• 자원리싸이클링
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• 제30권3호
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• pp.30-40
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• 2021

본 연구는 미생물의 접촉 및 비접촉 매커니즘에 따른 비소의 미생물 침출 효율을 보여준다. 12-14 kDa의 반투과성막으로 구성된 분리시스템에서 Acidithiobacillus ferroxidans와 광물찌꺼기의 흡착을 제어하며 접촉 및 비접촉 시스템을 구분하였으며 1.0% 및 0.5% w/v의 두 가지 광액 농도에서 침출효율을 비교하였다. 회분식 미생물 침출 실험을 10일간 수행하면서 비소와 철의 총 농도, 철 이온종 변화, pH, 산화환원전위를 비교하며 박테리아 활동을 확인하였다. 높은 광액 농도인 1.0%에서 박테리아의 흡착에 의해 비소 침출 효율이 20.0%에서 44.9%로 증가하였다. 이러한 결과는 박테리아의 접촉 메커니즘이 광물찌꺼기 내 비소 침출에 큰 영향을 준다는 것을 보여준다. 따라서, 광물찌꺼기 내 비소 제거는 2단계 또는 비접촉 미생물 침출 방법이 1단계 또는 접촉 미생물 침출 방법보다 효율적이지 않다는 것을 보여주었다.

• 한국식품저장유통학회지
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• 제17권3호
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• pp.320-327
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• 2010

연근즙 첨가수준에 따라 백김치를 제조한 후 $5^{\circ}C$에서 4주간 저장하면서 숙성 중의 이화학적, 관능적 특성을 조사하였다. 연근즙의 첨가수준이 증가할수록 pH는 감소, 산도는 반대로 증가하는 경향을 보였고 숙성기간 중에도 같은 경향을 보였다. 탁도는 첨가수준이 증가할수록 증가함을 볼 수 있었으며, 숙성 2주까지는 대조군의 비해 첨가군의 경우 탁도가 증가하는 경향을 보였으나 숙성 3주, 4주에서는 약간 더 감소하는 경향을 보였다. 색도 L 값과 a 값은 연근즙 첨가수준이 증가할수록 감소하였고, b 값은 증가하였다. 환원당은 연근즙 3%와 6% 첨가군의 경우 증가하였다가 연근즙 9%와 12% 첨가군의 경우 감소하는 경향을 보였다. 숙성기간에 따라서는 감소하는 경향을 볼 수 있었다. 비타민 C함량은 대조군보다 연근즙 첨가군의 경우 모든 숙성기간에서 더 높게 나타났다. 경도는 대조군보다는 모든 첨가군의 경우 약간 높은 값을 보였지만 첨가수준에 따른 일정한 경향은 보이지 않았다. 숙성기간에 따른 변화로는 숙성기간이 증가할수록 감소하는 경향을 보였다. 관능검사결과에서는 연근즙 6% 첨가군의 경우 색, 냄새, 아삭아삭한 정도 및 전체적인 기호도가 가장 높게 나타나 백김치에 연근즙의 첨가수준이 6%정도가 적절한 것으로 나타났다.

• Journal of Microbiology and Biotechnology
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• 제10권4호
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• pp.559-563
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• 2000

A dextransucrase gene (dsrB742) that expresses a dextransucrase to synthesize mostly ${\alpha}-1{\rightarrow}6$ linked dextran with a low amount (3-5%) of ${\alpha}-1{\rightarrow}3$ branching was cloned and sequenced from Leuconostoc mesenteroides B-742CB. The 6.1-kb PstI fragments were ligated with pGEM-3Zf(-) and transformed into E. coli $DH5{\alpha}$. The recombinant clone (pDSRB742) synthesized dextran on an agar plate containing 2% (w/v) sucrose. The dextran synthesized was hydrolyzed with Penicillium endo-dextranase. The hydrolyzate was composed of glucose, isomaltose, isomaltotriose, and branced pentasaccharide. The nucleotide sequence of dsrB742 showed one open reading frame (ORF) composed of 4,524 bp encoding dextrasnsucrase. The deduced amino acid sequence revealed a calculated molecular mass of 168.6 kDa. It also showed an activity band of 184 kKa on a non-denaturing SDS-PAGE (10%). The amino acid sequence of DSRB742 exhibited a 50% similarity with DSRA from L. mesenteroides B-1299, a 70% similarity with DSRS from L. mesenteroides B-512 (F, FMCM) and a 45-56% similarity with Streptococcal GTFs.

• 한국결정학회지
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• 제15권1호
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• pp.40-43
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• 2004

The peptide deformylase from the pathogenic bacterium Staphylococcus aureus has been over-expressed in Escherichia coli and crystallized in the presence of the inhibitor actinonin at 297 K using polyethylene glycol 20000 as a precipitant. X-ray diffraction data have been collected to 2.2 ${\AA}$ resolution. The crystal is trigonal, belonging to the space group $P3_121$ (or its enantiomorph $P3_221$), with unit cell parameters of a = b = 62.70 ${\AA}$ c = 108.23 ${\AA}$, ${\alpha}\;=\;{\beta}\;=\;90^{\circ},\;and\;{\gamma}\;=\;120^{\circ}$. An asymmetric unit contains a monomer of the recombinant enzyme, giving a $V_M$ of 2.84 ${\AA}^3\;Da^_{-1}$ and a solvent content of 56.7%.

• BMB Reports
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• 제34권4호
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• pp.310-315
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• 2001

The uneven distribution of acidic and basic chitinases in different parts of rice seed, and also the characterization of hull-specific chitinases, are reported here. After extraction of chitinases from polished rice, bran, and rice hulls, the chitinases were separated into acidic and basic fractions, according to their behavior on an anion exchanger column. Both fractions from different parts of rice seed showed characteristic activity bands on SDS-PAGE that contained 0.01% glycol chitin. The basic chitinases from rice hulls were further purified using chitin affinity chromatography. The chitinase, specific to rice hulls (RHBC), was 88-fold purified with a 1.3% yield. RHBC has an apparent molecular weight of 22.2 kDa on SDS-PAGE. The optimal pH and temperature were 4.0 and $35^{\circ}C$, respectively. With [$^3H$]chitin as a substrate, RHBC has $V_{max}$ of 13.51 mg/mg protein/hr and $K_m$ of 1.36 mg/ml. This enzyme was an endochitinase devoid of ${\beta}$-1,3-glucanase, lysozyme, and chitosanase activities.

• Journal of Microbiology and Biotechnology
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• 제18권1호
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• pp.59-62
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• 2008

The peptide methionine sulfoxide reductases (Msrs) are enzymes that catalyze the reduction of methionine sulfoxide back to methionine. Because of two enantiomers of methionine sulfoxide (S and R forms), this reduction reaction is carried out by two structurally unrelated classes of enzymes, MsrA (E.C. 1.8.4.11) and MsrB (E.C. 1.8.4.12). Whereas MsrA has been well characterized structurally and functionally, little information on MsrB is available. The recombinant MsrB from Bacillus subtilis has been purified and crystallized by the hanging-drop vapor-diffusion method, and the functional and structural features of MsrB have been elucidated. The crystals belong to the trigonal space group P3, with unit-cell parameters a=b=136.096, $c=61.918{\AA}$, and diffracted to $2.5{\AA}$ resolution using a synchrotron-radiation source at Pohang Light Source. The asymmetric unit contains six subunits of MsrB with a crystal volume per protein mass $(V_M)\;of\;3.37{\AA}^3\;Da^{-1}$ and a solvent content of 63.5%.

• 한국전기전자재료학회논문지
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• 제22권9호
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• pp.776-780
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• 2009

In this study, the opto-electric properties of EL devices with PMN dielectric layer with variation of firing tempereature were investigated. For the PMN dielectric layer process, the paste was prepared by optimization of quantitative mixing of PMN powder, $BaTiO_3$, Glass Frit, $\alpha$-Terpineol and ethyl cellulose. The EL device stack consists of Alumina substrate ($Al_2O_3$), metallic electrode (Au), insulating layer (manufactured PMN paste), phosphor layer (ELPP- 030, ELK) and transparent electrode (ITO), which is well structure as a thick film EL device. The phase transformation properties of PMN dielectric with various firing temperatures of $150^{\circ}C$ to $850^{\circ}C$ was characterized by XRD. Also the opto-electric properties of EL devices with different firing temperature were investigated by LCR meter and spectrometer. We found the best opto-electric property was obtained at the condition of $550^{\circ}C$ firing which is 3432.96 $cd/m^2$ at 1948.3 pF Capacitance, 40 kHz Frequency, 40% Duty, Vth+330 V voltage.

• Journal of Microbiology and Biotechnology
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• 제26권6호
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• pp.1087-1097
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• 2016

An intracellular lipase from Anoxybacillus flavithermus HBB 134 was purified to 7.4-fold. The molecular mass of the enzyme was found to be about 64 kDa. The maximum activity of the enzyme was at pH 9.0 and 50℃. The enzyme was stable between pH 6.0 and 11.0 at 25℃, 40℃, and 50℃ for 24 h. The K_m and V_max of the enzyme for pNPL substrate were determined as 0.084 mM and 500 U/mg, respectively. Glycerol, sorbitol, and mannitol enhanced the enzyme thermostability. The enzyme was found to be highly stable against acetone, ethyl acetate, and diethyl ether. The presence of PMSF, NBS, DTT and β-mercaptoethanol inhibited the enzyme activity. Hg²⁺, Fe³⁺, Pb²⁺, Al³⁺, and Zn²⁺ strongly inhibited the enzyme whereas Li⁺, Na⁺, K⁺, and NH₄⁺ slightly activated it. At least 60% of the enzyme activity and stability were retained against sodium deoxycholate, sodium taurocholate, n-octyl-β-D-glucopyranoside, and CHAPS. The presence of 1% Triton X-100 caused about 34% increase in the enzyme activity. The enzyme is thought to be a true lipase since it has preferred the long-chain triacylglycerols. The lipase of HBB 134 cleaved triolein at the 1- or 3-position.

• 반도체디스플레이기술학회지
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• 제9권3호
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• pp.41-45
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• 2010

The ZnO thin films doped with Ga(GZO) and both Ga and Ge(GZO:Ge) were deposited on glass substrate by using RF sputtering system respectively. Structural, morphological and optical properties of the films deposited in the same condition were investigated. Structural properties of the films were investigated by Field Emission Scanning Electron Microscopy, FE-SEM images and X-ray diffraction, XRD analysis. These studies showed shape of films' surface and direction of film growth respectively. It's showed that all films were deposited by vertical orientation strongly. It can be confirmed that all dopants of targets were included in deposited films by results of EDX analysis. UV-Vis spectrometer results showed that all samples had highly transparent characteristics in visible region and have similar 3.28~3.31 eV band gap. It was found that existence of all dopants by EDX analysis. Morphology and roughness of surface of each film were clearly shown by Atomic Force Microscopy, AFM images. It was found in this research that film doped with Ge more dense and stable with hardly any difference in gap energy compared to ZnO films.

• Journal of Applied Biological Chemistry
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• 제44권3호
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• pp.113-118
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• 2001

Xylose (glucose) isomerase was purified to homogeneity from cell-extracts of Streptomyces chibaensis J-59 via ammonium sulfate precipitation followed by chromatography on DEAE-cellulose, and gel filtration on Sephacryl S-300. The purified enzyme is a homotetramer with a native molecular mass of 180 kDa and a subunit molecular mass of 44 kDa. The amino acid N-terminal sequence of glucose isomerase from S. chibaensis J-59 was determined to be Ser-Tyr-Gln-Pro-Thr-Pro-Glu-Asp-Arg-Phe-Thr-Phe-Gly-Leu. The first 14 amino acids of the N-terminal sequence of the enzyme showed strong analogies with N-terminal sequences of glucose isomerase produced by other Streptomyces spp. The optimum pH and temperature for activity were 7.5 and 85, respectively. The purified enzyme required $Mg^{2+}$, $Co^{2+}$, and $Mn^{2+}$ for the activity, $Mg^{2+}$ being the most effective. The enzyme was not inhibited by $Ca^{2+}$, but was inhibited by $Hg^{2+}$, $Ag^+$, and $Cu^{2+}$. The $K_m$, $V_{max}$, and $k_{cat}$ values of S. chibaensis J-59 isomerase for glucose were 83 mM, 40.9 U/mg, and $1,843min^{-1}$, respectively. In the presence of $Co^{2+}$, cell-free enzymes retained 100% without loss of activities by the heat-treatment at $70^{\circ}C$ for 7 days. The enzyme retained 50% residual activity after heating at $85^{\circ}C$ for 13.5 h, at $90^{\circ}C$ for 126 min. The enzyme is more thermostable than any other glucose isomerases of Streptomyces spp.