bphen]/$Cs_2CO_3$/Al were fabricated and evaluated. In the emission layer [EML], N,N-dicarbazolyl-3,5-benzene [mCP] was used as a single host and bis(2-phenyl quinolinato)-acetylacetonate iridium(III) [Ir(pq)2acac]/fac-tris(2-phenylpyridinato) iridium(III) $[Ir(ppy)_3]$/iridium(III) bis[(4,6-di-fluoropheny)-pyridinato-N,C2] picolinate [FIrpic] were used as red/green/blue dopants, respectively. The fabricated devices were divided into five types (D1, D2, D3, D4, D5) according to the structure of the emission layer. The electroluminescence spectra showed three peak emissions at the wavelengths of blue (472~473 nm), green (495~500 nm), and red (589~595 nm). Among the fabricated devices, the device of D1 doped in a mixed fashion with a single emission layer showed the highest values of luminance and quantum efficiency at the given voltage. However, the emission color of D1 was not pure white but orange, with Commission Internationale de L'Eclairage [CIE] coordinates of (x = 0.41~0.45, y = 0.41) depending on the applied voltages. On the other hand, device D5, with a double emission layer of $mCP:[Ir(pq)_2acac(3%)+Ir(ppy)_3(0.5%)]$/mCP:[FIrpic(10%)], showed a nearly pure white color with CIE coordinates of (x = 0.34~0.35, y = 0.35~0.37) under applied voltage in the range of 6~10 V. The luminance and quantum efficiency of D5 were $17,160cd/m^2$ and 3.8% at 10 V, respectively.

• Journal of Microbiology
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• v.41 no.3
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• pp.207-211
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• 2003

Extracellular protease, from Aeromonas hydrophila Ni 39, was purified 16.7-fold to electrophoretic homogeneity with an overall yield of 19.9％, through a purification procedure of acetone precipitation, and Q Sepharose and Sephacryl S-200 chromatographies. The isoelectric point of the enzyme was 6.0 and the molecular mass, as determined by Sephacryl S-200 HR chromatography, was found to be about 102 kDa. SDS/PAGE revealed that the enzyme consisted of two subunits, with molecular masses of 65.9 kDa. Under standard assay conditions, the apparent $K_{m}$ value of the enzyme toward casein was 0.32 mg/ml. About 90％ of the proteolytic activity remained after heating at 60$^{\circ}C$ for 30 min. The highest rate of azocasein hydrolysis for the enzyme was reached at 60$^{\circ}C$, and the optimum pH of the enzyme was 9.0. The enzyme was inhibited by the serine protease inhibitor, phenylmethylsulfonyl fluoride (PMSF), by about 87.9％, but not by E64, EDTA, pepstatin or 1,10-phenanthroline. The enzyme activity was inhibited slightly by Ca$\^$2＋/, Mg$\^$2＋/ and Zn/supb 2＋/ ions.

• BMB Reports
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• v.32 no.3
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• pp.239-246
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• 1999

A tripeptidase (PepT) was purified to homogeneity from Bacillus subtilis through four sequential chromatographies including DEAE-Sepharose ion exchange, hydroxylapatite, mono-Q FPLC ion exchange, and Superose-12 FPLC gel filtration. The apparent molecular mass of the enzyme was 49,200 Da and 51,400 Da as determined by sodium dodecylsulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography, respectively, and the enzyme exists in a monomeric form. The physicochemical properties of the enzyme were as follows: optimum pH at 7.5, optimum temperature at $60^{\circ}C$, and pI at 4.9. The $K_m$ and $V_{max}$ values of the enzyme were 4.3 mM and 2.5 mmol/min/mg, respectively, with MetAla-Ser as substrate. The B. subtilis PepT requires $Co^{2+}$ ion(s) for activation, while it is inactivated by EOTA and 1,10-phenanthroline, suggesting that it is a metalloprotein. The enzyme was not inhibited by any of serine protease, aspartic protease, or leucine aminopeptidase inhibitors. The enzyme showed comparable activities towards four different substrates including Met-Ala-Ser, Leu-Gly-Gly, Leu-Ser-Phe, and Leu-Leu-Tyr. The amino terminal sequence of PepT determined by Edman degradation was found to be MKEEIIERFTTYVXV and turned out to be identical to that of PepT deduced from a cloned B. subtilis pepT.

• BMB Reports
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• v.34 no.6
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• pp.551-558
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• 2001

We extended the measurable time scale of DNA dynamics to submicrosecond using a long-lifetime metal-ligand complex, $[Ru(phen)_2(dppz)]^{2+}$ (phen=1,10-phenanthroline, dppz=dipyrido[3,2-a:2',3'-c]phenazine) (RuPD), which displays a mean lifetime near 350 ns. We partially characterized the fluorescence resonance energy transfer (FRET) in calf thymus DNA from RuPD to nile blue (NB) using frequency-domain fluorometry with a high-intensity, blue light-emitting diode (LED) as the modulated light source. There was a significant overlap of the emission spectrum of the donor RuPD with the absorption spectrum of the acceptor NB. The F$\ddot{o}$rster distance ($R_0$) that was calculated from the spectral overlap was $33.4\;{\AA}$. We observed dramatic decreases in the steady-state fluorescence intensities of RuPD when the NB concentration was increased. The intensity decays of RuPD were matched the closest by a triple exponential decay. The mean decay time of RuPD in the absence of the acceptor NB was 350.7 ns. In a concentration-dependent manner, RuPD showed rapid intensity decay times upon adding NB. The mean decay time decreased to 184.6 ns at $100\;{\mu}M$ NB. The FRET efficiency values that are calculated from the mean decay times increased from 0.107 at $20\;{\mu}M$ NB to 0.474 at $100\;{\mu}M$ NB concentration. The use of FRET with a long-lifetime metal-ligand complex donor is expected to offer the opportunity to increase the information about the structure and dynamics of nucleic acids.

• BMB Reports
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• v.34 no.6
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• pp.509-516
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• 2001

A genomic DNA fragment that contains the gene, which codes for a novel extracellular serine protease in Burkholderia pseudomallei, was cloned by using pQE40 as a vector. It was maintained in Escherichia coli JM109. The expression of the gene(s) resulted in the production of a 52 kDa protease. The recombinant protease was purified from the culture filtrate via ammonium sulfate fractionation, gel filtration, and anion-exchange chromatography. The purified protease had an optimum pH and temperature of pH 8.9 and $38^{\circ}C$, respectively. The protease activity was inhibited by EGTA, EDTA, and PMSF, but not 1,10-phenanthroline. The first 11 amino acid residues from the N-terminus of the purified protease were identified as LAPNDPYYYGY. PNDPYY was found to show homology to the Bacillus cereus microbial serine protease and B. subtilis PD498 serine protease. These results indicate that the protease that was purified in this study is an extracellular calcium-dependent serine protease. The purified protease was able to digest the human serum 19A, IgG, albumin, and transferrin, as well as bovine muscle actin and myosin. Furthermore, it was able to promote or cause dermonecrosis in experimental rabbits. These results propose the possible role of a novel B. pseudomallei extracellular calcium-dependent serine protease in the virulence of the pathogen.

• Proceedings of the Korean Vacuum Society Conference
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• 2010.08a
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• pp.119-119
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• 2010

다층박막구조를 갖는 유기발광소자는 저분자 증착 기술이 발전함에 따라 다양한 구조로 제작이 가능해 다양한 구조 설계를 통하여 발광특성을 향상할 수 있게 되었다. 다층박막구조에서 유기발광소자의 발광효율을 향상시키기 위하여 다양한 주입층과 수송층을 사용하여 전하의 주입 장벽과 이동도를 제어할 수 있다. 저분자 유기발광소자에서 가장 많이 이용되는 tris(8-hydroxyquinoline) aluminum (Alq3) 또는 7-diphenyl-1, 10-phenanthroline (BPhen)을 단일구조로 전자수 송층으로 사용한 유기발광소자의 발광 메커니즘에 대한 연구가 많이 진행되었지만, Alq3 와 BPhen 을 같이 사용하였을 때 나타나는 전기적 특성과 광학적 특성에 대한 연구는 미미하다. 따라서 본 연구에서는 전자 수송층으로 Alq3 와 BPhen 을 다중 이종구조를 사용하여 녹색 유기발광소자를 제작하고 이의 전기적 특성과 광학적 특성을 연구하였다. 유기발광소자를 제작한 후 Alq3와 BPhen 다중 이종구조의 위치와 이종구조 개수의 변화에 따라 발광 특성 비교를 위하여 인가된 전압에 대한 전류밀도와 휘도, 발광 효율 및 전력 효율을 측정하였다. 다중 이종구조로 제작할 경우 단일 BPhen층의 두께가 얇아지기 때문에 단일 이종구조의 소자보다 BPhen층의 정공차단 능력이 저하되어 저전압에서는 Alq3/BPhen 계면에서의 누설되는 정공의 수가 증가하였다. 또한 이종구조의 수가 증가할수록 단일 이종구조일 때에 비하여 인가된 전압에 대한 전류밀도가 감소하였다. 이는 Alq3와 BPhen 내에서 각각 전자의 이동도가 다르기 때문에 Alq3/BPhen 이종계면에서 전자가 축적되어 공간전하를 형성하므로 내부전계가 형성되어 구동전압이 증가하는 것으로 보인다. 그러나 다중 이종구조로 된 전자 수송층을 포함한 유기발광소자의 발광 효율은 구동전압의 변화에 따라 변하지 않는다. 이종계면의 수가 증가함에 따라 각각의 이종계면에서 축적되는 전자의 양이 감소하기 때문에 고전압에서 발광효율의 저하가 감소하였다. 그러므로 다중 이종구조를 가진 전자수송층 내에서 전자의 주입과 수송에 대한 원리는 안정화된 발광효율을 가지는 유기발광소자를 제작하는데 중요하다.

• Proceedings of the Korean Vacuum Society Conference
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• 2011.08a
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• pp.320-320
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• 2011

차세대 디스플레이로 각광 받고 있는 유기발광소자는 빠른 응답속도, 넓은 시야각 및 얇은 두께로 제작이 가능한 장점들을 가지고 있으나, 고효율 유기발광소자를 제작하기 위하여 엑시톤 형성 효율을 증가시키고 형성된 엑시톤의 소멸을 감소시켜 발광 효율을 증진하는 연구가 활발히 진행되고 있다. 유기발광소자의 발광 효율을 증진하기 위하여 소자의 구조에 대한 구조적 연구와 발광 물질에 대한 재료적 연구 등이 진행되고 있으며, 그 중에서 발광층에 사용하는 인광 물질은 삼중항 상태의 엑시톤을 광자로 천이할 수 있는 특성이 있어서 높은 발광 효율의 유기발광소자 제작이 가능하기 때문에 많은 연구가 진행되고 있다. 그러나 인광 물질을 사용한 유기발광소자의 엑시톤 수명이 형광 물질을 사용한 유기발광소자의 엑시톤 수명보다 길기 때문에, 인광 물질을 사용한 유기발광소자에서 형성된 삼중항 엑시톤끼리 서로 충돌하여 소멸될 확률이 높아지는 문제점이 있다. 또한, 인광물질을 사용한 유기발광소자 동작시에 높은 전류 영역에서 삼중항 엑시톤 형성 양이 많아서 삼중항 엑시톤 소멸 확률이 증가하는 문제점이 있다. 본 연구에서는 고효율 유기발광소자를 제작하기 위하여 유기발광소자의 발광층으로 인광 호스트 물질에 iridium을 포함한 중금속 착화합물 계열의 녹색 인광 도펀트 물질인 tris(2-phenylpyridine) iridium(III) ($Ir(ppy)_3$)를 도핑하였다. 제작된 유기발광소자는 전류 증가에 따른 삼중항 엑시톤 충돌로 인한 발광 효율 감소를 억제하기 위하여 인광 도펀트인 $Ir(ppy)_3$와 같은 lowest unoccupied molecular orbital 준위를 가지는 4,7-diphenyl-1,10-phenanthroline 전자 수송층을 사용하였다. 전기적 및 광학적 특성 분석 결과 제작된 유기발광소자에서 삼중항 엑시톤 소멸을 최소화하여 발광 효율이 증가한 것을 확인하였다. 본 실험의 결과는 $Ir(ppy)_3$을 도핑한 녹색 인광 유기발광소자의 삼중항 엑시톤 충돌을 억제하여 유기발광소자의 발광 효율을 증진하는 메커니즘을 이해하는데 중요하다.

• Journal of the Korean Chemical Society
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• v.39 no.1
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• pp.40-46
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• 1995

A new analytical luminescence method for the Tb+3 and Eu+3 ions was studied using the fluorescence enhancement of the ions on the TLC plate. Compared to the specific emission intensities of the ions in aqueous or ethanol solution, if spotted on the TLC plate, the line intensities were extremely enhanced. There was additional enhancement effect of the lines from the ions on the TLC plate, if treated with ο-phenanthroline. Based on the luminescence enhancement, the detection limit of the ions was lowered more than 6 order of magnitude compared to the luminescence method using solution samples. The energy-transfer mechanism was also explained for the theoretical back ground of the luminescence enhancement.

• Journal of Microbiology and Biotechnology
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• v.17 no.5
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• pp.761-768
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• 2007

Serratia proteamaculans HY-3 isolated from the digestive tract of a spider produces an extracellular protease named arazyme, with an estimated molecular mass of 51.5 kDa. The purified enzyme was characterized as having high activities at wide pH and temperature ranges. We further characterized biochemical features of the enzymatic reactions under various reaction conditions. The protease efficiently hydrolyzed a broad range of protein substrates including albumin, keratin, and collagen. The dependence of enzymatic activities on the presence of metal ions such as calcium and zinc indicated that the enzyme is a metalloprotease, together with the previous observation that the proteolytic activity of the enzyme was not inhibited by aspartate, cysteine, or serine protease inhibitors, but strongly inhibited by 1,10-phenanthroline and EDTA. The araA gene encoding the exoprotease was isolated as a 5.6 kb BamHI fragment after PCR amplification using degenerate primers and subsequent Southern hybridization. The nucleotide sequence revealed that the deduced amino acid sequences shared extensive similarity with those of the serralysin family of metalloproteases from other enteric bacteria. A gene(inh) encoding a putative protease inhibitor was also identified immediately adjacent to the araA structural gene.