• Proceedings of the Korean Society of Precision Engineering Conference
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• 2012.10a
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• pp.865-866
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• 2012

• Proceedings of the Korean Society of Precision Engineering Conference
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• 2012.10a
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• pp.867-868
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• 2012

• Journal of the Korean Society of Manufacturing Process Engineers
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• v.12 no.5
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• pp.16-22
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• 2013

A two-dimensional photonic crystal structure was investigated using a roll-to-roll nanoreplication and physical vapor deposition processes for the inexpensive enhanced fluorescence substrate which is not sensitive to the polarization directions of excitation light source. An 8 inch silicon master having nano dot array with a diameter of 200 nm, a height of 100 nm and a pitch of 400 nm was prepared by KrF laser scanning lithography and reactive ion etching processes. A flexible polymer mold was fabricated by flat type UV replication process and a deposition of 10 nm nickel layer as an anti-adhesion layer. A roll mold was prepared by warping the flexible polymer mold on an aluminum roll base and a roll-to-roll UV replication process was carried out using the roll mold. After the deposition of ~ 100 nm $TiO_2$ layer on the replicated nano dot array, a 2 dimensional photonic crystal structure was realized with a resonance wavelength of 635 nm for both p- and s-polarized light sources.

• Bulletin of the Korean Chemical Society
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• v.27 no.5
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• pp.642-648
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• 2006

Mushroom tyrosinase (MT) structural changes in the presence of $Cu ^{2+}$ and $Ni ^{2+}$ were studied separately. Far-UV CD spectra of the incubated MT with the either of the metal ions indicated reduction of the well-ordered secondary structure of the enzyme. Increasing in the maximum fluorescence emission of anilinonaphthalene-8-sulfonic acid (ANS) was also revealing partial unfolding caused by the conformational changes in the tertiary structure of MT. Thermodynamic studies on the chemical denaturation of MT by dodecyl trimethylammonium bromide (DTAB) showed decrease in the stability of MT in the presence of $Cu ^{2+}$ or $Ni ^{2+}$ using their activation concentrations. Both activities of MT were also assessed in the presence of different concentrations of these ions, separately, with various monophenols and their corresponding diphenols. Kinetic studies revealed that cresolase activity on p-coumaric acid was boosted in the presence of either of the metal ions, but inhibited when phenol, L-tyrosine, or 4-[(4-methylphenyl)azo]-phenol was substrate. Similarly, catecholase activity on caffeic acid was enhanced in the presence of $Cu ^{2+}$ or $Ni ^{2+}$, but inhibited when catechol, L-DOPA, or 4-[(4-methylbenzo)azo]-1,2-benzenediol was substrate. Results of this study suggest that both cations make MT more fragile and less active. However, the effect of the substrate structure on the MT allosteric behavior can not be ignored.

• BMB Reports
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• v.43 no.6
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• pp.419-426
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• 2010

Aeromonas hydrophila is a bacterial pathogen that infects a large number of eukaryotes, including humans. The UDP-galactose 4'-epimerase (GalE) catalyzes interconversion of UDP-galactose to UDP-glucose and plays a key role in lipopolysaccharide biosynthesis. This makes it an important virulence determinant, and therefore a potential drug target. Our earlier studies revealed that unlike other GalEs, GalE of A. hydrophila exists as a monomer. This uniqueness necessitated elucidation of its structure and active site. Chemical modification of the 6xHis-rGalE demonstrated the role of histidine residue in catalysis and that it did not constitute the substrate binding pocket. Loss of the 6xHis-rGalE activity and coenzyme fluorescence with thiol modifying reagents established the role of two distinct vicinal thiols in catalysis. Chemical modification studies revealed arginine to be essential for catalysis. Site-directed mutagenesis indicated Tyr149 and Lys153 to be involved in catalysis. Use of glycerol as a cosolvent enhanced the GalE thermostability significantly.

• Applied Chemistry for Engineering
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• v.23 no.1
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• pp.71-76
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• 2012

Biofouling by marine organisms such as algae and barnacles causes lots of significant problems in marine systems such as a rise of the maintenance-repair cost for the ship and the marine structures. In this work, a fluoropolymer, perfluoropolyether (PFPE), was applied as an anti-biofouling coating material that prevents the adhesion of marine organisms and facilitates the removal of them. Water contact angles of various surfaces were tested to examine the hydrophobicity of the PFPE-modified surface. The PFPE-modified surface showed the water contact angle of $64.5^{\circ}$ which is a remarkable rise from $46.7^{\circ}$ of amine-treated surface. When the substrate was treated with PFPE, the adhesion on the of the barnacle and other marine organisms were repressed around 15% by the enhanced hydrophobicity. In addition, the removal the of the adhered marine organisms were better comparing to that of the surface prepared by PDMS. Surfaces of the substrate treated by PFPE were characterized through physical and chemical methods to analyze the biofouling results. Degree of biomolecular adhesion to the substrate was quantified by the measurement the fluorescence intensity of marine organisms dyed with green fluorescence. PFPE is expected to be applicable not only to anti-biofouling systems but also to medical devices where the prevention of protein adhesion is required.

• Biotechnology and Bioprocess Engineering:BBE
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• v.9 no.2
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• pp.137-142
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• 2004

In this study, a simple procedure is described for patterning biotin on a glass substrate and then selectively immobilizing proteins of interest onto the biotin-patterned surface. Microcontact printing (CP) was used to generate the micropattern of biotin and to demonstrate the selective immobilization of proteins by using enhanced green fluorescent protein (EGFP) as a model protein, of which the C-terminus was fused to a core streptavidin (cSA) gene of Streptomyces avidinii. Confocal fluorescence microscopy was used to visualize the pattern of the immobilized protein (EGFP-cSA), and surface plasmon resonance was used to characterize biological activity of the immobilized EGFP-cSA. The results suggest that this strategy, which consists of a combination of $\mu$CP and cSA-fused proteins. is an effective way for fabricating biologically active substrates that are suitable for a wide variety of applications. one such being the use in protein-protein assays.

• Biotechnology and Bioprocess Engineering:BBE
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• v.11 no.2
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• pp.146-153
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• 2006

A passive microfluidic delivery system using hydrophobic valving and pneumatic control was devised for microfluidic handling on a chip. The microfluidic metering, cutting, transport, and merging of two liquids on the chip were correctly performed. The error range of the accuracy of microfluid metering was below 4% on a 20 nL scale, which showed that microfluid was easily manipulated with the desired volume on a chip. For a study of the feasibility of biochemical reactions on the chip, a single enzymatic reaction, such as ${\beta}-galactosidase$ reaction, was performed. The detection limit of the substrate, i.e. fluorescein $di-{\beta}-galactopyranoside$ (FDG) of the ${\beta}-galactosidase$ (6.7 fM), was about 76 pM. Additionally, multiple biochemical reactions such as in vitro protein synthesis of enhanced green fluorescence protein (EGFP) were successfully demonstrated at the nanoliter scale, which suggests that our microfluidic chip can be applied not only to miniaturization of various biochemical reactions, but also to development of the microfluidic biochemical reaction system requiring a precise nano-scale control.