• Carbon letters
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• 제8권4호
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• pp.274-279
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• 2007

In order to understand the breakthrough behaviour of iodine vapours on impregnated carbon systems, an active carbon, 80 CTC grade, $12{\times}30$ BSS particle size and $1104\;m^2/g$ surface area, was impregnated with metal salts such Cu, Cr, Ag, Mo and Zn, and an organic compound Triethylene diamine (TEDA) to prepare different carbon systems such as whetlerite, whetlerite/TEDA, whetlerite/KI/KOH and ASZMT. The prepared adsorbents along with active carbon were characterized for surface area and pore volume by $N_2$ adsorption at liquid nitrogen temperature. These carbon systems were compared for their CT (concentration X time) values at 12.73 to 53.05 cm/sec space velocities and 2 to 5 cm carbon column bed heights. The carbon column of 5.0 cm bed height and 1.0 cm diameter was found to be providing protection against iodine vapours up to 5.5 h at 3.712 mg/L iodine vapour concentration and 12.73 cm/sec space velocity. The study clearly indicated the adsorption capacities of carbon systems to be directly proportional to their surface area values. Dead layer with all the prepared carbon systems was found to be less than 2.0 cm indicating it to be minimum bed height to have protection against $I_2$ vapours. Effect of carbon bed height and flow rate was also studied. The active carbon showed maximum protection at all bed heights and flow rates in comparison to all other impregnated carbon systems, showing that only physical adsorption is responsible for the removal of iodine vapours.

• 대한화학회지
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• 제29권2호
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• pp.178-182
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• 1985

비철특수합금중 아연(II) 구리(II)와 마그네슘(II)을 양이온 교환수지(Dowex 50w${\times}$8, 80-100 mesh)와 음이온 교환수지(IRA-400)을 이용하여 이온교환크로마토그라프로서 분리하는 방법을 연구 하였다. 이온교환수지는 25 ${\times}$ 2cm ID 칼럼에 넣고 흐르는 속도는 0.30 ml/min으로 조절하였다. 아연(II), 구리(II), 마그네슘(II)와 같은 비철금속 이온들을 분리하기 위한 좋은 용리액의 조건은 다음과 같다. 0.5M $NaNO_3$ (pH 3.1), 0.2~0.5M HCl + 50~90% Acetone과 1M HAc + 0.1M NaAcf(pH 3.7)였으며 0.1M NaAc + 1M NaAc(pH 3.7), 0.5M HCl + 50% Acetone이 가장 좋은 용리액으로 판명되었다. 분리된 용출액은 원자흡광 광도계로 측정하였으며 특히 아연 (II)은 음이온 교환수지에서 0.12N HCl과 1.5N $NH_4OH$ 수용액으로 분리하고 E.D.T.A로 적정하였다.

• 미생물학회지
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• 제47권3호
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• pp.194-199
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• 2011

알칼리성 protease를 생산하는 호알칼리성 균주를 분리하여 Bacillus pseudofirmus HS-54로 동정하였고, HS-54가 생산하는 알칼리성 protease를 ammonium sulfate 침전, DEAE cellulose chromatography, sephadex G-100 gel filtration을 통과시켜 정제하였는데, 정제된 protease의 분자량은 27 kDa이었다. 정제된 효소의 반응최적 pH는 10.0이었고 pH 7.0-11.0에서 비교적 안정하였다. 또한 정제된 효소의 반응최적 온도는 $50^{\circ}C$이었고 $10-55^{\circ}C$에서 안정하였다. 금속이온에 대한 영향은 $Ca^{2+}$와 $Mg^{2+}$ 등에 의해 효소활성이 촉진되었으나, $Hg^{2+}$, $Zn^{2+}$, $Cu^{2+}$, $Al^{3+}$ 등에 의해서 효소활성이 저해되었다. 본 효소는 PMSF에 의해 강하게 저해를 받는 것으로 보아 serine protease에 속하는 것으로 판단된다.

• Journal of Microbiology and Biotechnology
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• 제11권6호
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• pp.964-972
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• 2001

The kinetics of copper ion biosorption by Pseudomonas stutzeri cells immobilized in alginate was investigated. During the first few minutes of the metal uptake, the copper biosorption was rapid and then became progressively slower until an equilibium was rapid, and then became progressively slower until an equilibrium was reached. At a biomass concentration of 100g/l, the copper biosorption reaction reached approximately 90% of the equilibrium position within 30 min. A Freundich-type adsorption isotherm model was constructed based on kinetics with different amounts of biomass. When using this model, the experimental values only agreed well with the predicted values in a solution containing less than 200 mg/l Cu(II). Desorption of the bound copper ions was achieved using electrolytic solutions of HCl, $H_2SO_4$, EDTA, and NTA (0.1 or 0.5 M). Metal desorption with 0.1 M NTA allowed the reuse of the biosorbent for at least ten consecutive biosorption/desorption cycles, without an apparent decrease in its metal biosorption capability. A packed-bed column reactor of the immobilized biomass removed approximately 95% of the metal in the first 30 liter of wastewater [containing 100 mg/l Cu(II)] delivered at a rate of 20 L/day, and, thereafter, the rate gradually decreased.

• Journal of Microbiology and Biotechnology
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• 제27권6호
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• pp.1120-1127
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• 2017

Marasmius scorodonius secretes an extracellular laccase in potato dextrose broth, and this enzyme was purified up to 206-fold using $(NH_4)_2SO_4$ precipitation and a Hi-trap Q Sepharose column. The molecular mass of the purified laccase was estimated to be ~67 kDa by SDS-PAGE. The UV/vis spectrum of the enzyme was nontypical for laccases, and metal content analysis revealed that the enzyme contains 1 mole of Fe and Zn and 2 moles of Cu per mole of protein. The optimal pH for the enzymatic activity was 3.4, 4.0, and 4.6 with 2,2'-azino-bis(3-ethylbenzothazoline-6-sulfonate) (ABTS), guaiacol, and 2,6-dimethoxy phenol as the substrate, respectively. The optimal temperature of the enzyme was $75^{\circ}C$ with ABTS as the substrate. The enzyme was stable in the presence of some metal ions such as $Ca^{2+}$, $Cu^{2+}$, $Ni^{2+}$, $Mg^{2+}$, $Mn^{2+}$, $Ba^{2+}$, $Co^{2+}$, and $Zn^{2+}$ at a low concentration (1 mM), whereas $Fe^{2+}$ completely inhibited the enzymatic activity. The enzymatic reaction was strongly inhibited by metal chelators and thiol compounds except for EDTA. This enzyme directly decolorized Congo red, Malachite green, Crystal violet, and Methylene green dyes at various decolorization rates of 63-90%. In the presence of 1-hydroxybenzotriazole as a redox mediator, the decolorization of Reactive orange 16 and Remazol brilliant blue R was also achieved.

• 한국미생물·생명공학회지
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• 제30권4호
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• pp.352-358
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• 2002

토양으로부터 maltopentaose생산성 amylase를 분비하는 세균 KSM B-404를 분리하여 그의 형태적, 생리적인 특성을 고려한 결과 Bacillus megaterium으로 동정되었다. 효소는 ($NH_4$)$_2$$SO_4$ 침전 분획, DEAE-Toyopearl 및 Superdex 75 HR 10/30 크로마토그래피로 129배 정제되었으며 21.4%의 활성이 회수되었다. 정제된 효소를 SDS-PACE로 분석한 결과 분자량은 약 68 kDa이었고, 최적 반응 온도는 $50^{\circ}C$이며 $Ca^{2+}$ 이온의 존재 시 열 안정성이 증가하였다. 한편 최적 반응 pH는 6.0~7.0부근이며 알칼리 조건에서도 안정하였다. 또한 효소의 활성은 $Cu^{2+}$ , $Hg^{2+}$ 그리고 특히 Fe/eup 3+/이온 등의 금속이온에 의해 강하게 저해 받았고 acetic anhydride, EDTA , hydroxylamine-HCI, $\rho$ - chloromercuribenzoate 등의 저해제에 의해서 활성이 저해되었으나 concanavalin A에 의한 저해 효과는 나타나지 않았다. 전분의 가수분해 산물을 HPLC로 분석한 결과 maltopentaose가 주산물로 나타났으며 반응 24시간 후 총 가수분해 산물의 약 52%를 차지하였다.

• 생명과학회지
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• 제8권5호
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• pp.497-503
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• 1998

GTase와 CDase를 함께 분비$\cdot$생산하는 B. stearother-mophilus KJl6 균주의 CDase를 ammonium sulfate 침전, DBAE-cellulose, Sephadex G-100 column chromatogra-phy, 및 FPLC로 수율 7%, 비활성 12.4 units/mg, 정제도 87.6배로 정제된 CDase를 얻었으며 SDS-PAGE 상 단일 band를 확인하였다. 정제된 CDase의 분자량은 약 68,000 dalton 이었고 활성 최적 pH와 온도는 6.0와 55$^{\circ}C$였다. pH 안정성은 5.5~8.5의 범위에서 비교적 안정하였으며, 온도 안정성은 5$0^{\circ}C$에서 2시간까지는 안정하였고, 7$0^{\circ}C$에서 1시간 전처리하여도 80% 이상의 잔존활성을 나타내었다. 효소 활성은 $Cu^{+2}$와 $Hg^{+2}$와 같은 금속이온과 p-chlorome-rcuribenzoate, N-bromosuccinimide, mercaptoethanol, dithiothreitol에 의해서 효소활성이 강하게 저해되었다. 기질에 대한 반응 특이성은 $\gamma$ -CD를 가장 잘 분해하였으며, 그 외에 soluble starch나 amylose, amylopectin 등의 기질도 잘 분해하나 이들의 분해속도는 $\gamma$-CD에 비해서는 늦었다. 이들 기질의 최종 분해산물은 maltose였으며, maltose는 거의 분해되지 않았다.

• Bulletin of the Korean Chemical Society
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• 제32권2호
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• pp.444-450
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• 2011

A novel method that utilizes poly(5-methyl-2-thiozyl methacrylamide-co-2-acrylamido-2-methyl-1-propanesulfonic acid-co-divinylbenzene) [MTMAAm/AMPS/DVB] as a solid-phase extractant was developed for simultaneous preconcentration of trace Cd(II), Co(II), Cr(III), Cu(II), Fe(III), Mn(II), Ni(II), Pb(II), and Zn(II) prior to the measurement by flame atomic absorpiton spectrometry (FAAS). Experimental conditions for effective adsorption of the metal ions were optimized using column procedures. The optimum pH value for the simultaneously separation of the metal ions on the new adsorbent was 2.5. Effects of concentration and volume of elution solution, sample flow rate, sample volume and interfering ions on the recovery of the analytes were investigated. A high preconcentration factor, 100, and low relative standard deviation values, $\leq$1.5% (n = 10), were obtained. The detection limits (${\mu}gL^{-1}$) based on the 3s criterion were 0.18 for Cd(II), 0.11 for Co(II), 0.07 for Cr(III), 0.12 for Cu(II), 0.18 for Fe(III), 0.67 for Mn(II), 0.13 for Ni(II), 0.06 for Pb(II), and 0.09 for Zn(II). The validation of the procedure was performed by the analysis of two certified reference materials. The presented method was applied to the determination of the analytes in various environmental samples with satisfactory results.

• 미생물학회지
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• 제14권2호
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• pp.65-74
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• 1976

Atternaria sp. was isolated from soil and crude cellulases were prepared from wheat bran culture of the fungus. The activities of the crude enzyme were studied on five different subvstrates and some phsical properties were also examined, crude enzymes were purified by column chromatography on DEAE Sephadex and Sephadex, Isozymes were separated some of which were active specifically on DEAE cellulose and some were primarily active on cellulose and CM-cellulose. The optimal points of pH and temperature for the crude enzyme were varied depending on the substrates ; On cellulose they were at pH 6.0 and 40.deg.C, on CM-cellulose at pH's 4.0 and 6.0 and 60.deg.C, and on DEAW-cellulose at pH 5.0 and 50.deg.C. Two active fractions, F-1 and F-II on Na-CMC was used as substrate the Km values of crude enzyme, F-I and F-II were calculated to be $4{\times}10^{-5}$ , 1.1 * 10$^{-4}$ , and $1.25{\times}10^{-4}mN$ resepctively. The Ki value of $Cu^{++}$ for crude enzyme was$4{\times}^{-4}mN$ , while that of $Nm^{++}$ while in the same concentration of $Mn^{++}$ it reached to 91%. Some 57% activity of F-1 was inhibited in s mN $Cu^{++}$, whereas it was inhibited as much as 81% in the same concentration above the concentration of 0.3 mM with tis activity reaching up to 137% in 2 mM. On the other hand the F-11 was inhibited by the presence of M $n^{++}$ and some 67% activity was inhibited at 2mM.

• 미생물학회지
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• 제45권3호
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• pp.257-262
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• 2009

Bacillus licheniformis WL-12의 carboxymethyl cellulase (cellulase) 유전자를 함유한 대장균 균체 파쇄상등액으로부터 DEAE-Sepharose와 Q-Sepharose 컬럼 크로마토그래피를 통해 cellulase를 정제하였다. 정제된 효소의 비활성은 163 U/mg이었으며, SDS-PAGE에 의해 측정된 분자량은 약 49.5 kDa으로 나타났다. pH 5.5와 $55^{\circ}C$에서 최대 반응활성을 보였으며, SDS (5mM)에 의해서는 cellulase의 활성이 완전히 저해되었고 $Cu^{2+}$5mM)에 의해서는 약간 증진되었다. 정제된 cellulase는 CMC, konjac, barley $\beta$-glucan과 lichenan을 가수분해하였으나 xylan, locust bean gum 및 p-nitrophenyl-$\beta$-glucopyranoside를 분해하지 못하였다. Cellooligosaccharides를 정제된 WL-12 cellulase로 분해하였을 때 cellobiose와 cellotriose가 주된 최종 반응산물로 관찰되었으며 cellobiose보다는 중합도가 큰 cellotriose, cellotetrasoe와 cellopentaose는 분해하였으나 cellobiose는 분해하지 못하는 것으로 확인되었다.