• Title/Summary/Keyword: Vmax

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Experimental Study on the Soot Formation Behavior of Octane Single Fuel Droplet Under the Constant Volume Combustion Conditions (정적 연소 조건에서 Octane 단일 연료 액적의 매연 생성 거동에 관한 연구)

  • Lim, Young Chan;Suh, Hyun Kyu
    • Transactions of the Korean Society of Mechanical Engineers B
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    • v.41 no.6
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    • pp.389-395
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    • 2017
  • This study was performed to provide the information of the soot formation behavior of octane single fuel droplet under the identical combustion conditions. To achieve this, this experimental study provide the results of the soot formation characteristics of octane droplet in accordance with different initial droplet diameter($d_0$), at the same time, experiment was conducted under the same combustion conditions which are 1.0atm of ambient pressure($P_{amb}$), 21% of oxygen concentration($O_2$) and 79% of nitrogen concentration($N_2$). Visualization of octane droplet combustion was performed by visualization system with high speed camera. The results of maximum soot volume fraction($f_{vmax}$) was almost the same under the equivalent ambient conditions regardless of initial droplet diameter. Furthermore, maximum soot volume fraction was showed the higher value in the measuring direction between $135^{\circ}$ and $315^{\circ}$ since the soot-tail is generated during two opposing igniters movement process.

Influence of Food Dye on the Activity of Hepatic Azo Reductase and the Effect of Flavin (식용 Azo 색소가 Hepatic Azo Reductase에 미치는 영향과 Flavin의 효과)

  • 윤혜정;원형란
    • Journal of Food Hygiene and Safety
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    • v.2 no.1
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    • pp.9-14
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    • 1987
  • With the market of food products, the use of food additives is on the increase. The dye as food additives, can be used for some foods which are difficult to preserve their own colors. It can be also classified as tar dye, vegetable dye and mineral dye. Because tar dye has dense toxicity, only 15 articles among them are legally allowed to be used. Among the allowed articles, the azo compound amaranth, tartrazine, sunset yellow, and allura red, were used in determining and comparing rat hepatic azo reductase activity and we observed the flavin's effects as follows: 1. Investigation with amaranth as substrate gave an apparent Km of $645\;\mu\textrm{M}$ and Vmax of 50 n mol/min/mg protein. 2. On investigation using a fixed amaranth concentration over a range of flavin concentration, FAD significantly increased the activity of the azo reductase compared with only minor increases in reaction mediated by the NADPH-generating system alone. 3. On investigation with amaranth, tartrazine, sunset yellow allura red as electron acceptor in the absence or presence of 300 mM-FAD, sunset yellow was reduced at a rat similar to amaranth, tartrazine was reduced at a slower rate and allura red was reduced a little more rapidly.

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Purification and Properties of an Extracellular Chitinase from Streptomyces sp. (Streptomyces속 균주로 부터 생산되는 Chitinase의 정제 및 그 성질)

  • Hong, Yong-Ki;Seu, Jung-Hwn
    • Microbiology and Biotechnology Letters
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    • v.7 no.3
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    • pp.149-155
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    • 1979
  • Streptomyces sp. 115-5 was selected as the most active microorganism of about 200 strains for the production of chitinase. The enzyme was purified by (NH$_4$)$_2$SO$_4$ treatment, 1st-Sephadex G-100, DEAE-Cellulose, 2nd-Sephadex G-100 column chromatography, and evidence for homogenity was obtained from CM-Sephadex C-50 column chromatography and polyacylamide gel electrophoresis. The purified enzyme hydrolyzed chitin (N-acetyl glucosamine polymer) and chitosan (glucosamine polymer) but not cellulose. And with chitin as the substrate, a Km value of 3.6 mg of chitin per ml and a Vmax of 100 $\mu$mo1e fer hr were found. The activation of the chitinase was 3.66 kcal per mole. The molecular weight of the enzyme was esti-mated about 56,000 daltons by Sephadex G-100 chromatography and isoelectric point as pH 3.0.

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Enzymatic Properties of Cyclodextrin Glycosyltransferase from Alkalophilic Bacillus sp. YC-335 (호알칼리성 Bacillus sp.가 생산하는 Cyclodextrin Glycosyltransferase의 효소적 특성)

  • Jung, Yong-Joon;Jung, Myeong-Ho;Yu, Ju-Hyun
    • Korean Journal of Food Science and Technology
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    • v.23 no.1
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    • pp.93-97
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    • 1991
  • The enzymatic properties of purified CGTase from alkalophilic Bacillus sp. YC-335 have been examined. Apparent Vmax values of the enzyme in transferring glycosyl residues ${\alpha}-,\;{\beta}-and\;{\gamma}-cyclodextrin(CD)$ to sucrose were $16.13,\;21.8\;and\;9.8{\mu}moles/min/mg\;protein$, respectively and Km values of the corresponding CD were 1.68, 0.33 and 0.37 mM, respectively. A number of saccharides, specially starch hydrolyzates such as glucose and maltose, could activate the dextrinizing activity of the enzym. However, the dextrinizing activity was inhibited by ${\beta}-CD$. It was found from Lineweaver-Burk plot that the inhibition of CGTase by ${\beta}-CD$ was noncompetitive. High performance liquid chromatographic analysis showed that the enzyme has three kinds of activity ; transglycosylation and disproportionation as well as cyclization.

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Purification and Properties of Alkaline Pretense from Xanthomonas sp. YL-37 (Xanthomonas sp. YL-37 균주가 생산하는 Alkali성 단백질분해효소의 정제 및 성질)

  • 장형수;권태종
    • Microbiology and Biotechnology Letters
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    • v.26 no.5
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    • pp.427-434
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    • 1998
  • An alkaline protease was 4-fold purified, yielding 2.3% of recovery by ammonium sulfate precipitation, CM-cellulose column chromatography and Sephadex G-100 column chromatography. The purified enzyme was estimated to be monomeric with molecular weight of about 62,000 from polyacrylamide gel eletrophoresis (PAGE) and sodiumdodecylsulfate polyacrylamide gel electrophoresis (SDS-FAGE). The optimal pH and temperature of the alkaline pretense activity were 11.0 and 50$^{\circ}C$, respectively, exhibiting high stability at pH value from 6.0 to 11.0 at 50$^{\circ}C$ for 30 minute. The alkaline pretense was activated by MnSO$_4$, CaCl$_2$, and was inhibited by CuSO$_4$, ZnSO$_4$, HgCl$_2$, EDTA and EGTA. Also, the enzyme was found to be a metaloenzyme requiring Mn$\^$2+/ as cofactor. The NH$_2$-terminal amino acid of alkaline protease was alanine. The Km and Vmax values of this enzyme for casein was 4.0 mg/$m\ell$ and 5,500 unit/$m\ell$, respectively.

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Taurine Transporter Activity in the Human Colon Carcinoma cell Line(HT-29) is Decreased during Cell Differentiation (인체 소장상피세포주(HT-29)의 분화단계에 따른 타우린수송체 활성의 변화)

  • 박태선
    • Journal of Nutrition and Health
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    • v.33 no.6
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    • pp.660-667
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    • 2000
  • Previous studies on the effect of age on intestinal taurine transport in animals have invariably shown a decline in the activity of the transport system with increasing age. In the present study changes in taurine transporter activity were observed during cell differentiation in the human colon carcinoma cell line HT-29 This cell line exhibits various enterocytic characteristics when differentiated and therefore has frequently been used to study the characteristcs and regulation of nutrient and drug absorption in the small intestine at the cellular level. Pre-treatment of the cells with $\beta$-alanine(10mM) reduced the taurine transport activity to 33% of the value for the control cells(p<0.05) which implies that taurine and $\beta$-alanine share a common $\beta$-amino acid transport system for their celluar uptake in the HI-29 was continued until 21 days post seeding. Kinetic studies of the taurine transporter were conducted in the HT-29 cell line with varying taurine concentration(5-60$\mu$M) in the uptake medium Both Vmax and the Michaelis-Menten constant(Km) of taurine transporter were decreased as differentiation of the HT-29 cell line was progressed ; Vmax of the taurine transporter in cells incubated for 4, 14 and 21 days post seeding was 2.79$\pm$3.4m 16.89$\pm$1.74, and 0.85$\pm$0.08 and 0.32$\pm$0.01nmol.mg protein-1 .30min-1 respectively(p<0.001) and Km was 42.3$\pm$3.4, 16.89$\pm$1.74, and 11.2$\pm$3.0$\mu$M respectively (p<0.01) These results indicate that the activity of sodium dependent active taurine transport system in the HT-29 cell line is decreased as confluent cells are differentiated. This phenomenon in cell culture system corresponds well with the earlier observation of lower intestinal taurine transport activity in suckling rats compared to that in adult animals although direct relationship of cell differentiation with in vivo aging process needs further verification.

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Analysis of Catalases from Photosynthetic Bacterium Rhodospirillum rubrum Sl

  • Lim, Hee-Kyung;Kim, Young-Mi;Lee, Dong-Heon;Kahng, Hyung-Yeel;Oh, Duck-Chul
    • Journal of Microbiology
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    • v.39 no.3
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    • pp.168-176
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    • 2001
  • Five different types of catalases from photosynthetic bacterium Rhodospirillum rubrum S1 grown aerobically in the dark were found in this study, and designated Catl (350 kDa), Cat2 (323 kDa), Cat3 (266 kDa), Cat4 (246 kDa), and Cat5 (238 kDa). Analysis of native PAGE revealed that Cat2, Cat3, and Cat4 were also produced in the cells anaerobically grown in the light. It is notable that only Cat2 was expressed much more strongly in response to the anaerobic condition. Enzyme activity staining demonstrated that Cat3 and Cat4 had bifunctional catalase-peroxidase activities, while Catl, Cat2, and Cat5 were typical monofunctional catalases. S1 cells grown aerobically in the presence of malate as the sole source of carbon exhibited an apparent catalase Km value of 10 mM and a Vmax of about 705 U/mg protein at late stationary growth phase. The catalase activity of Sl cells grown in the anaerobic environment exhibited a much lower Vmax of about 109 U/mg protein at late logarithmic growth phase. The catalytic activity was stable in the broad range of temperatures (30$\^{C}$-60$\^{C}$), and pH (6.0-10.0). R. rubrum S1 was much more resistant to H$_2$O$_2$in the stationary growth phase than in the exponential growth phase regardless of growth conditions. Cells of stationary growth phase treated with 15 mM H$_2$O$_2$for 1 h showed 3-fold higher catalase activities than the untreated cells. In addition, L-glutamate induced an 80-fold increase in total catalase activity of R. rubrum S1 compared with magic acid. Through fraction analyses of S1 cells, Cat2, Cat3, Cat4 and Cat5 were found in both cytoplasm and periplasm, while Catl was localized only in the cytoplasm.

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The Effect of Dehydronifedipine on the Oxidation of Aflatoxin $B_1$ by Cytochrome P450 3A4 (Cytochrome P450 3A4에 의한 Aflatoxin $B_1$의 산화에 대한 Dehydronifedipine의 영향)

  • 김복량;권강범;김동현
    • Toxicological Research
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    • v.15 no.1
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    • pp.95-101
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    • 1999
  • Cytochrome P450 (CYP) 3A4 metabolizes aflatoxin B1 (AFB1) to AFB1-exo-8,9-epoxide (8,9-epoxidation) and aflatoxin Q1 (AFQ1; 3$\alpha$-hydroxylation) simultaneously. We investigated whether each metabolite was formed via its own binding site of CAP3A4 active site. Kinetics of the formation of the two metabolites were sigmoidal and consistent with the kinetics of substrate activation. The HIll model predicted that two substrate binding wites are involved in the oxidationof AFB1 by CYP3A4. Dehydronifedipine, a metabolite of nifedipine generated by CYP3A4, inhibited the formation of AFQ1 without any inhibition in the formation of AFB1-exo-8,9-epoxidation. Dehydronifedipine was found to act as a reversible competitive inhibitor against 3$\alpha$-hydroxylation of AFB1. Vmax and S0.5 of the 8,9-epoxidation were not changed in the presence of 0, 50, or 100 $\mu\textrm{M}$ dehydronifedipine. S0.5 of 3$\alpha$-hydroxylation was increased from 58$\pm$4 $\mu\textrm{M}$ to 111$\pm$8 $\mu\textrm{M}$ in the presence of 100 $\mu\textrm{M}$ nifedipine whereas Vmax was not changed. These results suggest that there exist two independent binding sites in the active site of CAP3A4 . One binding site is responsible for AFB1-exo-8,9-epoxidation and the other is involved in 3$\alpha$-hydroxylation of AFB1. Dehydronifedipine might selectively bind to the site which is responsible for the formation of AFQ1 in the active site of CYP3A4.

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Characteristics of Recombinant Alginate Lyase of a Marine Bacterium, Pseudomonas sp. (해양 미생물 Pseudomonas sp.의 유전자 재조합 Alginate Lyase의 특성)

  • KIM Young-Ok;KIM Gu-Taek;KIM Hyun-Kuk;KIM Dae-Kyung;HUH Sung-Hoi;KONG In-Soo
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.29 no.5
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    • pp.637-642
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    • 1996
  • We isolated a marine bacterium, Pseudomonas sp,, which could produce the enzyme of alginate lyase, and cloned the alginate lyase gene in Escherichia coli. The cloned DNA was overexpressed with approximately $50\%$ amount of total proteins. In addition, the expressed proteins were not secreted into the medium, and most of them existed in the cytoplasm by the soluble form, but not observed any inclusion body by TIM. For the optimum enzyme activity, temperature was $20^{\circ}C$, pH was 7.0, and Km and Vmax values of the enzyme were $0.4\%$ and 625 units/mg, respectively.

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The Succession of Microbial Populations and Variation of Enzyme Activities in Composting of Apple Pomace (사과박 퇴비화에서의 미생물군집의 천이와 효소활성도의 변화)

  • Lee, Yong-Ok;Jo, Ik-Hwan;Lee, Yong-Se;Jun, Ha-Joon
    • Journal of the Korea Organic Resources Recycling Association
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    • v.7 no.2
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    • pp.73-82
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    • 1999
  • To verify the usefulness of enzyme activity as a index for the stability or maturity of apple pomace composting. the succession of microbial populations using viable count procedure. and Vmax of ${\beta}$-glucosidase and cellobiohydrolase were measured. based on an increase in fluorescence as the nonfluorescent methylumbelliferyl substrates were enzymatically hydrolyzed, leading to the highly fluorescent methylumbelliferyl molecule 4-methylumbelliferone(MUF). The activities of these enzymes in the decomposition of carbohydrates were gradually decreased in the course of the time. Correlation between microbial population and enzyme activity was not significant with exception of fungi. and the fungi were represented in high density. This indicates that the fungi probably play a major role in composting of apple pomace.

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