• Title/Summary/Keyword: high purification

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A Study on the Purification Chara00cteristics of Bentonite with Dry-Based Process (벤토나이트광의 건식 정제 특성 연구)

  • 정수복;김완태;채영배;임정한
    • Journal of the Mineralogical Society of Korea
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    • v.15 no.4
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    • pp.283-291
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    • 2002
  • Dry-based processes such as crushing, milling, sieving, magnetic and gravity separation were employed in order to investigate the purification characteristics of bentonite. The CECs of Gampo 13 and 35 bentonites were estimated at 88.3 and 93.3 meq/100 g and the samples contained quartz and feldspar as impurity minerals. According to the physical properties of constituent minerals of bentonite, the purification techniques were adopted to enhance the grade of montmorillonite High grade of montmorillonite could be obtained by the combination of each process. Consequently, the recovery of final products of Gampo 13 and 35 bentonite were 68.6 and 49.5%, and the CECs of them were 96.9 and 109.6 meq/100 g, respectively.

The Purification Capacity of Zizania latifolia on Wetlands of Munpyeong Stream

  • Kim, Ha-Song;Ihm, Byung-Sun
    • The Korean Journal of Ecology
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    • v.25 no.1
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    • pp.63-70
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    • 2002
  • This study examined the changes of water quality in relation to distribution of hydrophytes, and the purification capacity of Zizania latifolia to improve the effluent from Munpyeong stream from March 1997 to December 1999. While the concentration of nitrogen and phosphorous in water were increased during the farming season, those decreased, during the streaming down to paddy and drainage areas. In investigated sites, the Z. latifolia was dominant community according to the development of the natural wetlands. Furthermore, it formed a large community owing to its high adaptability to environmental changes in the agriculture lands. In September, the leaves productivity of the Z. latifolia were 4,032g D.W/$m^2$and roots were 7,680gD.W/$m^2$. The purification capacity of the Z. latifolia for NH$_3$-N, $No_3$-N, and PO$_4$-P were 13.41, 17.07, and 4.58 respectively during 5 days. The results suggested that it needs to establish wetlands vegetated by hydrophytes to improve the water quality of the effluent from agricultural lands.

Recombinant Expression, Isotope Labeling, and Purification of Cold shock Protein from Colwellia psychrerythraea for NMR Study

  • Moon, Chang-Hun;Jeong, Ki-Woong;Kim, Hak-Jun;Heo, Yong-Seok;Kim, Yang-Mee
    • Bulletin of the Korean Chemical Society
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    • v.30 no.11
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    • pp.2647-2650
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    • 2009
  • Cold shock proteins (Csps) are a subgroup of the cold-induced proteins on reduction of the growth temperature below the physiological temperature. They preferentially bind to single-stranded nucleic acids to translational regulation via RNA chaperoning. Csp plays important role in cold adaptations for the psychrophilic microorganism. Recently, Cold shock protein from psychrophilic bacteria, Colwellia psychrerythraea (CpCsp) has been identified. Three dimensional structures of a number of Csps from various microorganisms have been solved by NMR spectroscopy or X-ray crystallography, but structures of psychrophilic Csps were not studied yet. Therefore, cloning and purification protocols for further structural study of psychrophilic Csp have been optimized in this study. CpCsp was expressed in E. coli with pET-11a vector system and purified by ion exchange, size exclusion, and reverse phase chromatography. Expression and purification of CpCsp in M9 minimal media was carried out and $^{15}N$-labeled proteins with high purity over 90% was obtained. Further study will be carried out to investigate the tertiary structure and dynamics of CpCsp.

Optimized purification and characterization of expressed hMC4R-TM2

  • Park, Yu-Geun;Song, Jooyoung;Kim, Yongae
    • Journal of the Korean Magnetic Resonance Society
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    • v.16 no.2
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    • pp.147-161
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    • 2012
  • Human melanocortin-4 receptor (hMC4R) among MC-Rs, expressed in the brain, is in charge of the control on energy homeostasis and food intake. The structure and function of human MC4R have been studied to understand their essential function and roles. To investigate the structure and function, it is necessary to prepare sufficient amounts of proteins. However, their expression and purification is demanding and time-consuming due to their innate insoluble and toxic properties. The heterozygous mutations of hMC4R, exchange of Asp 90 to Asn located in second transmembrane, cause severe obesity in human. To obtain purified hMC4R wt-TM2 for structural studies, it was first over-expressed and purified by fast protein liquid chromatography (FPLC) and then solution NMR studies were performed to get high-resolution spectra. In here, we established optimized purification scheme to get more purified target peptide.

Isolation and Purification of Bioactive Materials Using High-Performance Counter-Current Chromatography (HPCCC) (고속역류크로마토그래피 기술을 이용한 생리활성 물질의 분리 및 정제)

  • Jung, Dong-Su;Shin, Hyun-Jae
    • KSBB Journal
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    • v.25 no.3
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    • pp.205-214
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    • 2010
  • Many successive liquid-liquid extractions occur enabling purification of the crude material to occur. In high performance counter-current chromatography (HPCCC), crude material is partitioned between two immiscible layers of solvent phases. The stationary phase (SP) is retained by hydrodynamic force field effect and the mobile phase (MP) is pumped through the column. Purification occurs because of the different solubility of the components in the liquid mobile and stationary phases. There are many key benefits of liquid stationary phases such as high mass and volume injection loadings, total sample recovery, and easy scale-up. Many researchers showed that predictable scale-up from simple test is feasible with knowledge of the stationary phase retention for the planned process scale run. In this review we review the recent advances in HPCCC research and also describe the key applications such as natural products and synthetics (small or large molecules).

The case study on wireless lan design technique for Bansong purification plant using network integrated management system and security switch (네트워크 통합관리시스템과 보안스위치를 이용한 반송정수장 무선랜 구축사례)

  • Park, Eunchul;Choi, Hyunju
    • Journal of Korean Society of Water and Wastewater
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    • v.32 no.4
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    • pp.309-315
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    • 2018
  • Currently, the commercialization of the $5^{th}$ Generation (5G) service is becoming more prevalent in domestic communication network technology. This has reduced communication delay time and enabled large-capacity data transmission and video streaming services in real-time. In order to keep pace with these developments, K-water has introduced a smart process control system in water purification plants to monitor the status of the water purification process. However, since wireless networks are based on the public Long Term Evolution (LTE) network, communication delay time remains high, and high-resolution video services are limited. This is because communication networks still have a closed structure due to expense and security issues. Therefore, with 5G in its current form, it is very difficult to accommodate future services without improving the infrastructure of its communication networks. In recognition of these problems, this study implemented the authentication and management function of wireless networks on a wired network management system in the K-water Bansong water purification plant. The results confirmed that wired Local Area Network (LAN) services give a higher security performance than an expensive commercial wireless LAN system. This was achieved by using an Internet Protocol (IP) address management system of wired networks and the packet filtering function of the Layer2 (L2) switch. This study also confirmed that it is possible to create a wireless LAN service that is 3.7 times faster than the existing LTE communication network.

Isolation, Purification, and Characterization of a Thermostable Xylanase from a Novel Strain, Paenibacillus campinasensis G1-1

  • Zheng, Hongchen;liu, Yihan;Liu, Xiaoguang;Wang, Jianling;Han, Ying;Lu, Fuping
    • Journal of Microbiology and Biotechnology
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    • v.22 no.7
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    • pp.930-938
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    • 2012
  • High levels of xylanase activity (143.98 IU/ml) produced by the newly isolated Paenibacillus campinasensis G1-1 were detected when it was cultivated in a synthetic medium. A thermostable xylanase, designated XynG1-1, from P. campinasensis G1-1 was purified to homogeneity by Octyl-Sepharose hydrophobic-interaction chromatography, Sephadex G75 gel-filter chromatography, and Q-Sepharose ion-exchange chromatography, consecutively. By multistep purification, the specific activity of XynG1-1 was up to 1,865.5 IU/mg with a 9.1-fold purification. The molecular mass of purified XynG1-1 was about 41.3 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Sequence analysis revealed that XynG1-1 containing 377 amino acids encoded by 1,134 bp genomic sequences of P. campinasensis G1-1 shared 96% homology with XylX from Paenibacillus campinasensis BL11 and 77%~78% homology with xylanases from Bacillus sp. YA-335 and Bacillus sp. 41M-1, respectively. The activity of XynG1-1 was stimulated by $Ca^{2+}$, $Ba^{2+}$, DTT, and ${\beta}$-mercaptoethanol, but was inhibited by $Ni^{2+}$, $Fe^{2+}$, $Fe^{3+}$, $Zn^{2+}$, SDS, and EDTA. The purified XynG1-1 displayed a greater affinity for birchwood xylan, with an optimal temperature of $60^{\circ}C$ and an optimal pH of 7.5. The fact that XynG1-1 is cellulose-free, thermostable (stability at high temperature of $70^{\circ}C{\sim}80^{\circ}C$), and active over a wide pH range (pH 5.0~9.0) suggests that the enzyme is potentially valuable for various industrial applications, especially for pulp bleaching pretreatment.

Avantor® ACE® Wide Pore HPLC Columns for the Separation and Purification of Proteins in Biopharmaceuticals (바이오의약품의 단백질 분리 및 정제를 위한 Avantor® ACE® 와이드 포어 HPLC 컬럼 가이드)

  • Matt James;Mark Fever;Tony Edge
    • FOCUS: LIFE SCIENCE
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    • no.1
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    • pp.3.1-3.7
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    • 2024
  • The article discusses the critical role of chromatography in the analysis and purification of proteins in biopharmaceuticals, emphasizing the importance of comprehensive characterization for ensuring their safety and efficacy. It highlights the use of Avantor® ACE® HPLC columns for the separation and purification of proteins, focusing on the analysis of intact proteins using reversed-phase liquid chromatography (RPLC) with fully porous particles. This article also details the application of different mobile phase additives, such as TFA and formic acid, and emphasizes the advantages of using type B ultra-pure silica-based columns for efficiency and peak shape in biomolecule analysis. Additionally, it addresses the challenges of analyzing intact proteins due to slow molecular diffusion and introduces the concept of solid-core (or superficially porous) particles, emphasizing their benefits over traditional porous particles for the analysis of therapeutic proteins. Furthermore, it discusses the development of Avantor® ACE® UltraCore BIO columns, specifically designed for the high-efficiency separation of large biomolecules, such as proteins, and demonstrates their effectiveness in achieving high-resolution separations, even for higher molecular weight proteins like monoclonal antibodies (mAbs). In addition, it underscores the complexity of analyzing and characterizing intact protein biopharmaceuticals, requiring a range of analytical techniques and the use of wide-pore stationary phases, operated at elevated temperatures and with relatively shallow gradients. It highlights the comprehensive range of options offered by Avantor® ACE® wide pore columns, including both fully porous and solid-core particles, bonded with a variety of complementary stationary phase chemistries to optimize selectivity during method development. The use of ultrapure and highly inert base silica is emphasized for enabling the use of lower concentrations of mobile phase modifiers without compromising analyte peak shape, particularly beneficial for LC-MS applications. Then the article concludes by emphasizing the significance of reversed-phase liquid chromatography and its compatibility with mass spectrometry as a valuable tool for the separation and analysis of intact proteins and their closely related variants in biopharmaceuticals.

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Separation and Purification of 2,6-dimethylnaphthalene in the Light Cycle Oil(II) - Separation of Individual Isomers of Dimethylnaphthalene - (접촉분해경유에 함유된 2,6-dimethylnaphthalene의 분리, 정제(II) - Dimethylnaphthalene 이성체 성분간 분리 -)

  • Kim, Su Jin;Kim, Sang Chai;Kawasaki, Junjiro
    • Applied Chemistry for Engineering
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    • v.7 no.5
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    • pp.869-876
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    • 1996
  • Purification of 2,6-dimethylnaphthalene(2,6-DMNA) from the distillate containing a mixture of dimethylnaphthalene(DMNA) isomers of very high concentration was investigated by crystallization-recrystallization combination as a after-treatment for separation and purification of 2,6-DMNA in the light cycle oil(LCO). The separation of individual isomers of DMNA was studied by crystallization with the distillate as a feed. 2,6-DMNA, 2,7-dimethylnaphthalene(2,7-DMNA) and 2,3-dimethylnaphthalene(2,3-DMNA) were concentrated to crystal, and it was fould that separation between a group of 2,6-, 2,7-, 2,3-DMNA isomers and a group of the other DMNA isomers was possible. However, it was not possible to separate 2,6-, 2,7- and 2,3-DMNA from one another. To select the most suitable recrystallization solvent for purification of 2,6-DMNA, several conventional solvents, which have been employed commercially as recrystallization solvents for high purity performance, were tested, through measurement of solubility of 2,6- and 2,7-DMNA. The solvent used were hexane, iso-propyl ether, ethyl acetate and ethanol. From the solubility results for 2,6- and 2,7-DMNA, ethanol seemed to be the most suitable solvent for purification of 2,6-DMNA. Finally, with crystal recovered by crystallization as a feed and ethanol as a solvent, recrystallization experiments were conducted under various conditions. Purification of 2,6-DMNA was easily done with increasing operating temperature and solvent to feed ratio. These results show that the crystallization-recrystallization combination is an effective one for separation of individual isomers of DMNA.

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Increased Yield of High-Purity and Active Tetrameric Recombinant Human EC-SOD by Solid Phase Refolding

  • Ryu, Kang;Kim, Young-Hoon;Kim, Young-Hwa;Lee, Joon-Seok;Jeon, Byeong-Wook;Kim, Tae-Yoon
    • Journal of Microbiology and Biotechnology
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    • v.18 no.10
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    • pp.1648-1654
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    • 2008
  • Superoxide dismutase (SOD) removes damaging reactive oxygen species from the cellular environment by catalyzing the dismutation of two superoxide radicals to hydrogen peroxide and oxygen. Extracellular superoxide dismutase (EC-SOD) is a tetramer and is present in the extracellular space and to a lesser extent in the extracellular fluids. Increasing therapeutic applications for recombinant human extracellular superoxide dismutase (rEC-SOD) has broadened interest in optimizing methods for its purification, with a native conformation of tetramer. We describe a solid phase refolding procedure that combines immobilized metal affinity chromatography (IMAC) and gel filtration chromatography in the purification of rEC-SOD from Escherichia coli. The purified rEC-SOD tetramer from the $Ni^{2+}$-column chromatography is refolded in Tris buffer. This method yields greater than 90% of the tetramer form. Greater than 99% purity is achieved with further purification over a Superose 12PC 3.2/30 column to obtain the tetramer and specific activities as determined via DCFHDA assay. The improved yield of rEC-SOD in a simple chromatographic purification procedure promises to enhance the development and therapeutic application of this biologically potent molecule.