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유전체 배리어 방전 플라즈마를 이용한 애시드레드 27 수용액의 색도 제거
조진오,김병남,목영선 제주대학교 공과대학 첨단기술연구소 2006 尖端技術硏究所論文集 Vol.17 No.2
The physicochemical processes of dielectric barrier discharge (DBD) such as in-situ formation of chemically active species and emission of UV light were utilized for the decolorization of an aqueous solution formed with distilled water and an azo dye Acid Red 27. The DBD reactor consisted of two coaxial dielectric tubes with different diameters. Aqueous electrolyte solution was filled in the inner tube, which acted as the discharging electrode. The DBD reactor was submerged in the Acid Red 27 solution that was grounded. In this case, the Acid Red 27 solution acted not only as the counter electrode but also as the cooling medium of the DBD reactor. The DBD reactor with the aqueous discharging electrode was found to be more energy-efficient for the generation of ozone than that with typical metal electrode. The chemically active species (mostly ozone) produced in the DBD reactor were well dispersed in the Acid Red 27 solution using a porous gas diffuser, thereby increasing the gas-liquid contact area available for the decolorization. The results have clearly shown that the DBD reactor system was very effective for decolorizing the Acid Red 27 solution. For the purpose of improving the performance of the DBD reactor system, MnO_(2) catalyst was added to the Acid Red 27 solution. It was found that the catalyst significantly enhanced the decolorization.
Highly stable trypsin-aggregate coatings on polymer nanofibers for repeated protein digestion
Kim, Byoung Chan,Lopez-Ferrer, Daniel,Lee, Sang-Mok,Ahn, Hye-Kyung,Nair, Sujith,Kim, Seong H.,Kim, Beom Soo,Petritis, Konstantinos,Camp, David G.,Grate, Jay W.,Smith, Richard D.,Koo, Yoon-Mo,Gu, Man B WILEY-VCH Verlag 2009 Proteomics Vol.9 No.7
<P>A stable and robust trypsin-based biocatalytic system was developed and demonstrated for proteomic applications. The system utilizes polymer nanofibers coated with trypsin aggregates for immobilized protease digestions. After covalently attaching an initial layer of trypsin to the polymer nanofibers, highly concentrated trypsin molecules are crosslinked to the layered trypsin by way of a glutaraldehyde treatment. This process produced a 300-fold increase in trypsin activity compared with a conventional method for covalent trypsin immobilization, and proved to be robust in that it still maintained a high level of activity after a year of repeated recycling. This highly stable form of immobilized trypsin was resistant to autolysis, enabling repeated digestions of BSA over 40 days and successful peptide identification by LC-MS/MS. This active and stable form of immobilized trypsin was successfully employed in the digestion of yeast proteome extract with high reproducibility and within shorter time than conventional protein digestion using solution phase trypsin. Finally, the immobilized trypsin was resistant to proteolysis when exposed to other enzymes (i.e., chymotrypsin), which makes it suitable for use in “real-world” proteomic applications. Overall, the biocatalytic nanofibers with trypsin aggregate coatings proved to be an effective approach for repeated and automated protein digestion in proteomic analyses.</P>
Mok, Young Geun,Lee, Byoung Doo,Kim, Young Jin,Lee, Chang Eun,Kim, Dong Gwan,Lee, Joohyun,Shim, Jaekyung,Meng, Yuling,Rosen, Barry P.,Choi, Jong Soon,Shin, Hyoung Sun,Kim, Seong-Ki,Lee, June Seung,Hwa Elsevier 2008 FEBS letters Vol.582 No.6
<P><B>Abstract</B></P> <P>We cloned a plant gene, <I>Ntcyc07</I>, conferring arsenite tolerance by expressing a tobacco expression library in WT yeast (Y800). Expression of <I>Ntcyc07</I> increased the tolerance to As(III) and decreased its accumulation, suggesting that the enhanced As(III) tolerance resulted from a reduction of the intracellular arsenic level. Interestingly, expression of <I>Ntcyc07</I> increased the expression of the As(III) export carrier <I>ACR3</I>, but repressed that of As(III) uptake channel <I>FPS1</I>. Ntcyc07p interacted with Acr1p, which is the transcriptional activator of <I>ACR3</I>, but not with the <I>ACR3</I> promoter. Taken together, the data indicated that Ntcyc07p promoted As(III) tolerance by decreasing the intracellular level of As(III) via increasing the expression of <I>ACR3</I> and reducing that of <I>FPS1.</I> </P>
Influence of Squid Liver Powder on Accumulation of Cadmium in Serum, Kidney and Liver of Mice
Byoung-Mok Kim,Soo-Young Lee,In-Hak Jeong 한국식품영양과학회 2013 Preventive Nutrition and Food Science Vol.18 No.1
In this study, the effect of squid liver powder intake on accumulation of cadmium in mice was investigated. Subjects were divided into 4 groups including the control group (CON), squid liver powder group with lipids not removed (SLP100), and squid liver powder groups with lipids removed (LFSLP50 and LFSLP100). Feed intake and food efficiency ratio of squid liver powder groups was significantly higher than the CON. As a result of investigating cadmium content in hair, serum, liver, and kidney during intake of squid liver powder, all groups showed increase in cadmium accumulation through consistent, long-term intake. Especially, cadmium content in liver and kidney of LFSLP100 was significantly higher than the content of SLP100 and CON. As a result of pathological observation on liver and kidney tissues according to squid liver powder diet, LFSLP100 showed most serious pathological symptoms. In case of kidney tissues, degeneration was significantly more severe in LFSLP100 compared to other groups. Such results suggest that cadmium concentration in human body can be increased by ingestion of whole squid including internal organs and that tissues can be damaged by increased cadmium concentration. More specific and systematic studies are deemed necessary.
Influence of Squid Liver Powder on Accumulation of Cadmium in Serum, Kidney and Liver of Mice
Kim, Byoung-Mok,Lee, Soo-Young,Jeong, In-Hak The Korean Society of Food Science and Nutrition 2013 Preventive Nutrition and Food Science Vol.18 No.1
In this study, the effect of squid liver powder intake on accumulation of cadmium in mice was investigated. Subjects were divided into 4 groups including the control group (CON), squid liver powder group with lipids not removed (SLP100), and squid liver powder groups with lipids removed (LFSLP50 and LFSLP100). Feed intake and food efficiency ratio of squid liver powder groups was significantly higher than the CON. As a result of investigating cadmium content in hair, serum, liver, and kidney during intake of squid liver powder, all groups showed increase in cadmium accumulation through consistent, long-term intake. Especially, cadmium content in liver and kidney of LFSLP100 was significantly higher than the content of SLP100 and CON. As a result of pathological observation on liver and kidney tissues according to squid liver powder diet, LFSLP100 showed most serious pathological symptoms. In case of kidney tissues, degeneration was significantly more severe in LFSLP100 compared to other groups. Such results suggest that cadmium concentration in human body can be increased by ingestion of whole squid including internal organs and that tissues can be damaged by increased cadmium concentration. More specific and systematic studies are deemed necessary.