• Title/Summary/Keyword: $pH_u$

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Effect of Salicylic and Picolinic Acids Acids on the Adsorption of U(VI) onto Oxides (산화물 표면의 U(VI) 흡착에 미치는 살리실산과 피콜린산의 영향)

  • Park, Kyoung-Kyun;Jung, Euo-Chang;Cho, Hye-Ryun;Song, Kyu-Seok
    • Journal of Nuclear Fuel Cycle and Waste Technology(JNFCWT)
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    • v.7 no.4
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    • pp.219-227
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    • 2009
  • The effect of organic acids on the adsorption of U(VI) onto oxide surfaces ($TiO_2)$(anatase), $SiO_2$(amorphous) and $Al_2O_3$(amorphous)) has been investigated. Two different organic acids, salicylic and picolinic acids, were used. Changes of adsorption ratio of U(VI), which depend on the existence of organic acids in a sample, were measured as a function of pH. Quantities of adsorbed organic acids, which depend on the existence of U(VI) in a sample, were also measured as a function of pH. It is confirmed that the soluble complex formation of U(VI) with organic acids can deteriorate the adsorption of U(VI) onto $TiO_2$ surface. It is noteworthy that salicylic acid does not affect the adsorption of U(VI) onto $SiO_2$ surface, however, picolinic acid enhances the adsorption of U(VI) onto $SiO_2$ surface. The latter effect can be understood by considering the formation of a ternary surface complex on $SiO_2$ surface, which was confirmed by the co-adsorption of picolinic acid with U(VI) and the change in a fluorescence spectra of U(VI) on surface, In the case of $Al_2O_3$, organic acids themselves were largely adsorbed onto a surface without deteriorating the adsorption of U(VI). This would support the possibility of a ternary surface complex formation on the $Al_2O_3$ surface, and an additional spectroscopic study is required.

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Characterization of Cellulase from Bacillus subtilis NSC Isolated from Soil (토양으로부터 단리한 Bacillus subtilis NSC 유래 Cellulase의 특성 규명)

  • Kim, Sang Jin;Park, Chang-Su
    • Journal of Chitin and Chitosan
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    • v.23 no.4
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    • pp.228-233
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    • 2018
  • We isolated microorganisms from soil, which is sampled at forest, Kyeonbuk, Korea, as cellulolytic microorganisms. The isolated strains were identified by analysis of 16S rRNA gene from the starins. The result, four kinds of Bacillus subtilis, one kind of Bacillus amyloliquefaciens, and one kind of Bacillus cereus were identified. Among these strains, Bacillus subtilis was selected due to its high cellulase activity and this strain was named as Bacillus subtilis CNS. The optimum pH and temperature of the cellulase from Bacillus subtilis CNS was pH 5.0 and $40^{\circ}C$, respectively. In the investigation of pH and temperature stability, the cellulase from Bacillus subtilis NSC stabled pH 4.0~6.0 range and until $40^{\circ}C$ for 30 min perfectly. In the enzyme activity for various cellulosic substrate, cellulase from Bacillus subtilis CNS showed the highest activity for CM-cellulose. And, the enzyme activities for alkali swollen cellulose, Alpha-cellulose, Sigmacell-cellulose, and Avicel were approximately 31%, 8%, 8% and 4% of activity for CM-cellulose, respectively. In the degradation of CM-cellulose, the 0.26 U/ml and 0.52 U/ml of cellulase showed 0.43 and 0.76 U/ml activity for CM-cellulose after the reaction of 120 min, respectively.

미생물유래 Transglutaminase의 생산을 위한 생물반응기 운전 조건 확립

  • Lee, Hwa-Jeong;Yu, Jae-Su;Jeon, Gye-Taek;Jeong, Yong-Seop
    • 한국생물공학회:학술대회논문집
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    • 2000.04a
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    • pp.239-242
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    • 2000
  • Experimental studies on the effects of impeller to provide the microbial transglutaminase derived from Streptoverticillium mobaraense have been conducted. The optimal production medium was determined by latin-square design, and the effects of aeration and agitation were observed by using different sizes and shapes of impellers for the poduction of transglutaminase. The effects of pH and temperature were also evaluated for the production of transglutaminase in flasks. As a result, pH is more effective than temperature for both enzyme production and growth of the microorganism. The peak enzyme activity for transglutaminase in fermenter was 0.7 U/mL, but this was still well below the avereage enzyme activity, 1,3 U/mL, obtained in flask runs.

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Phylogenetics, Safety and In Vitro Functional Properties of Bacillus Species Isolated from Iru, a Nigerian Fermented Condiment

  • Adewumi, Gbenga Adedeji;Grover, Sunita;Isanbor, Chukwuemeka;Oguntoyinbo, Folarin Anthony
    • Microbiology and Biotechnology Letters
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    • v.47 no.4
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    • pp.498-508
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    • 2019
  • Bacillus species were isolated from iru, a traditional fermented condiment in Nigeria. Polyphasic approach was used to evaluate the phylogenetic relationship and strain sub-type of the isolated species. Additionally, the phylogenetic profiles of the species isolated from iru were compared with those of bacilli isolated from different continents. The phylogenetic diversity analysis was performed using the combination of 16S rRNA gene sequencing, ITS-PCR, ITS-PCR-RFLP, and M13 RAPD-PCR. The analysis revealed that Bacillus subtilis U170B and B. subtilis U146A isolated from iru were the closest relatives of strains belonging to the phylogeny of B. subtilis sensu stricto and were related to other bacilli isolated from different continents that had functional benefits. The two isolated species exhibited resistance to acidic pH (pH 2.0). The survival rates of B. subtilis U170B, B. subtilis U146A, and B. clausii UBBC-07 (commercial probiotic strain) cultured at pH 2.0 for 3 h were 33.45, 12.44, and 9.53%, respectively. The strains were highly tolerant to bile salts [0.3% (w/v)]. B. subtilis U170B exhibited the highest cell viability (43.45%) when cultured for 3 h in the presence of bile salts, followed by B. subtilis U146A (25%) and B. clausii UBBC-07 (18.94%). B. subtilis U170B and B. subtilis U146A did not exhibit haemolytic activity and were susceptible to different antibiotics. Additionally, these two strains exhibited weak antagonistic activity against B. cereus. The diverse wild strains of B. subtilis can be used as a safe multifunctional starter culture for the industrial production of condiments with health benefits.

Gemcitabine-induced Cell Death in Lung Cancer Cells : the Role of p53 (폐암 세포에서 Gemcitabine에 의한 세포 사멸과 p53의 역할)

  • Kim, Doh-Hyung;Bae, Gang-U;Yong, Wha-Shim;Choi, Eun-Kyung;Kim, Youn-Seup;Park, Jae-Seuk;Jee, Young-Koo;Lee, Kye-Young
    • Tuberculosis and Respiratory Diseases
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    • v.53 no.3
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    • pp.275-284
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    • 2002
  • Background : Gemcitabine is a new anti-cancer agent for treating non-small cell lung cancer. Functioning as an antimetabolite, it induces anti-cancer effects by suppressing DNA synthesis after being incorporated into the DNA as a cytosine arabinoside analogue. When Gemcitabine is incorporated into the DNA, the p53 gene may be activated by induction of the DNA defect. However, there are a few studies on the molecular mechanisms of Gemcitabine-induced cell death. This study examined the role of p53 in Gemcitabine-induced cell death. Methods : A549 and NCl-H358 lung cancer cells were used in this study. The cell viability test was done using a MTT assay at Gemcitabine concentrations of 10nM, 100nM, 1uM, 10uM and 100uM. A FACScan analysis with propium iodide staining was used for the cell cycle analysis. Western blot analysis was done to investigate the extent of p53 activation. For the functional knock-out of p53, stable A549-E6 cells and H358-E6 cells were transfected pLXSN-16E6SD which is over expresses the human papilloma virus E6 protein that constantly degrades p53 protein. The functional knock out of p53 was confirmed by Western blot analysis after treatment with a DNA damaging agent, doxorubicine. Results : Gemcitabine exhibited cell toxicity in dose-dependent fashion. The cell cycle analysis resulted in an S phase arrest. Western blot analysis significant p53 activation in time-dependent manner. Gemcitabine-induced cytotoxicity was reduced by 20-30% in the A549-E6 cells and the 30-40% in H358-E6 cells when compared with the A549-neo and H358-neo control cells. Conclusion : Gemcitabine induces an S phase arrest, as expected for the anti-metabolite, and activates the p53 gene, Furthermore, p53 might play an important role in Gemcitabine-induced cell death. Further investigation into the molecular mechanisms on how Gemcitabine activates the p53 gene and its signaling pathway are recommended.

H.P.L. Value in Abnormal Pregnancy by Hemagglutination-Inhibition Reaction (비정상임산부(非正常妊産婦)의 혈청중(血淸中) H.P.L.의 혈구응집조지반응(球凝集阻止反應)에 의한 측정(測定)에 관(關)한 연구(硏究))

  • Kim, Dong-Jin;Shin, Myon-Woo
    • Clinical and Experimental Reproductive Medicine
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    • v.4 no.1
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    • pp.27-32
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    • 1977
  • Serum levels of human placental lactogen were measured by hemagglutination inhibition reaction in 26 normal pregnant state and in patients with 16 toxemia and 6 F.D.I.U. beyond their thirtieth week of gestation to evaluate their clinical usefulness. It was realized that HPL-HAIR Test Kit was easy to use and produced reliable results. The general conclusion were as follows: 1) HPL value was $6{\sim}8$ug/ml in normal pregnancy. 2) The levels in mild toxemia were similar in the normal state. 3) The levels in severe toxemia were similar or slightly lower than in the normal and mild toxemia. 4) The levels in F.D.I.U. were lower than in the normal state.

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Cellulose 분해효소를 분비하는 Trichoderma sp. C-4 균주의 분리 및 특성

  • Son, Young-June;Sul, Ok-Ju;Chung, Dae-Kyun;Han, In-Seob;Choi, Yun-Jae;Jeong, Choon-Soo
    • Microbiology and Biotechnology Letters
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    • v.25 no.4
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    • pp.346-353
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    • 1997
  • During the screening of cellulase producing microorganisms, a fungal strain C-4 was selected from etiolated leaves. Based on taxonomic studies, the fungus could be classified as a strain of Trichoderma sp. When the strain C-4 was cultured in Mandels' media at 28$circ$C for 6 days, the enzyme activities detected in broth were as follows: 8.2 U/ml (28.1 U/mg) of CMCase activity, 0.75 U/ml (2.58 U/mg) of Avicelase activity, 1.67 U/ ml (5.68 U/mg) of $eta$-glucosidase activity. The optimum pH for enzyme induction was 6.2. The crude enzyme retained 100% of its original CMCase activity at 50$circ$C for 1 hr (pH 5.0), and at 4$circ$C for 24 hrs (pH 5.0). There was no effect on the CMCase activity in the presence of 1 mM of CsCl, LiCl, MgCl$_{2}$, and FeCl$_{2}$, respectively. When the crude enzyme was treated with trypsin and chymotrypsin (2% W/w) for 10 minutes, the remaining CMCase activity was 70%, but there was no further loss of activity for 60 minutes treatment at 30$circ$C. The crude enzyme showed the synergism with rumen fluid for the hydrolysis of Avicel and CMC by 118% and 130%, respectively.

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Optimization for the DXAMase production from Lipomyces starkeyi using statistically designed experiments

  • Park, Jun-Seong;Gang, Hui-Gyeong;Gang, Seong-Ju;Kim, Byeong-Hun;Park, Don-Hui;Kim, Do-Man
    • 한국생물공학회:학술대회논문집
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    • 2002.04a
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    • pp.211-214
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    • 2002
  • The optimal condition for the production of DXAMase, containing the both characteristics of dextranase and amylase, was studied based on different levels of pH, temperature, and aeration rate. Response surface methodology was applied to find the optimatic condition showing the relationship between the fermentation response(dextranase and amylase activity of DXAMase) and the fermentation variables(pH, temperature, and agitation rate). In case of dextranase activity, the condition of pH 4.06, $28.08^{\circ}C$, and 235.14 rpm showed the highest activity, 2.26 U/ml, and for amylase activity, the condition of pH 4.01, $27.96^{\circ}C$, and 212.01 rpm showed the highest activity, 3.52 U/ml. For the production of DXAMase, dextranase and amylase, the optimum condition was pH 4.06, $28.08^{\circ}C$, and 234.80 rpm.

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Plant responses to nano and micro structured carbon allotropes: Water imbibition by maize seeds upon exposure to multiwalled carbon nanotubes and activated carbon

  • Dasgupta-Schubert, N.;Tiwari, D.K.;Francis, E. Reyes;Martinez Torres, P.;Villasenor Cendejas, L.M.;Lara Romero, J.;Villasenor Mora, C.
    • Advances in nano research
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    • v.5 no.3
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    • pp.245-251
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    • 2017
  • Multiwalled carbon-nanotubes (MWCNT) and micro-structured carbon, such as biochar or activated carbon (AC), have been seen to significantly increase the growth indices of certain plant species such as maize (Zea mays L.). Seed imbibition is the stage where environmental factors that affect water transport across the seed coat barrier, make a large impact. This work explores the effect on water imbibition by maize seeds when the aqueous environment surrounding the seed is diluted by small concentrations (10 and 20 mg/l) of pristine MWCNT (p-MWCNT), carboxylate functionalized MWCNT (COO-MWCNT) and AC. The degree of sensitivity of the process to (i) large structural changes is seen by utilizing the nano (the MWCNT) and the micro (the AC) allotropic forms of carbon; (ii) to small changes in the purity and morphology of the p-MWCNT by utilizing 95% pure and 99% pure p-MWCNTs of slightly differing morphologies; and (iii) to MWCNT functionalization by using highly pure (97%) COO-MWCNT. Water imbibition was monitored over a 15 hour period by Near Infrared Thermography (NIRT) and also by seed weighing. Seed surface topography was seen by SEM imaging. Analysis of the NIRT images suggests rapid seed surface topological changes with the quantity of water imbibed. While further work is necessary to arrive at a conclusive answer, this work shows that the imbibition phase of the maize seed is sensitive to the presence of MWCNT even to small differences in the purity of the p-MWCNT and to small differences in the physicochemical properties of the medium caused by the hydrophilic COO-MWCNT.

Production and Characterization of New Structured-oligosaccharides from Mixed-enzyme of Dextransucrase and ${\alpha}$-amylase (Dextrnasucrase와 ${\alpha}$-amylase의 혼합효소를 이용한 새로운 구조의 올리고당 생산 및 특성 연구)

  • Lee, In-Su;Kim, Do-Man;Chang, Pahn-Shick
    • KSBB Journal
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    • v.14 no.6
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    • pp.707-712
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    • 1999
  • We have produced new-structured oligosaccharides using mixed-enzyme reactor of dextransucrase from Leuconostoc mesenterides B-512FMCM and ${\alpha}$-amylase. When the concentrations of sucrose and starch were 10%(w/v) and 5%(w/v), respectively, the maximum yield of oligosaccharides with both dextransucrase(100U) and ${\alpha}$-amylase(1000U) was 66.4%. The activity of dextransucrase in mixed-enzyme reactor was increased about 2.5 times by acceptor reaction with starch hydrolyzates. As the activities of dextransucrase:${\alpha}$-amylase were increased from 20U:200U to 500U:5000U, the amount of polymer was increased and the yield of oligosaccharides was decreased. By the addition of sucrose into mixed-enzyme reactor following the prehydrolysis of starch with ${\alpha}$-amylase, the yield was increased up to 12% compared with that of mixed-enzyme reactor without the addition of starch hydrolyzate. New structured-oligosaccharides showed heat resistance up to 140$^{\circ}C$ and was stable in acidic condition at pH 3~6.

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