• Proceedings of the Materials Research Society of Korea Conference
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• 2003.03a
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• pp.51-51
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• 2003

• KSBB Journal
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• v.4 no.2
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• pp.123-127
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• 1989

The separation of trypsin inhibitir using reverse micellar system was invertigated. Among the biffer system tested, 1.0M $CaCl_2$ solution (pH 3.0) and 1.0M NaCl soluation (pH 11.5) were most effective for solubilization and de-solubilization of protein, respectively. When these conditions were applied to two model sampeles, one of which was composed of the same amount of 7S protein and trpsin inhibitor, and the other of which was composed of the same amount of soluble soybean protein isolates and trypsin inhibitor, highly pure trypsin inhibitor was obtained. And in the real soybean, Kwng Gyo, pure trypsin inhibior was also obtained.

• The Transactions of the Korean Institute of Electrical Engineers C
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• v.54 no.8
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• pp.378-383
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• 2005

We report the development of miniature fluorescence detection systems that employ miniature prism, mirrors and low coat CCD camera to detect the fluorescence emitted from 40 fluorescently-labeled protein patterns without scanner. This kind of miniature fluorescence detection system can be used in point of care. We introduce two systems, one uses prism+mirror block and the other uses prism and two mirrors. A large NA microscope eyepiece and low cost CCD camera are used. We fabricated protein chip containing multi-pattern BSA labeled with Cy5, using MEMS technology and modified the surface chemically to clean and to immobilize proteins. The measurements show that the combination of prism and mirrors can homogenize elliptical excitation light over the sample with higher optical efficiency, and increase the separation between excitation and fluorescence light at the CCD to give higher signal intensity and higher signal to noise ratio. The measurements also show that protein concentrations ranging from 10 ng/ml to 1000 ng/ml can be assayed with very small error. We believe that the proposed fluorescence detection system can be refined to build a commercially valuable hand-held or miniature detection device.

• Agricultural and Biosystems Engineering
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• v.6 no.2
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• pp.77-82
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• 2005

The fractionation of green juice could be one of the ways to treat the green juice for saving the bio re-sources by using the basic processes of protein coagulation and separating juice coagulation into protein paste and brown juice and storing the final products. The fractionation of Chinese cabbage juice can be accomplished by applying the combine method of the formic acid with rate of 0.3% and the propionic acid with rate of 0.1 % added 4 hours later in the juice with maximum recovery of protein coagulation. The separation of coagulation into the protein paste and the brown juice completed in 6.5 hours by set up method in a special designed storage. The protein paste could be stored safely for 30days in anaerobic condition.

• KSBB Journal
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• v.13 no.2
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• pp.125-132
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• 1998

Protein affinity membrane was prepared via the coating of chitosan gel on the porous flat polysulfone membrane surface, followed by the immobilization f the reactive dye (Cibacron Blue 3GA) to the chitonsan gel. The maximum protein binding capacity of affinity membrane was about 70${\mu}g/cm^2$ determined by the batch adsorption experiments of human serum albumin (HSA). Using module of this membrane, the characteristics of protein chromatography were investigated through the experiments of elution and frontal chromatography of HSA. This membrane module promises as a chromatography column, since it represented a lower pressure drop and a greater reproducibility. The protein separation ratio was significantly influenced by the flow rate of mobile phase and the injection quantity of HSA. The dynamic protein binding capacity of module decreased from the equilibrium binding capacity with increasing flow rate and approached the value of 15 - 20 ${\mu}g/cm^2$ for flow rates above 6 mL/min.

• Textile Coloration and Finishing
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• v.21 no.6
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• pp.56-63
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• 2009

In this study we have evaluated the separation characteristics and concentration of sericin using tubular type ultrafiltration membrane in silk degumming solution that extracted from electrolytic reduction water process. Ultrafiltration membranes have used in sericin separation performance and the separation characteristics of membrane satisfied typical Hagen-Poiseuille equation. It had the increase of flux according to the increase of feed pressure and temperature in occasion of pure water flux. And also the flux and solute rejection had about $25{\sim}60{\ell}/m^2{\cdot}h$ and more than 95% in sericin feed solution with concentration 1.00~1.89% at feed pressure force of $3{\sim}8kgf/cm^2$ respectively. In addition, the separation performance of tubular type ultrafiltration membrane for silk degumming solution was very steady-state with long experiment time.

• Membrane and Water Treatment
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• v.2 no.2
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• pp.91-103
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• 2011

The flux behavior in the separation of equimolar bovine serum albumin (BSA) and bovine hemoglobin (HB) in aqueous solutions by cross-flow ultrafiltration (UF) was investigated, in which polyacylonitrile membrane with a molecular weight cut-off (MWCO) of 100 kDa was used. BSA and HB have comparable molar mass (67,000 vs. 68,000) but different isoelectric points (4.7 vs. 7.1). The effects of process variables including solution pH (6.5, 7.1, and 7.5), total protein concentration (1.48 and 7.40 ${\mu}M$), transmembrane pressure (69, 207, and 345 kPa), and solution ionic strength (with or without 0.01 M NaCl) on the separation were examined. It was shown that the ionic strength had a negligible effect on separation performance under the conditions studied. Although BSA and HB are not rigid bodies, the flux decline in the present cross-flow UF did not result from the mechanism of cake filtration with compression. In this regard, the specific cake resistance when pseudo steady-state was reached was evaluated and discussed.

• Korean Chemical Engineering Research
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• v.49 no.6
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• pp.840-845
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• 2011

Degradation products of agarose are biologically active and thus used as an ingredient in pharmaceuticals or functional cosmetics. Furthermore, it has been strongly considered as a substrate for bio-ethanol fermentation. Recently, we isolated new agarase-producing microorganism, Pseudoalteromonas sp. from south sea of Korea. In this study, we aimed to separate and purify the agarase from culture broth of this strain. Separation of agarase was performed by ion- exchange chromatography on DEAE-Sepharose resin. Equilibrium pH and volume ratio of resin to the amount of protein were optimized for the efficient adsorption of protein. 410 ${\mu}g$ of protein was completely adsorbed to 3 mL of resin at pH 7.5. The total amount of eluted protein increased as NaCl concentration increased to 400 mM at isocratic elution. Agarase was separated by linear gradient elution of NaCl (0~1,000 mM). Three major protein peaks were observed and the presence or absence of agarase in these eluted proteins was measured by Lugol's staining technique. Only six eluted protein fractions showed strong agarase activity.

• Journal of Microbiology and Biotechnology
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• v.17 no.11
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• pp.1751-1757
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• 2007

Elastin-like polypeptides (ELPs) undergo a reversible inverse phase transition upon a change in temperature. This thermally triggered phase transition allows for a simple and rapid means of purifying a fusion protein. Recovery of ELPs-tagged fusion protein was easily achieved by aggregation, triggered either by raising temperature or by adding salt. In this study, levansucrase has been used as a model enzyme in the development of a simple one-step purification method using ELPs. The levansucrase gene cloned from Pseudomonas aurantiaca S-4380 was tagged with various sizes of ELPs to functionally express and optimize the purification of levansucrase. One of two ELPs, ELP[V-20] or ELP[V-40], was fused at the C-terminus of the levansucrase gene. A levansucrase-ELP fusion protein was expressed in Escherichia coli $DH5{\alpha}$ at $37^{\circ}C$ for 18 h. The molecular masses of levansucrase-ELP[V-20] and levansucrase-ELP[V-40] were determined as 56 kDa and 65 kDa, respectively. The phase transition of levansucrase-ELP[V-20] occurred at $20^{\circ}C$ in 50 mM Tris-Cl (pH 8) buffer with 3 M NaCl added, whereas the phase transition temperature ($T_t$) of levansucrase-ELP[V-40] was $17^{\circ}C$ with 2 M NaCl. Levansucrase was successfully purified using the phase transition characteristics of ELPs, with a recovery yield of higher than 80%, as verified by SDS-PAGE. The specific activity was measured spectrophotometrically to be 173 U/mg and 171 U/mg for levansucrase-ELP[V-20] and levansucrase-ELP[V-40], respectively, implying that the ELP-tagging system provides an efficient one-step separation method for protein purification.

• Korean Journal of Food Science and Technology
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• v.22 no.1
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• pp.56-60
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• 1990

The changes in the partition coefficient of model proteins (lysozyme, myoglobin, conalbumin, bovine serum albumin) in an aqueous two-phase system formed by polyethylene glycol and dextran were examined in order to improve the capacity of counter current distribution for the protein fractionation and concentration. The protein distribution patterns in CCD with 30 tubes varied with the pH of the system, and both theoretical and measured values agreed well. From the mixture of model protein, pure BSA fraction was appeared at the upper-phase of 14th tube having pH 4.5, pure myoglobin at the lower-phase of the 16th be with pH 6.5 and conalbumin at the lower-phase of 4th tube with pH 12. The result indicated the possible use of CCD method for protein fractionation, if the partition coefficient of proteins was manipulated by pH and other means.