• Proceedings of the Korea Crystallographic Association Conference
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• 2002.11a
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• pp.49-49
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• 2002

A strategy for the synthesis of more stable and large periodic mesoporous organo-silica materials has been developed for the 2D hexagonal mesoporous organosilica by the core-shell approach using nonionic PEO-PLGA-PEO triblock copolymer templates. The BET surface area of the solvent-extracted hexagonal mesoporous organosilica is estimated to be 1,016 ㎡/g and the pore volume, pore diameter, and wall thickness are 1.447 ㎤/g, 65 Å, and 43 Å, respectively. More hydrophobic PLGA block than the PPO block used for templates of mesoporous silica proves to be quite effective in confining the organosilicates within the PEO phase. Reaction temperature and acid concentration of an initial solution as well as the chemical nature of the bloc k copolymer templates also demonstrate to be important experimental parameters for ordered organosilica mesophase. Moreover, the mesoporous organosilicas prepared with the PEO-PLGA-PEO block templates maintain their structural integrity for up to 25 days in boiling water at 100℃. The mesoporous materials with large pores and high hydrothermal stability prepared in this study has a potential for many applications.

• Archives of Pharmacal Research
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• v.20 no.2
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• pp.115-121
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• 1997

Ile-269 in horse liver alcohol dehydrogenase isoenzyme S(HLADH-S) was mutated to serine by phosphorothioate-based site-directed mutagenesis in order to study the role of the residue in coenzyme binding. The specific activity of the mutant(1269S) enzyme to ethanol was increased 49-fold. All turnover numbers of 1269S enzyme toward 9 primary alcohols were increased. The mutant enzyme showed 3.6, 4.6, 11.6-fold higher catalytic efficiency for $5{\beta}$-androstane-3, 17-dione, $5{\beta}$-cholanic acid-3-one and retinal than wild-type, respectively. The reaction mechanism of 1269S enzyme was ordered bi bi as wild-type's. These results indicate that the hydrophobic interaction of Ile-269 residue with coenzyme plays an important role in dissociation of coenzyme from enzyme-coenzyme complex, which has been known as the rate limiting step of ADH reaction.

• Proceedings of the Korean Society Of Semiconductor Equipment Technology
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• 2002.11a
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• pp.123-126
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• 2002

For the mold die sticking mechanism, the major explanation is that EMC filler of silica wears die surface roughened, which results in increase of adhesion strength. As big differences in experimental results from semiconductor manufacturers are dependent on EMC models, however, chemisorptions or acid-base interaction is apt to be also functioning as major mechanisms. In this investigation, the plasma source ion implantation (PSII) using $O_2$, $N_2$, and $CF_4$ modifies sample surface to form a new dense layer and improve surface hardness, and change metal surface condition from hydrophilic to hydrophobic and vice versa. Through surface energy quantification by measuring contact angle and surface ion coupling state analysis by Auger, major governing mechanism for sticking issue was figured out to be a complex of mechanical and chemical factors.

• Archives of Pharmacal Research
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• v.2 no.1
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• pp.35-47
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• 1979

In order to increase the dissolution rate of furosemide(4-choro-N-furfury1-5-sulfamoy1 anthranilic acid_, various ratio coprecipitates with water-soluble polymers, such as polyvinylpyrrolidone and polythylene glycol, of different molecular weight, were prepared and quantitatively studied by comparing their dissolution characteristics of furosemide at powder state and at nondisintegrating disk state containing constant surface area at various temperatures and rotating velocities. The dissolution characteristics of furosemide from pure furosemide disks and 1:2(w/w) furosemide-PVP coprecipitate disks were in accordance with Noyes-Nernst equation and the rate constant of dissolution was proportional to the square root of rotating velocity of the disks. The intrinsic rate of dissoluton at 150 rpm, 37.deg.C was $2.21{\times}10^{-7}$ for the PVP 10, 000 COPRECIPITATE, $1.64{\times}10^{-7}$ for the PVP 40, 000 coprecipitate, and$ 1.44 {\times} 10^{-7}$for the PVP 360, 000 corprecipitate, while the rate was $1.27{\times}10^{-8}M/cm^{2} min$ for pure furosemide, repectively. The activation energy of dissolution was about 17, 000 for furosemide and about 7, 300 cal/mole for the 1:2 furosemide PVP 40, 000 coprecipitate, respectively.

• Proceedings of the Membrane Society of Korea Conference
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• 2004.05a
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• pp.191-194
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• 2004

A novel type of intelligent microcapsule reactor system was prepared. The reactor can recognize pH change in the medea and control reaction rate by itself. For the reactor system, acrylic acid (AA), N-isopropylacrylamide (NIPAM), and glucose oxidase (GOD) were selected as a pH-responsive device, a gating device according and a reaction device, respectively. Poly(NIPAM-co-AA) (P-NIPAM-co-AA) are known to change its hydrophilicity-hydrophobicity due to pH change. They were integrated in a core-shell microcapsule space. GOD was loaded inside the core space and the pores in the outside shell layer were filled with P-NIPAM-co-AA linear grafted chains as pH-responsive gates by plasma graft filling polymerization method. When P-NIPAM-co-AA gates are hydrophilic at high pH value, this microcapsule permits glucose penetration into the core space and GOD reaction proceeds. However, when P-NIPAM-co-AA gates are hydrophobic at low pH value, this microcapsule forbids glucose penetration and GOD reaction will not occur. The accuracy of this concept was examined.

• Korean Journal of Microbiology
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• v.26 no.1
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• pp.52-59
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• 1988

A partially purified preparation of L-galactonolactone oxidase which catalyzes the last step of L-ascorbic acid biosynthesis was obtained from Saccharomyces cerevisiae ATCc 26787. The purification procedures included Triton X-100 treatment, protamine sulfate precipitation, ammonium sulfate precipitation, DEAE-Sepharose CL-6B ion exchange chromatography, Sephadex G-150 gel filtration chromatography, and Phenyl-Sepharose CL-4B hydrophobic interaction chromatography. The optimum temperature for the enzyme activity was about $34^{\circ}C$ and the optimum pH was 6.8-7.0. The substrate specificity was confined to L-aldonolactones, L-galactono-1,4-lactone and L-gulono-1,4-lactone. An apparent Km value of 0.294mM with L-galactono-1,4-lactone as a substrate was found. By comparing the substrate specificities of this enzyme with those of isofunctional enzymes of higher plants and animals, it becomes evident that the enzyme of S. cerevisiae ATCC 26787 is rather similar to the L-gulonolactone oxidase of animals than the galactonolactone dehydrogenase of higher plants.

• Journal of the Microelectronics and Packaging Society
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• v.9 no.4
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• pp.31-34
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• 2002

For the mold die sticking mechanism, the major explanation is that the silica as a filler in EMC (epoxy molding compound) wears die surface to be roughened, which results in increase of adhesion strength. As the sticking behavior, however, showed strong dependency on the EMC models based on the experimental results from different semiconductor manufacturers, chemisorption or acid-base interaction is apt to be also functioning as major mechanisms. In this investigation, the plasma source ion implantation (PSII) using $O_2, N_2$, and $CF_4$ modifies sample surface to form a new dense layer and improve surface hardness, and change metal surface condition from hydrophilic to hydrophobic or vice versa. Through surface energy quantification by measuring contact angle and surface ion coupling state analysis by Auger, major governing mechanism for sticking issue was figured out to be a complex of mechanical and chemical factors.

• Microbiology and Biotechnology Letters
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• v.23 no.3
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• pp.322-328
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• 1995

A thermophilic bacteria showing proteolytic activity against defatted soybean was isolated from soil. It was identified as Bacillus amyloliquefaciens based on its morphological and physiological characteristics. The Bacillus amyloliquefaciens NS 15-4 was cultivated at 50$\circ$C by rotary shaking in a medium containing defatted soybean. An extracellular protease from this strain was purified to homogeneity by ammonium sulfate precipitation, ion exchange, and hydrophobic interaction chromatographies. The molecular weight of the enzyme was estimated to be approximately 30,000 by SDS-PAGE and the N-terminal amino acid sequence of the enzyme was turned out to be AQSVPYGISQIKAPA. The optimum temperature and pH for the enzyme reaction were 60$\circ$C and 11, respectively, and its thermostability was increased by the addition of calcium ion. The enzyme was inactivated by phenylmethylsulfonylfluoride, suggesting it be a serine protease. Comparing with other commercial proteases, the enzyme showed relatively high proteolytic activity against defatted soybean, a water-insoluble protein substrate.

• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.5
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• pp.1015-1018
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• 1998

Capsaicin(8-methyl-N-vanillyl-6-nonenamide: CAP) known well as a major compound of not taste in hot pepper, was investigated for the inhibition effect on in vitro nitrosation. CAP(100$\mu$mol) inhibited the formation of N-nitrosoproline(NPRO) and N-nitrosothioproline(NTPRO) by 56% and 26%, respectively. Vanillyl alcohol inhibited the nitrosation of proline by a concentration-dependent manner, and vanillic acid and vanillin were less effective in blocking the nitrosation of proline compared to CAP and anillyl alcohol. The inhibitory effect of NPRO formation by CAP was evaluated to similar with alpha-tocopherol, and vanillyl alcohol was more effective than alpha-tocopherol in blocking the nitrosation of proline. Our results suggested that CAP and its metabolites such as vanillyl alcohol could inhibit endogenous nitrosation in hydrophobic biological environment.

• Bulletin of the Korean Chemical Society
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• v.17 no.11
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• pp.1036-1039
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• 1996

Synthetic lipoidal peptides based on viral protein sequences have been prepared. These peptides contain an N-palmitoyl group at the N-terminal residue, which is a modified cysteine, containing a S-[2,3-bis(acyloxy)-(2-R,S)-propyl] moiety. When this residue (Pam3Cys) is at the N-terminus of a synthetic peptide, it acts as potent immunoadjuvant to enhance both IgM and IgG antibody responses to the attached peptide. Conventional analytical procedures (e.g., Edman degradation and amino acid analysis) are either not applicable due to the N-terminal modification, or do not provide confirmation of the intact structure. Chromatographic analysis is also hindered by the tendency of these lipoidal Pam3Cys peptides to form large aggregates, and in some cases to be permanently adsorbed on reversed phase columns. We have applied several mass spectrometric techniques, including fast atom bombardment (FAB), electrospray ionization (ESI) and matrix assisted laser desorption ionization (MALDI) to characterize the intact structures of a number of different Pam3Cys synthetic peptides. The MALDI-MS has been found to be the most sensitive for the analysis of the structure of Pam3Cys peptides.