• 미생물학회지
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• 제30권4호
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• pp.310-315
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• 1992

수용액으로부터 $Pb^{2+}$ 의 흡수와 분리를 Staphylococcus epidermidis 를 이용하여 조사하였다. 흡수된 $Pb^{2+}$의 양을 초기 $Pb^{2+}$ 의 양에 대한 비율로 나타낸 것을 흡수율이라고 정의할 경우, 세균체의 농도가 높을수록 흡수율은 증가하였으며 세균체 단위 중량당 흡수율은 감소하였다. $Pb^{2+}$ 의 흡수율은 수용액의 pH 가 상승함에 따라 점차 증가하다가 최고치를 나타낸 후 감소하는 경향을 보였으며 $Pb^{2+}$ 의 농도가 증가할수록 흡수율의 최고치는 더 낮은 pH 에서 나타났다. HCI 과 EDTA 는 효과적인 탈락체로 작용하였으며 흡수와 탈착 cycle 의 횟수에 따른 세균체의 $Pb^{2+}$에 대한 흡수 능력에는 거의 변화가 없었다.$Pb^{2+}$ 이 다른 중금속 이온과 함께 혼재할 경우 세균내의 결합위치에 대한 경쟁적인 흡수로 인하여 $Pb^{2+}$ 의 흡수율이 변화하였으며, 공존하는 중금속 이온의 이온 반경이 작을수록$Pb^{2+}$ 의 흡수율이 더 크게 감소하였다.

• 공업화학
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• 제1권1호
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• pp.83-90
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• 1990

PbTe, SnTe, PbSnTe계 반도체는 저온 열전재료로서 이들의 화학조성과 비화학양(nonstoichiometry)은 열전 특성에 중요한 인자가 된다. 본 연구에서는 $(Pb_1\;_xSn_x)_1$ $_yTe_y$의 x=0.1, 0.2, 0.3, 0.4, 0.5인 고용체 시편을 제조하여 이들의 조성을 분석하고 화학조성과 전기전도도 및 열기전력과의 상관 관계를 조사하였다. 조성분석을 위하여 Pb의 함량은 EDTA와 Pb(II) 표준용액을 이용한 착화합물 역적정법을, Te의 함량은 $KMnO_4$와 Fe(II)표준용액을 이용한 산화환원 역적정법을 사용하였다. 또한 300K-750K의 온도범위에서 직류 4접점법에 의해 전기전도도를, Heat Pulse법에 의해 열기전력을 측정하였다. 모든 시편은 금속성분 (Pb+Sn) 보다는 Te의 양이 많은 비화학양의 조성을 보이며 p - 형의 반도성을 가졌고 주석의 함량이 증가할수록 비화학양도 증가하였다. 열기전력의 측정으로 시편의 주 전하나르개는 정공임을 확인할 수 있었고 비화학양에 따른 열기전력의 변화를 saturation 영역 내에서 온도에 따른 Fermi Level의 변화폭과 관련지어 설명하였다. x=0.1인 시편은 약 670K 에서 p - 형으로부터 n - 형으로 전도특성이 전환되었는데 이는 이온도에서 saturation영역에서 intrinsic영역으로 전이되며 전자의 이동도가 정공의 이동도보다 크다는 사실로부터 설명되었다.

• Journal of the korean society of oceanography
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• 제34권1호
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• pp.49-57
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• 1999

A red tide organism, Amphidinium carterae was incubated under different iron/chelator and nitrate concentrations to investigate the factors controlling the growth. The chelation capacity played a critical role in regulating the nitrate reductase (NR) activity and in vivo fluorescence of this organism. However, there was a significant difference between the NR activity and in vivo fluorescence in response to trace metals and chelator treatments. In vivo fluorescence was the highest in FeEDTA 10 ${\mu}$M treatments and the lowest in DTPA 10 ${\mu}$M treatments. This indicates that the availability of the trace metal is important in regulating the in vivo fluorescence of this photosynthetic microalgae In contrast, NR activity showed the highest values in trace metal enriched treatments, and trace metal + DTPA treatments showed fairly high NR activities. This suggests that DTPA treatment did not hinder the NR activity as much as it did in vivo fluorescence. In vivo fluorescence and NR activity increased with nitrate concentration of up to 50 ${\mu}$M and remained relatively constant or the rate of increase decreased above that concentration, indicating that initial nitrate concentration of higher than a certain level would not accelerate the growth of A. carterae. Further investigation is needed to elucidate the reason for the difference in timing sequence between the NR and in vivo fluorescence in response to different metal treatments and chelation capacity.

• Journal of Microbiology and Biotechnology
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• 제18권4호
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• pp.663-669
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• 2008

The solvent-tolerant bacterium Enterobacter sp. VKGH12 is capable of utilizing n-butanol and contains an $NAD^+$-dependent n-butanol dehydrogenase (BDH). The BDH from n-butanol-grown Enterobacter sp. was purified from a cell-free extract (soluble fraction) to near homogeneity using a 3-step procedure. The BDH was purified 15.37-fold with a recovery of only 10.51, and the molecular mass estimated to be 38 kDa. The apparent Michaelis-Menten constant ($K_m$) for the BDH was found to be 4 mM with respect to n-butanol. The BDH also had a broad range of substrate specificity, including primary alcohols, secondary alcohols, and aromatic alcohols, and exhibited an optimal activity at pH 9.0 and $40^{\circ}C$. Among the metal ions studied, $Mg^{2+}$ and $Mn^{2+}$ had no effect, whereas $Cu^{2+},\;Zn^{2+}$, and $Fe^{2+}$ at 1 mM completely inhibited the BDH activity. The BDH activity was not inhibited by PMSF, suggesting that serine is not involved in the catalytic site. The known metal ion chelator EDTA had no effect on the BDH activity. Thus, in addition to its physiological significance, some features of the enzyme, such as its activity at an alkaline pH and broad range of substrate specificity, including primary and secondary alcohols, are attractive for application to the enzymatic conversion of alcohols.

• 한국해양학회지
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• 제11권2호
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• pp.64-70
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• 1976

기수호인 화진포에 대한 생태학적인 연구가 여러 차례에 걸쳐 실시된 바 있으나( 홍사오외 1969; 엄규백, 1971, 1973; 전승관 외 1969; 변충규 외 1975) 현생퇴적물에 대한 퇴적환경적 연구는 실시된 바 없다. 따라서 본 연구에서는 화진포의 퇴적물에 대한 조직표준치와 분포 특성 및 호수퇴적물중에 포함된 점토광물의 종류와 호수퇴적물의 화학성분을 퇴적과정의 퇴적요인으로 하여 본 역의 현생퇴적환경특성을 밝히고자 한다.

• Journal of Microbiology and Biotechnology
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• 제21권6호
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• pp.627-636
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• 2011

A commercially important alkaline protease, produced by Bacillus sp. RRM1 isolated from the red seaweed Kappaphycus alvarezii (Doty) Doty ex Silva, was first recognized and characterized in the present study. Identification of the isolated bacterium was done using both biochemical characterization as well as 16S rRNA gene sequencing. The bacterial strain, Bacillus sp. RRM1, produced a high level of protease using easily available, inexpensive agricultural residues solid-state fermentation (SSF). Among them, wheat bran was found to be the best substrate. Influences of process parameters such as moistening agents, moisture level, temperature, inoculum concentration, and co-carbon and co-nitrogen sources on the fermentation were also evaluated. Under optimized conditions, maximum protease production (i.e., 2081 U/g) was obtained from wheat bran, which is about 2-fold greater than the initial conditions. The protease enzyme was stable over a temperature range of 30-$60^{\circ}C$ and pH 6-12, with maximum activity at $50^{\circ}C$ and pH 9.0. Whereas the metal ions $Na^+$, $Ca^{2+}$, and $K^+$ enhanced the activity of the enzyme, others such as $Hg^{2+}$, $Cu^{2+}$, $Fe^{2+}$, $Co^{2+}$, and $Zn^{2+}$ had rendered negative effects. The activity of the enzyme was inhibited by EDTA and enhanced by $Cu^{2+}$ ions, thus indicating the nature of the enzyme as a metalloprotease. The enzyme showed extreme stability and activity even in the presence of detergents, surfactants, and organic solvents. Moreover, the present findings opened new vistas in the utilization of wheat bran, a cheap, abundantly available, and effective waste as a substrate for SSF.

• 한국재료학회:학술대회논문집
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• 한국재료학회 2011년도 추계학술발표대회
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• pp.33.1-33.1
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• 2011

Strontium doped lanthanum manganite (LSM) with perovskite structure for SOFC cathode material shows high electrical conductivity and good chemical stability, whereas the electrical conductivity at intermediate temperature below $800^{\circ}C$ is not sufficient due to low oxygen ion conductivity. The approach to improve electrical conductivity is to make more oxygen vacancies by substituting alkaline earths (such as Ca, Sr and Ba) for La and/or a transition metal (such as Fe, Co and Cu) for Mn. Among various cathode materials, $LaSrMnCuO_3$ has recently been suggested as the potential cathode materials for solid oxide fuel cells (SOFCs). As for the Cu doping at the B-site, it has been reported that the valence change of Mn ions is occurred by substituting Cu ions and it leads to formation of oxygen vacancies. The electrical conductivity is also affected by doping element at the A-site and the co-doping effect between A-site and B-site should be described. In this study, the $La_{1-x}Sr_xMn_{0.8}Cu_{0.2}O_{3{\pm}{\delta}}$ ($0{\leq}x{\leq}0.4$) systems were synthesized by a combined EDTA-citrate complexing process. The crystal structure, morphology, thermal expansion and electrical conductivity with different Sr contents were studied and their co-doping effects were also investigated.

• Journal of Microbiology and Biotechnology
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• 제18권9호
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• pp.1555-1563
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• 2008

A novel $\alpha$-amylase ($\alpha$-1,4-$\alpha$-D-glucan glucanohydrolase, E.C. 3.2.1.1), ScAmy43, was found in the culture medium of the phytopathogenic fungus Sclerotinia sclerotiorum grown on oats flour. Purified to homogeneity, ScAmy43 appeared as a 43 kDa monomeric enzyme, as estimated by SDS-PAGE and Superdex 75 gel filtration. The MALDI peptide mass fingerprint of ScAmy43 tryptic digest as well as internal sequence analyses indicate that the enzyme has an original primary structure when compared with other fungal a-amylases. However, the sequence of the 12 N-terminal residues is homologous with those of Aspergillus awamori and Aspergillus kawachii amylases, suggesting that the new enzyme belongs to the same GH13 glycosyl hydrolase family. Assayed with soluble starch as substrate, this enzyme displayed optimal activity at pH 4 and $55^{\circ}C$ with an apparent $K_m$ value of 1.66 mg/ml and $V_{max}$ of 0.1${\mu}mol$glucose $min^{-1}$ $ml^{-1}$. ScAmy43 activity was strongly inhibited by $Cu^{2+}$, $Mn^{2+}$, and $Ba^{2+}$, moderately by $Fe^{2+}$, and was only weakly affected by $Ca^{2+}$ addition. However, since EDTA and EGTA did not inhibit ScAmy43 activity, this enzyme is probably not a metalloprotein. DTT and $\beta$-mercaptoethanol strongly increased the enzyme activity. Starting with soluble starch as substrate, the end products were mainly maltotriose, suggesting for this enzyme an endo action.

• BMB Reports
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• 제38권1호
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• pp.17-23
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• 2005

During the screening of xylanolytic enzymes from locally isolated fungi, one strain BCC14405, exhibited high enzyme activity with thermostability. This fugal strain was identified as Aspergillus cf. niger based on its morphological characteristics and internal transcribed spacer (ITS) sequences. An enzyme with xylanolytic activity from BCC14405 was later purified and characterized. It was found to have a molecular mass of ca. 21 kDa, an optimal pH of 5.0, and an optimal temperature of $55^{\circ}C$. When tested using xylan from birchwood, it showed $K_m$ and $V_{max}$ values of 8.9 mg/ml and 11,100 U/mg, respectively. The enzyme was inhibited by $CuSO_4$, EDTA, and by $FeSO_4$. The homology of the 20-residue N-terminal protein sequence showed that the enzyme was an endo-1,4-$\beta$-xylanase. The full-length gene encoding endo-1,4-$\beta$-xylanase from BCC14405 was obtained by PCR amplification of its cDNA. The gene contained an open reading frame of 678 bp, encoding a 225 amino acid protein, which was identical to the endo-1,4-$\^{a}$-xylanase B previously identified in A. niger.

• Journal of Microbiology and Biotechnology
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• 제8권6호
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• pp.639-644
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• 1998

Extracellular serine proteases were isolated from a soil bacterium, alkalophilic coryneform bacterium TU-19, which have been grown in a liquid medium optimized at 3$0^{\circ}C$ and pH 10.0. Three different sizes, 120 kDa (protease I), 80 kDa (protease II), and 45 kDa (protease III), of serine pro teases were purified using Sephadex G-150 and QAE-Sephadex chromatography (Kang et al. 1995. Agric. Chem Biotech. 38: 534-540). SDS-PAGE showed that the 120 kDa protease was degraded into the 80 kDa protease in 20 mM Tris-HCI (pH 8.0) buffer solution. This degradation was enhanced in the presence of 0.5 M NaCl and 5 mM EDTA, but was inhibited in the presence of 5 mM $CaCl_2$. These results indicated that the $Ca^{2＋}$ ion seems to stabilize the 120 kDa protease like other proteases derived from Bacillus species. The $NH_2$-terminal amino acid sequences of the 10 residues of both proteases were completely identical: Met-Asn-Thr-Gln-Asn-Ser-Phe-Leu-Ile-Lys. In contrast to this, the 80 kDa protease has 1.5 times higher specific activity than the 120 kDa protease does (Kang et al. 1995. Agric. Chern. Biotech. 38: 534-540). Therefore the C-terminal of the 120 kDa protease seems to be autolyzed to the 80 kDa protease but this autolysis did not decrease the protease activity. Optimum pH and temperature of both 80 kDa and 120 kDa proteases were pH 10.5 and $45^{\circ}C$, respectively, and pH and thermal stability were almost identical. Several divalent ions except the $Fe^{2＋}$ ion showed similar effects on activities of both proteases, which are similarly resistant to three different detergents.