• Title/Summary/Keyword: 분자선

Search Result 670, Processing Time 0.026 seconds

Treatment of Textile Wastewater by Membrane-Bioreactor Process (막-생물반응조 공정을 이용한 염색폐수의 처리)

  • 강민수;김성수;황규대;강종림
    • Proceedings of the Membrane Society of Korea Conference
    • /
    • 1996.10a
    • /
    • pp.60-61
    • /
    • 1996
  • 염색폐수를 처리하기 위하여, 일반적으로 물리.화학적 공정과 호기성 생물학적 공정을 조합한 방법들을 사용하고 있다. 하지만 호기성 생물학적 공정은 난분해성 물질의 제거능력이 낮고, 염색폐수의 주된 오염원인 염료분자가 호기성 미생물에 대한 에너지원으로 적합하지 않아 분해되기 어려우며, 물리.화학적 공정을 이용한 처리방법으로도 높은 처리효율을 얻을 수가 없다. 이러한 문제점을 극복하기 위하여 염색폐수 처리에 혐기-호기공정을 이용하며, 혐기성 공정에서 생물학적으로 분해되기 어려운 고분자 물질들을 가수분해하여 생물학적으로 분해가능한 저분자물질로 전환시키고, 호기성 공정에서 저분자 물질을 효과적으로 처라할 수 있기때문에 기존의 염색폐수 처리공정에 비하여 훨씬 높은 처리효율을 얻을 수 있다. 특히, 혐기성 미생물은 호기성 미생물에 비하여 난분해성 물질에 대한 분해력이 높고, 생물독성 물질에 대한 내성이 강하기 때문에 수중생물에 유해한 염료를 함유한 염색폐수의 색도제거에 효과적인 것으로 기대된다. 또한, 막분리 공정은 유기물 및 미생물이 막표면에 축적, 증식함으로써 막세공에 막힘현상을 초래하여 역세척 등의 물리적인 방법이나 화학약품을 이용한 화학적 세척 방법으로도 투과플럭스의 회복이 불가능한 상태를 유발함으로 막의 수명을 단축시키는 원인이 된다. 따라서, 혐기-호기공정과 조합하면 색도성분 제거 및 막 오염의 원인이 되는 유기물 및 용존성 고형물을 제거하고, 막 오염의 억제를 통한 후 수염의 연장은 물론, 처리수의 수질향상에 활용될 수 있을 것으로 사료된다.1로 강구와 함께 공구강 vial에 장입 후, Spex mixer/mill을 이용하여 기계적 합금화 하였다. 기계적 합금화 공정으로 제조한 분말에 대한 X-선 회절분석과 시차 열분석으로 합금화 정도를 분석하였다. (Bi1-xSbx)2Te3 및 Bi2(Te1-ySey)3 합금분말을 10-5 torr의 진공중에서 300℃∼550℃의 온도로 30분간 가압소결하였다. 가압소결체의 파단면에서의 미세구조를 주사전자현미경으로 관찰하였으며, 상온에서 가압소결체의 열전특성을 측정하였다. (Bi1-xSbx)2Te3의 기계적 합금화에 요구되는 공정시간은 Sb2Te3 함량에 따라 증가하여 x=0.5 조성에서는 4 시간 45분, x=0.75 조성에서는 5 시간, x=1 조성에서는 6 시간 45분의 vibro 밀링이 요구되었다. n형 Bi2(Te1-ySey)3 합금분말의 제조에 요구되는 밀링시간 역시 Bi2Se3 함량 증가에 따라 증가하였으며 Bi2(Te0.95Se0.05)3 합금분말의 제조에는 2시간, Bi2(Te0.9Se0.1)3 및 Bi2(Te0.85Se0.15)3 합금분말의 형성에는 3시간의 bivro 밀링이 요구되었다. 기계적 합금화로 제조한 p형 (Bi0.2Sb0.8)2Te3 및 n형 Bi2(Te0.9Se0.1)3 가압 소결체는 각기 2.9x10-3/K 및 2.1x10-3/K 의 우수한 성능지수를 나타내었다.ering)가 필수적이다. 그러나 침전법에서 얻게 되는 분말은 매우 미세하여 colloid를 형성하게 되며, 이러한 colloid 상태의 미세한 침전입자가 filte

  • PDF

Structural Analysis and Magnctic Propcrics of Amorphous $Fe_{78}Si_{9}B_{13}$ Alloy (비정질 $Fe_{78}Si_{9}B_{13}$ 합금의 구조와 자성 연구)

  • 이희복;송인명;유성초;임우영
    • Journal of the Korean Magnetics Society
    • /
    • v.3 no.3
    • /
    • pp.179-184
    • /
    • 1993
  • The X-ray diffraction pattern of amorphous $Fe_{78}Si_{9}B_{13}$ alloy was analyzed to obtain the radial distribution function (RDF) where the first peak was in the form of Gaussian function. The calculated coordination number of the form of Gaussian functiono The calculated coordination number of the sample is 13.5, the mean distance betweeon near-neighbor atoms $r_{0}$ is $2.595{\AA}$ and a Gaussian parametet ${\delta}r$ indicating near-neighbor atomic distri-bution is $0.27{\AA}$. The temperature dependence of saturated magnetization at low temperature could be explained by spin wave excitations theory yielding the spin wave stiffness constant as $117.8\;meV\;{\AA}^2$. Also, we tried to fit the observed temperature dependence of saturated magnetization with the Handrich's equation of the modified molecular field theory for the amorphous ferromagnet. Nice fittings are obtained when we used the parameters ${\Delta}=0.32$(S=1/2) and ${\Delta}=0.23$(S=1), respectively. Finally, the calculated spin wave stiffness constant using the parameters and the structural data are $149\;meV\;{\AA}^2$ for S=1/2 and $138\;meV\;{\AA}^2$ for S=1, respectively. The mean exchange coupling integral between near-neighbor atoms was estimated to be 17.9 meV for S=1/2 and 6.7 meV for S=1.

  • PDF

Functionalities of Squid Liver Hydrolysates (오징어 간 가수분해물의 기능성)

  • Lee, Su-Seon;Park, Si-Hyang;Park, Joo-Dong;Konno, Kunihiko;Choi, Yeung Joon
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.41 no.12
    • /
    • pp.1677-1685
    • /
    • 2012
  • The autolysate and hydrolysate of a common squid liver, Todarodes pacificus, were prepared. Autolysis (liver ratio, pH, temperature) and Protamex-treated hydrolysis (pH, temperature, ratio of protease to liver) conditions were optimized by response surface methodology using central composite design for under 1 hr of hydrolysis time. The desirability profile indicated that maximum DH could be achieved at a squid liver of 93.5%, pH 6.4, and $47^{\circ}C$ in autolysis, while that of Protamex-treated hydrolysis did at a Protamex-to-squid liver level of 0.33%, pH 6.0, and $55^{\circ}C$. Three amino acids, proline, cysteine, and methionine, were not detected in the total amino acid composition of the Protamex-treated hydrolysate, while they were detected in the free amino acid composition. Cadmium was $8.32{\pm}0.03$ mg/100 g-powder for raw, $3.56{\pm}0.02$ mg/100 g-powder for the autolysate, and $13.26{\pm}0.04$ mg/100 g powder for the Protamex-treated hydrolysate. The major molecular weight ranged from 1.0 to 1.5 kDa for the autolysate and from 210 to 470 Da for the Protamex-treated hydrolysate. Food functionalities of the autolysate, such as surface hydrolphobicity, emulsion activity index, emulsion stability, water, and fat adsorption, were similar to the Protamex-treated hydrolysate. Both the autolysate and Protamex-hydrolysate showed high inhibitory activities on the angiotensin-I converting enzyme. Cell toxicity against the HepG2 cell line was not detected in the autolysate or the Protamex-treated hydrolysate by 200 ${\mu}g/mL$.

Spectroscopic Identifications and Phase Equilibria of THF + 3-OH THF + CH4 Clathrate Hydrates (삼성분계 THF + 3-OH THF + CH4 크러스레이트 하이드레이트의 상평형 거동 해석 및 분광학적 분석)

  • Kim, Heejoong;Ahn, Yun-Ho;Moon, Seokyoon;Hong, Sujin;Park, Youngjune
    • Korean Chemical Engineering Research
    • /
    • v.55 no.3
    • /
    • pp.353-357
    • /
    • 2017
  • In this study, the inclusion phenomena of tetrahydrofuran + 3-hydroxytetrahydrofuran + $CH_4$ clathrate hydrates were explored via thermodynamic and spectroscopic approaches. The phase equilibria of the double hydrates - THF + $CH_4$ and 3-OH THF + $CH_4$ clathrate hydrates - were determined by pressure-temperature trace during hydrate formation and dissociation, and the result revealed that the equilibrium pressures were shifted to lower pressure region compared to pure $CH_4$ hydrate. The powder X-ray diffraction patterns revealed that the double hydrates of THF + 3-OH THF formed structure II type clathrate hydrates with $CH_4$. The dispersive Raman spectra of the double clathrate hydrates also exhibited that $CH_4$ can be trapped in both $5^{12}6^4$ and $5^{12}$ cages whereas THF and 3-OH THF were encaged in $5^{12}6^4$ cage.

Comparative Study on the Adsorptive Loss of Reduced Sulfur Compounds (RSC) by the Selection of Tubing Materials (튜빙의 종류에 따른 환원황화합물들의 흡착손실 비교 연구)

  • Kim Ki-Hyun;Ahn Ji-Won;Choi Ye-Jin
    • Journal of the Korean earth science society
    • /
    • v.26 no.7
    • /
    • pp.668-673
    • /
    • 2005
  • To collect or transfer samples of gaseous pollutants, various types of tubing are used. Hence, to analyze the uncertainties associated with the use of tubings, a series of comparative test were designed and conducted using the RSC standards with different concentration ranges. For the purpose of this study, we prepared tubings made of six different types of material which include: [1] silco-steel (S1), [2] stainless steel (S2), [3] silicone (S3), [4] PTFE Teflon (T1), [5] tygon (T2), and [6] brass (B). The patterns of RSC loss on to tubing walls, when compared on the basis of the least reactive material S1, exhibited that the extent of RSC loss varied dynamically. It was found that Teflon is highly stable. However, other materials tend to exhibit contrasting patterns of loss. S2 and B show significant loss of light RSC $(H_2S\;and\;CH_3SH)$, while S3 and T2 experience notable loss of heavy RSC (DMS and DMDS).

Structural and Functional Analysis of Nitrogenase Fe Protein with MgADP bound and Amino Acid Substitutions (MgADP 결합 및 아미노산 치환 Nitrogenase Fe 단백질의 구조 및 기능 분석)

  • Jeong, Mi-Suk;Jang, Se-Bok
    • Journal of Life Science
    • /
    • v.14 no.5
    • /
    • pp.752-760
    • /
    • 2004
  • The function of the [4Fe-4S] cluster containing iron (Fe-) protein in nitrogenase catalysis is to serve as the nucleotide-dependent electron donor to the MoFe protein which contains the sites for substrate binding and reduction. The ability of the Fe protein to function in this manner is dependent on its ability to adopt the appropriate conformation for productive interaction with the MoFe protein and on its ability to change redox potentials to provide the driving force required for electron transfer. The MgADP-bound (or off) conformational state of the nitrogenase Fe protein structure described reveals mechanisms for long-range communication from the nucleotide-binding sites to control affinity of association with the MoFe protein component. Two pathways, termed switches I and II, appear to be integral to this nucleotide signal transduction mechanism. In addition, the structure of the MgADP bound Fe protein provides the basis for the changes in the biophysical properties of the [4Fe-4S] observed when Fe protein binds nucleotides. The structures of the nitrogenase Fe protein with defined amino acid substitutions in the nucleotide dependent signal transduction pathways of the Switch I and Switch II have been determined by X-ray diffraction methods. These two pathways have been also implicated by site directed mutagenesis studies, structural analysis and analogies to other proteins that utilize similar nucleotide dependent signal transduction pathways. We have examined the validity of the assignment of these pathways in linking the signals generated by MgATP binding and hydrolysis to macromolecular complex formation and intermolecular electron transfer. The results provide a structural basis for the observed biophysical and biochemical properties of the Fe protein variants and interactions within the nitrogenase Fe protein-MoFe protein complex.

The Crystal Structure of a Bromine Sorption Complex of Dehydrated Fully $Ca^{2+}$-Exchanged zeolite A (칼슘이온으로 완전히 치환한 제올라이트 A를 탈수한 후 브롬을 흡착한 결정구조)

  • Jang, Se-Bok;Han, Young-Wook;Moon, Sung-Doo;Kim, Yang
    • Journal of the Korean Chemical Society
    • /
    • v.35 no.6
    • /
    • pp.630-635
    • /
    • 1991
  • The crystal structure of a bromine sorption complex of dehydrated fully $Ca^{2+}$-exchanged zeolite A (a = 12.211(2) ${\AA}$) has been determined by single-crystal X-ray diffraction techniques in the cubic space group, Pm3m at $21(1)^{\circ}C$. The crystal was prepared by dehydration at $360^{\circ}C$ and 2 ${\times}$ $10^{-6}$ Torr for 2 days, followed by exposure to about 180 Torr of bromine vapor at $24^{\circ}C$ for 30 min. In the resulting structure, six $Ca^{2+}$ ions are located on two different threefold axes associated with 6-ring oxygens. A total of six dibromine molecules are sorbed per unit cell. Each $Br_2$ molecule approaches a framework oxide ion axially, with O-Br = 3.12(7) ${\AA}$, Br-Br = 2.64(9) ${\AA}$ and O-Br-Br = $178(2)^{\circ}$, indicating a charge-transfer interaction. Full-matrix least-squares refinement converged to a conventional R index of 0.104 using the 103 independent reflections for which I > 3${\sigma}$ (I).

  • PDF

Crystal Structure of a Methanol Sorption Complex of Dehydrated Partially Cobalt(Ⅱ)-Exchanged Zeolite A (부분적으로 Co(Ⅱ) 이온으로 치환한 제올라이트 A를 탈수한 후 메탄올을 흡착한 결정구조)

  • Jang, Se Bok;Han, Yeong Uk;Kim, Yang
    • Journal of the Korean Chemical Society
    • /
    • v.38 no.5
    • /
    • pp.339-344
    • /
    • 1994
  • The crystal structure of a methanol sorption complex of dehydrated partially Co(II)-exchanged zeolite A, $Co_4Na_4-A{\cdot}6.5CH_3OH$ (a = 12.169(1) $\AA)$, has been determined by single-crystal X-ray diffraction techniques in the cubic space group Pm$\bar3$m at $21(1)^{\circ}C. $Co_4Na_4$-A was dehydrated at $360^{\circ}C\;and\;2{\times}10^{-6}$ torr for 2 days, followed by exposure to about 104 torr of methanol vapor at $22(1)^{\circ}C$ for 1 hr. The structure was refined to final error indices, $R_1$ = 0.061 and $R_2$ = 0.060 with 147 reflections, for which I > $3\sigma(I).$ In this structure, four $Co^{2+}$ ions and 1.5 $Na^+$ ions per unit cell lie at 6-ring positions: the $Na^+$ ions are recessed 0.44 $\AA$ into the sodalite unit and the Co(II) ions extend ca. 0.55 $\AA$ into the large cavity. 2.5 $Na^+$ ions lie in an 8-oxygen ring plane. The 6.5 methanol molecules are sorbed per unit cell. The 6.5 methanol oxygens, all in the large cavity, associate with the 4 $Co^{2+}$ ions and 2.5 $Na^+$ ions.

  • PDF

Gelatinases of Extracellular Matrix of Human Oocyte-Cumulus Complex (사람 난자-난구 복합체 ECM의 Gelatinase)

  • 이인선;나경아;김해권
    • Development and Reproduction
    • /
    • v.5 no.2
    • /
    • pp.123-129
    • /
    • 2001
  • When mammalian oocytes undergo maturation, cumulus cells surrounding the oocyte exhibit remodeling of their structure known as cumulus expansion. Many molecules including hyaluronic acid participate in this remodeling. The present study aimed to investigate a possible existence of matrix metalloproteinases(MMPs) in the extracellular matrix(ECM) of human oocyte-cumulus complex. ECM was extracted from the human oocyte-cumulus complex. Gelatin gel zymogram of ECM exhibited 7 gelatinases having molecular weight of 300kDa, 240kDa, 200kDa, 180kDa, 116kDa, 97kDa, and 84kDa. This gelatinase profile was very different from that of ovarian mural granulosa cell extract or white blood cell extract, indicating that the oocyte-cumulus complex donating ECM was free from other than cumulus cells. When ethylenediaminetetraacetic acid or 1', 10'-phenanthroline was added to the reaction buffer during zymographic development, almost gelatinase activities were abolished, suggesting that they were MMPs. Following incubation of ECM in the presence of aminophenylmercuric acetate, an activator of proMMPs, 4 gelatinases of 240kDa, 180kDa, 97kDa, and 84kDa disappeared with the concomitant appearance of 80kDa, 65kDa, and 60kDa gelatinases. Based upon these observation, it is suggested that ECM of the human oocyte-cumulus complex consists of gelatinases, presumed to be MMP-2 and MMP-9 isoforms.

  • PDF

Dose-Response of Chitooligosaccharide on Gut Ecology and Lipid Status in Rats (흰쥐에서 키토올리고당의 장 생태와 지질 상태에 미치는 용량에 따른 효과)

  • Kim, Yeon-Rok;Choi, Young-Sun
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.42 no.4
    • /
    • pp.563-569
    • /
    • 2013
  • This study was carried out to investigate the dose-response of chitooligosaccharide (with a molecular weight of 1~3 kDa) on antimicrobial activity and lipid lowering functions in rats. Sprague-Dawley male rats were given experimental diets containing 0 (control), 0.5, 2, or 5% chitooligosaccharide (COS) for 5 weeks. Weight gain and food intake were significantly lower in rats fed 5% COS than control rats and rats fed 0.5 and 2% COS. The numbers of fecal bacteria, including bifidobacteria, lactobacilli, bacteroides, total anaerobes, and total aerobes, which reflect gut microbiota, were significantly decreased in rats fed 5% COS. Plasma triglyceride concentrations significantly decreased in a dose-dependent manner in rats fed 2% or 5% COS, while plasma total cholesterol was not significantly different among groups. The hepatic concentration of triglycerides was lower in rats fed 5% COS, and fecal triglycerides significantly increased in rats fed 5% COS. These results indicate that 5% COS supplementation in a diet may exert antimicrobial activity in vivo, and inhibit the proliferation of typical gut microbes, while lowering lipids.