• Bulletin of the Korean Chemical Society
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• v.31 no.7
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• pp.2047-2050
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• 2010

• Biotechnology and Bioprocess Engineering:BBE
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• v.8 no.4
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• pp.240-245
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• 2003

The use of microfabricated microfluidic devices offers significant advantages over current technologies including fast analysis time and small reagent requirements. In the context of proteomic research, the possibility of using affinity-based separations for prefractionation of samples using microfluidic devices has significant potential. We demonstrate the use of microscale devices to achieve affinity separations of proteins using a device fabricated from borosilicate glass wafers. Photolithography and wet etching are used to pattern individual glass wafers and the wafers are fusion bonded at 650$^{\circ}C$ to obtain enclosed channels. A polymer has been successfully polymerized in situ and used either as a frit for packing beads or, when derivatized with Cibacron Blue 3GA, as a separation matrix. Both of these technologies are based on in situ UV photopolymerization of glycidyl methacrylate (GMA) and trimethylolpropane trimethacrylate (TRIM) in channels.

• Biotechnology and Bioprocess Engineering:BBE
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• v.7 no.1
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• pp.1-5
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• 2002

A fusion protein, consisting of a human epidermal growth factor (hEGF) as the recognition domain and human angiogenin as the toxin domain, can be used as a targeted therapeutic against breast cancer cells among others. The fusion protein was expressed as inclusion body in recombinant E. coli, and when the conventional, solution-phase refolding process was used the refolding yield was very low due to severe aggregation. It was probably because of the opposite electric charge at a neutral pH resulting from the vastly different pI values of each domain. The solid-phase refolding process that exploited the ionic interactions between ionic exchanger surface and the fusion protein was tried, but the adsorption yield was also very low, below $ 30\%$, regardless of the resins and pH conditions used. Therefore, to provide a higher ionic affinity toward the solid matrix, six lysine residues were tagged to the N-terminus of the hEGF domain. When heparin-Sepharose was used as the matrix, the adsorption capacity increased 2.5-3 times to about $88\%$. Besides the intrinsic affinity of angiogenin to heparin, the poly-lysine tag provided additional ionic affinity. And the subsequent refolding yield increased nearly 13-fold, from ca. $4.8\%$ in the conventional refolding of the untagged fusion protein to $63.6\%$. The process was highly reproducible. The refolded protein in the column eluate retained RNase bioactivity of angiogenin.

• Elastomers and Composites
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• v.55 no.3
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• pp.167-175
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• 2020

Various studies have been conducted to improve silica dispersion of silica filled tire tread compounds; among them, silica wet masterbatch (WMB) technology is known to be suitable for manufacturing silica filled compounds that have high silica content and high dispersibility. Till now, the WMB study is focused on the natural rubber (NR) or emulsion styrene-butadiene rubber (ESBR) that does not have a silica-affinity functional group, and a study of NR or ESBR having a silica-affinity functional group is still not well known. Unlike the dry masterbatch technology, the WMB technology can solve the problems associated with the high Mooney viscosity when applied to silica-friendly rubber. However, a coagulant suitable for each functional group has not yet been determined. Therefore, in this study, different coagulant applied silica WMB was prepared by applying calcium chloride, sulfuric acid, acetic acid, and propionic acid by using a carboxyl group functionalized reversible addition fragmentation chain transfer ESBR. The evaluation of the WMB compounds revealed that the calcium chloride added WMB compound showed excellent silica dispersion, abrasion resistance, and rolling resistance.

• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.197-203
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• 2001

A fusion protein, consisting of human epidermal growth factor as a recognition domain and human angiogenin as a toxin domain, can be used as a targeted therapeutic against breast cancer cells among others. The fusion protein was expressed as inclusion body in recombinant E. coli, and when the conventional, solution-phase refolding process was used the refolding yield was very low due to severe aggregation, probably due to the opposite surface charge due to vastly different pI values of each domain. Solid-phase refolding process exploiting ionic interactions between the solid matrix and the protein was tried, but the ionic binding yield was very low regardless of the resins and pH conditions used. To provide higher affinity toward the solid matrix, six lysine residues were tagged to the N -terminus of the hEGF domain When the cation exchange resins such as heparin- or CM-Sepharose were used as the matrix, the adsorption capacity increased 2.5-3 times and the subsequent refolding yield increased nearly IS times compared to the conventional process.

• Bulletin of the Korean Chemical Society
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• v.31 no.9
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• pp.2637-2643
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• 2010

In order to develop a new line injection system for spin draw yarn (FD SDY) fibers, the effect of various parameters in extrusion and melt line conditions on the dispersion and distribution of $TiO_2$ particles within FD PET fibers was investigated. As a result, the dispersibility of $TiO_2$ particles in a PET matrix is found to depend on the particle size and its surface characteristics. Surface modification of $TiO_2$ by dimethyl polysiloxane resulted in the improved dispersibility and affinity of $TiO_2$ particles in the PET matrix. Especially, residence time, mixing temperature, and mixing shear rate in the new line injection system under the SDY spinning process were very important parameters to minimize the agglomeration of $TiO_2$ particles. The FD SDY prepared by the new line injection system was superior to those using the polymerization process and the conventional masterbatch chip dosing process in the color-L and color-b values of the fibers.

• KSBB Journal
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• v.21 no.4
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• pp.279-285
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• 2006

We investigated the effects of immobilization chemistry on the yield of immobilization and the bioactivity of the immobilized enzymes. Trypsin as a model protein and macroporous polymer beads(Toyopearl AF 650M, Tosho Co., Japan) was used as a model matrix. Four methods were used to immobilize trypsin; covalent conjugation by reductive amination(at pH 10.0 and pH 4.0) and affinity interaction via streptavidin-biotin, and double-affinity interaction via biotin-streptavidin-biotin system. The covalent conjugation immobilized $3{\sim}4$ mg/ml-gel, ca. 3-fold higher than the affinity method. However, the specific activity of the covalently(pH 10.0) and affinity-immobilized trypsin(via streptavidin-biotin) are ca. 37% and 50%, respectively, of that of the soluble enzyme(on the low-molecular-weight BAPNA substrate). When the molecular size of a substrate increased, the affinity-immobilized trypsin showed higher clavage activity on insulin and BSA. This result seemed to indicate the streptavidin-biotin system allowed more steric flexibility of the immobilized trypsin in its interaction with a substrate molecule. To confirm this, we studied the molecular flexibility of immobilized trypsin using quartz crystal microbalance-dissipation. Self-assembled monolayers were formed on the Q-sensor surface by aminoalkanethiols, and gultaraldehyde was attached to the SAMs. Trypsin was immobilized in two ways: reductive amination(at pH 10.0) and the streptavidin-biotin system. The dissipation shift of the affinity-immobilized trypsin was $0.8{\times}10^{-6}$, whereas that of the covalently attached enzyme was almost zero. This result confirmed that the streptavidin-biotin system allowed higher molecular flexibility. These results suggested that the bioactivity of the immobilized enzyme be strongly dependent on its molecular flexibility.

• KSBB Journal
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• v.17 no.2
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• pp.153-157
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• 2002

A fusion protein, consisting of a human epidermal growth factor as the recognition domain and human angiogenin as the toxin domain, can be used as a targeted therapeutic against breast cancer cells among others. The fusion protein was expressed as an inclusion body in recombinant E. coli, yet when the conventional solution-phase refolding process was used the refolding yield was very low due to severe aggregation, probably because of the opposite surface charge resulting from the vastly different pl values of each domain. Accordingly the solid-phase refolding process, which exploits the ionic interactions between a solid matrix and the protein, was tried, however the ionic binding yield was also very low regardless of the resins and pH conditions used. Therefore, to provide a higher affinity toward the solid matrix, six Iysine residues were tagged to the N-terminus of the hEGF domain. When cation exchange resins, such as heparin- or CM-Sepharose, were used as the matrix, the adsorption capacity increased 2.5~3-fold and the subsequent refolding yield increased nearly 15-fold compared to the conventional process. A similat result was also obtained when an Ni-NTA metal affinity resin was used.

• Applied Chemistry for Engineering
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• v.10 no.6
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• pp.902-906
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• 1999

Electrically conducting composite films were prepared by a vapor phase in situ polymerization of pyrrole in the methyl cellulose film containing a copper(II) perchlorate. Methylcellulose had high affinity to pyrrole and was used as a matrix polymer. Conducting polypyrrole was embedded in the methylcellulose film forming a conducting network and the conductivity of the composite films ranged $10^{-1}$ to $10^{-7}S/cm$. The conductivities of conducting composite films were dependent on the nature of the matrix polymers, concentration of oxidant and polymerization time. In situ polymerization of pyrrole was observed in the matrix polymer and confirmed by UV-vis spectra. From the results of the thermogravimetric analysis, the chemical oxidative polymerization of pyrrole in the matrix polymers did not give any negative effects on the thermal stability of the composite films. Electron micrograph of composites indicated good penetration of PPy in the matrix polymer. DMA suggested a certain degree of incompatibility of the polypyrrole in the composites.

• Bulletin of the Korean Chemical Society
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• v.32 no.2
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• pp.477-482
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• 2011

The structural analysis of polytrimethylene terephthalate (PTT) and characterization of the hydrolytic degradation products after acid hydrolysis were performed using MALDI-TOF mass spectrometry. Mass spectra of the PTT samples were analyzed using a self-calibration method as well as an internal calibration method with standard materials of known masses. PTT structures constituting the samples were determined from the analyses of the spectra, and their relative compositions were estimated. The MALDI-TOF mass spectra of the acid-hydrolyzed PTT sample showed three main series of oligomer products with different end groups in accordance with the hydrolysis schemes. From the spectra of both $Na^+$ and $K^+$ adducts, it was concluded that the PTT samples have higher affinity for $Na^+$ compared with $K^+$ and therefore show higher ionization efficiency with sodium ions when dithranol is used as a matrix. Two different wavelength laser beams ($\lambda$ = 337 nm and 355 nm) were tested and it was observed that the 355 nm beam was more efficient in obtaining the MALDI spectra of PTT using dithranol as a matrix under our experimental conditions.