• 대한화학회지
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• 제24권1호
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• pp.25-33
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• 1980

토양에서 분리한 Pseudomonadaceae 속 박테리아로부터 pyrocatechase를 추출, 분리 정제하였으며, 이 효소의 특성을 검토한 결과 pyrocatechase는 catechol에 대하여 기질 특이성을 보여줌을 알았다. 효소 활성도의 최적조건은 pH 7∼10 부근과 온도 $35^{\circ}C$임을 알았으며, catechol에 대한 $K_m$값은 $1.9{\times}10^{-6}M$ 로 얻어졌다. 기질 유도체에 의한 효소 저해 실험결과 벤젠 고리의 ortho 위치에 두개의 수산기는 효소-기질간의 결합반응에 참여될 것이라고 추측했다. 기타 SH-잔기와 작용하는 화합물 또는 중금속 이온등의 첨가에 따른 효소 활성도의 저해 효과를 검토 하였으며, 효소 활성부위에 대하여도 검토해 보았다.

• Journal of Magnetics
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• 제13권3호
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• pp.110-113
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• 2008

In this study, heavy rare earth garnet $Tb_2Bi_1Ga_1Fe_4O_{12}$ powders were fabricated by a sol-gel and vacuum annealing process. The crystal structure was found to be single-phase garnet with a space group of Ia3d. The lattice constant $a_0$ was determined to be 12.465 ${\AA}$. From the analysis of the vibrating sample magnetometer (VSM) hysteresis loop at room temperature, the saturation magnetization and coercivity of the sample are 7.64 emu/g and 229 Oe, respectively. The N$\acute{e}$el temperature($T_N$) was determined to be 525 K. The M$\ddot{o}$ssbauer spectrum of $Tb_2Bi_1Ga_1Fe_4O_{12}$ at room temperature consists of 2 sets of 6 Lorentzians, which is the pattern of single-phase garnet. From the results of the M$\ddot{o}$ssbauer spectrum at room temperature, the absorption area ratios of Fe ions on 24d and 16a sites are 74.7% and 25.3%(approximately 3:1), respectively. These results show that all of the non-magnetic Ga atoms occupy the 16a site by a vacuum annealing process. Absorption area ratios of Fe ions are dependent not only on a sintering condition but also on the temperature of the sample. It can then be interpreted that the Ga ion distribution is dependent on the temperature of the sample. The M$\ddot{o}$ssbauer measurement was carried out in order to investigate the atomic migration in $Tb_2Bi_1Ga_1Fe_4O_{12}$.

• 약학회지
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• 제41권5호
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• pp.615-621
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• 1997

Dehydropeptidase-I (DHP-I) was solubilized from porcine kidney by treatment with n-butanol and partially purified 19.25 fold by $(NH_4)_2SO_4$ precipitation, DEAE-Sepharose CL-6B ion exchange chromatography and Sephacryl S-300 HR chromatography with an overall yield of 19.16. DHP-I showed its optimal activity at pH 7.5 and 25$^{\circ}C$. Its activity was stable under neutral and alkaline conditions, but was disappeared under acidic condition. And DHP-I was heat-labile and its activity remained at 45$^{\circ}C$ for 3hrs. The enzyme was not inhibited by dicationic ions, while its activity was increased by $Co^{2+}$(1mM) and $Zn^{2+}$ (0.1mM). The enzyme was inhibited by EDTA and N-ethylmaleimide. The relative molecular mass of DHP-I was estimated to be approximately 100kDa by gel filtration chromatography. The $K_m$ value of DHP-I for glycyldehydrophenylalanine (GDHP) was 1.98mM. DWP20418 [(1R, 5S, 6S)-6-[1-(R)-Hydroxyethyl]-1-methyl-2-[(2S, 4S)-2-(piperazinylcarbonyl)-1-(R)-hydroxyethyl)pyrrolidine-4-thio]carbapen-2-em-3-carboxylic acid], compared with meropenem (MEPM), was rather easily hydrolized by DHP-I, while it was four times more resistant than imipenem (IPM) to DHP-I.

• 농업과학연구
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• 제39권2호
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• pp.255-261
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• 2012

A bacterium AB-55, isolated from waste mushroom bed of Agaricus bisporus in Sukseong-myeon, Buyeo-gun, Chungcheongnam-do, Korea, was screened onto xylan agar congo-red plate by the xylanolysis method and was used to produce an xylanase in shaker buffle flask cultures containing oat spelt xylans. The phylogenetic analysis using 16S rRNA gene sequence data showed that the strain AB-55 had the highest homology (99.0%) with Bacillus subtilis and it was named as Bacillus subtilis AB-55. A xylanase was purified by ammonium sulfate precipitation (50~80%), gel filtration on sephacryl S-300, and ion exchange chromatography on DEAE sepharose FF. The molecular weight of the xylanase was estimated as 44 kDa by SDS-PAGE. Optimal pH and temperature for the xylanase activity was pH 7 and $50^{\circ}C$, respectively. N-terminal amino acid sequence of the enzyme was identified as Ser-Ala-Val-Lys-His-Gly-Ala-Ile-Val-Phe. The substrate specificity of the enzyme exhibited that it hydrolyzed efficiently oat spelt xylan as well as beechwood xylan, but showed no activity against Avicel and carboxymethyl clellulose (CMC). The enzyme activity was enhanced by $Fe^{2+}$ and $Mn^{2+}$ whereas was entirely inhibited by $Hg^+$.

• 한국식품저장유통학회지
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• 제20권3호
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• pp.435-439
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• 2013

닭털 단백질을 단백질 가수분해 효소인 Flavouzyme을 이용하여 8시간 동안 가수분해하여 가수분해물을 제조하였다. 닭털 단백질 가수분해물로부터 저분자량 펩타이드를 얻고자 한외여과를 하였고, 철분 결합 펩타이드를 분리하기 위해 Q-Sepharose와 Sephadex G-15 컬럼을 사용하여 분리하였다. 그 결과, 철분 결합력이 높은 펩타이드 분획, F12를 분리하였고, 향후 철분 보충제로써 활용이 가능하다고 판단된다.

• 한국식품과학회지
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• 제26권4호
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• pp.375-381
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• 1994

토양을 대상으로 하여 CGTase를 생산하는 균주를 분리, 선별하여 Bacillus stearothermophilus KY-126을 얻었다. CGTase의 정제는 ammonium sulfate precipitation, ion exchange chromatography, gel filtration의 과정을 통해 분리 정제하여 단일 효소를 얻었으며, 분자량은 약 67,000이었다. 효소 반응의 최적 온도는 $65^{\circ}C$였으며, $55^{\circ}C$에서 30분간 열처리에도 비교적 열에 안정하였다. 최저 활성 pH는 5.5였고 pH5.5에서 10.5까지 비교적 안정하였다. $HgCl_{2}$에 의해 저해를 받았으며, 그 외의 금속 이온에는 저해를 받지 않았다. Soluble starch로부터 CD의 전환율은 43%이었으며, ${\alpha}-:,\;{\beta}-:,\;{\gamma}-$, CD의 생성 비율은 2.9 : 2.1 : 1이었다.

• Journal of Microbiology and Biotechnology
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• 제6권1호
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• pp.1-6
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• 1996

A bacterial strain NS70 producing an alkaline protease was isolated from soil samples taken near a hot spring and identified as Bacillus licheniformis by its morphological and physiological properties and cellular fatty acid analysis. The isolated alkaline protease was purified by ammonium sulfate fractionation, DEAE-, CM-, and Phenyl-Sepharose column chromatography. The molecular weight of the purified enzyme was estimated to be 32, 000 Da by sodium dodecylsulfate polyacrylamide gel electrophoresis. Its optimal pH and temperature for proteolytic activity against Hammarsten casein were 12 and $65^{\circ}C$, respectively. The enzyme was stable at alkaline pH range from 6.0 to 12.0, and fairly stable up to $65^{\circ}C$. The enzyme was inhibited by phenylmethylsulfonyl fluoride but not by EDTA and N-ethylmaleimide indicating that the enzyme is serine protease. Enzyme activity was markedly inhibited by $Hg^{2+}$ and $Cu^{2+}$. Autolytic phenomena were observed on purified protease NS70 but autolysis was reduced by the addtion of $Ca^{2+}$ ion or bovine serum albumin.

• Journal of Microbiology and Biotechnology
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• 제21권3호
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• pp.256-262
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• 2011

A 20.9-kDa metalloprotease was isolated from dried fruiting bodies of the wild basidiomycete mushroom Lepista nuda. The N-terminal amino acid sequence of the protease was seen to be ATFVLTAATNTLFTA, thus displaying no similarity with the sequences of previously reported metalloproteases. The protease was purified using a procedure that entailed ion-exchange chromatography on CM-Cellulose, Q-Sepharose, and Mono S, and FPLC-gel filtration on Superdex 75. The protease functioned at an optimum pH of 7.0 and an optimum temperature of $50^{\circ}C$. It was also noted that the protease demonstrated a proteolytic activity of 1,756 U/mg toward casein. The $K_m$ of the purified protease toward casein was 6.36 mg/ml at a pH of 7.0 and with a temperature of $37^{\circ}C$, whereas the $V_{max}$ was 9.11 ${\mu}g\;ml^{-1}\;min^{-1}$. The activity of the protease was adversely affected by EDTA-2Na, suggesting that it is a metalloprotease. PMSF, EGTA, aprotinin, and leupeptin exerted no striking inhibitory effect. The activity of the protease was enhanced by $Fe^{2+}$, but was curtailed by $Cd^{2+}$, $Cu^{2+}$, $Hg^{2+}$, $Pb^{2+}$, $Zn^{2+}$, and $Fe^{2+}$ ions. The protease also exhibited inhibitory activity against HIV-1 reverse transcriptase with an $IC_{50}$ value of 4.00 ${\mu}M$. The $IC_{50}$ values toward hepatoma Hep G2 and leukemia L1210 cells in vitro were 4.99 ${\mu}M$ and 3.67 ${\mu}M$, respectively.

• 미생물학회지
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• 제30권2호
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• pp.71-77
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• 1992

Serratia marcescens ATCC 21074 의 세포배양액으로 부터 순수분리한 metalloprotease 의 자가분해성 및 안정성과 관련된 몇가지 효소적 특성을 조사하였다. 최적 반응온도와 pH 는 각각 37.deg.C, pH 8.0 였으며 안정성은 pH 5.0-11.0 범위에서, 온도의 경우 10-37.deg.C 에서 비교적 안정한 것으로 나타냈다. Differential scanning calorimeter 로 이효소의 열적 성질을 분석한 결과 변셩 시작 온도는 37.6 .deg.C, endothermic peak 온도는 43.2 .deg.C, enthaply 변화량은 -8.4 mJ/mg 이었다. 이 효소는 30.deg.C 에서 24 시간 동안 거의 자가분해가 일어나지 않았으나 변성된 단백질의 셩우 쉽게 자가분해되는 것으로 나타났다. 또한 이효소는 trypsin, .alpha.-chymotrypsin, elastase 에 의해서 분해되지 않았으나 분해되지 않았으나 thermolysin 에 의해서는 쉽게 분해되었다.

• 한국수소및신에너지학회논문집
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• 제25권1호
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• pp.1-10
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• 2014

Ceria ($CeO_2$) was used to scavenge free radicals which attack the membrane in the polymer electrolyte membrane water electrolysis (PEMWE) circumstance and to increase the duration of the membrane. In order to improve the electrochemical, mechanical and electrocatalytic characteristics, engineering plastic of the sulfonated polyether ether ketone (SPEEK) as polymer matrix was prepared in the sulfonation reaction of polyether ether ketone (PEEK) and the organic-inorganic blended composite membranes were prepared by sol-gel casting method with loading the highly dispersed ceria and cesium-substituted phophomolybdic acid(Cs-MoPA) with cross-linking agent contents of 0.01mL. In conclusion, CL-SPEEK/$Cs_{(2.5)}$-MoPA/ceria(1%) membrane showed the optimum results such as 0.1095S/cm of proton conductivity at $80^{\circ}C$, 2.906meq./g-dry-membrane of ion exchange capacity and mechanical characteristics, and 49.73MPa of tensile strength which were better than Nafion 117 membrane.