• Proceedings of the Botanical Society of Korea Conference
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• 1987.07a
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• pp.133-148
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• 1987

Gibberellin(GA) 3-$\beta$ hydroxylation is very important for the shoot elogation in the higher plants, since only 3$\beta$-hydryoxylated GAs promote shoot elogation in several plants. Fluctuation of 3$\beta$-hydryoxylase activity was examined during seed maturation using two cultivars of , P. vulgaris, Kentucky Wonder (normal) and Masterpiece (dwarf). Very immature seeds of both cultivars contain high level of 3$\beta$-hydroxylase activity (per mg protein). Both cultivars showed maximum of enzyme activity (per seed) in the middle of their maturation process. Gibberellin 3$\beta$-hydroxylase catalyzing the hydroxylation of GA20 to GA1 was purified 313-fold from very early immature seeds of P. vulgaris. Crude soluble enzyme extracts were purified by 15% methanol precipitation, hydrophobic interaction chromatogrphy, DEAE ion exchange column chromatography and gel filtration HPLC. The 3$\beta$-hydroxylase activity was unstable and lost much of its activity duting the purification. The molecular weight of purified enzyme was extimated to be 42, 000 by gel filtration HPLC and SDS-PAGE. The enzyme exhibited maximum activity at pH 7.7. The Km values for [2.3-3H] GA20 and [2.3-3H]GA9 were 0.29 $\mu$M and 0.33 $\mu$M, respectively. The enzyme requires 2-oxoglutarate as a cosubstrate; the Km value for 2-oxoglutarate was 250 $\mu$M using 3H GA20 as a substrate. Fe2+ and ascorbate significantly activated the enzyme at all purification steps, while catalase and BSA activated the purified enzyme only. The enzyme was inhibited by divalent cations Mn2+, Co2+, Ni2+, Cu2+, Zn2+, Cd2+ and Hg2+. Effects of several GAs and GA anaogues on the putrified 3$\beta$-hydroxylase were examined using [3H]GA9 and GA20 as a substrates. Among them, GA5, GA9, GA15, GA20 and GA44 inhibited the enzyme activity. [13C, 3H] GA20 was converted by the partially purified enzyme preparation to [13C, 3H]GA1, GA5 and GA6, which were identified by GC-MS, GA9 was converted only GA4, GA15 and GA44 were converted to GA37 and GA38, respectively. GA5 was epoxidized to GA6 by the preparation. This suggests that 3$\beta$-hydroxylation of GA20 and epoxidation of GA5 are catalyzed by the same enzyme in P, vulgaris.

• Journal of Powder Materials
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• v.18 no.6
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• pp.552-561
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• 2011

This study attempted to manufacture a Cu-15 at.%Ga coating layer via the cold spray process and investigated the effect of heat treatment environment on the properties of cold sprayed coating material. Three kinds of heat treatment environments, $5%H_2$+argon, pure argon, and vacuum were used in this study. Annealing treatments were conducted at $200{\sim}800^{\circ}C$/1 hr. With the cold sprayed coating layer, pure ${\alpha}$-Cu and small amounts of $Ga_2O_3$ were detected in the XRD, EDS, EPMA analyses. Porosity significantly decreased and hardness also decreased with increasing annealing temperature. The inhomogeneous dendritic microstructure of cold sprayed coating material changed to the homogeneous and dense one (microstructural evolution) with annealing heat treatment. Oxides near the interface of particles could be reduced by heat treatment especially in vacuum and argon environments. Vacuum environment during heat treatment was suggested to be most effective one to improve the densification and purification properties of cold sprayed Cu-15 at.%Ga coating material.

• Resources Recycling
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• v.24 no.4
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• pp.50-55
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• 2015

In this study, we have investigated solvent extraction of Ga and recovery of high pure Ga solution from MOCVD dust for manufacturing of LED chip. Effect of extractan, concentration of extractant were examined for choosing the more effective extractant and high pure Ga solution was fabricated by multi-stage extraction/stripping process. For extraction/separation of Ga based on the analysis of raw-material in previous study, 3 different extractants PC 99A, DP-8R, Cyanex 272 has been investigated and the extraction efficiency of 1.5 M Cyanex 272 was 43.8%. It was conformed that extraction efficiency of Ga was 83% in multi-stage extraction and 5N high purity Ga stripping solution without impurities also obtained.

• Journal of Microbiology and Biotechnology
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• v.15 no.2
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• pp.239-246
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• 2005

Some characteristics of two forms of glucoamylase (glucan 1 A-$\alpha$-glucosidase, EC 3. 2. I. 3) purified from Aspergillus coreanus NR 15-1 were investigated. The enzymes were produced on a solid, uncooked wheat bran medium of A. coreanus NR 15-1 isolated from traditional Korean Nuruk. Two forms of glucoamylase, GA-I and GA-II, were purified to homogenity after 5.8-fold and 9.6-fold purification, respectively, judged by disc- and SDS-polyacrylamide gel electrophoresis. The molecular mass of GA-I and GA-II were estimated to be 62 kDa and 90 kDa by Sephadex G-1OO gel filtration, and 64 kDa and 91 kDa by SDS-polyacrylarnide gel electrophoresis, respectively. The optimum temperatures of GA-I and GA-II were 60$^circ$C and 65$^circ$C, respectively, and the optimum pH was 4.0. The activation energy (Ea value) of GA-I and GA-II was 11.66 kcal/mol and 12.09 kcal/mol, respectively, and the apparent Michaelis constants (K_{m}) of GA-I and GA-II for soluble starch were found to be 3.57 mg/ml and 6.25 mg/ml, respectively. Both enzymes were activated by 1 mM Mn^{2+} and Cu^{2+}, but were completely inhibited by 1 mM N­bromosuccinimide. The GA-II was weakly inhibited by 1 mM p-CMB, dithiothreitol, EDTA, and pyridoxal 5-phosphate, but GA-I was not inhibited by those compounds. Both enzymes had significant ability to digest raw wheat starch and raw rice starch, and hydrolysis rates of raw wheat starch by GA-I and GA-II were 7.8- and 7.3-fold higher than with soluble starch, respectively.

• Microbiology and Biotechnology Letters
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• v.44 no.4
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• pp.470-478
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• 2016

A bacterium producing a large amount of chitinolytic enzyme was isolated from the intestinal tract of earthworm. The isolate was identified as Bacillus licheniformis by 16S ribosomal RNA analysis and designated as B. licheniformis GA9. The enzyme was purified by 40-60% ammonium sulfate precipitation, diethyl-aminoethyl groups exchange chromatography, and gel filtration chromatography. The molecular weight was estimated to be 52.1 kDa and the N-terminal amino acid sequence was D-S-G-K-N-G-K-I-I-R-Y-YP-I-R. The optimum activity of the purified chitinolytic enzyme was shown at pH 5.0 and $40^{\circ}C$, and the enzyme was stable in the ranges of $20-50^{\circ}C$ and pH 5.0-6.0. Enzyme activity was increased by $Co^{2+}$, while it was inhibited by $Cu^{2+}$ and $Fe^{2+}$. But it was recovered by chelating metals with ethylenediaminetetraacetic acid. The $K_m$ and $V_{max}$ values of the purified enzyme were 4.02 mg/ml and 0.52 mg/min, respectively. The chitinolytic enzyme characterized in this study has potential applications in areas such as biotechnology, biomedicine, agriculture, and nutrition.

• Korean Journal of Air-Conditioning and Refrigeration Engineering
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• v.28 no.12
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• pp.509-514
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• 2016

From the point of view to prevent airborne infection-related diseases such as H1N1, SARS, and MERS, an actual application of air cleaning and purification systems including technologies like UVGI has become increasingly important. Recently, an air purification system using REME (Reflective Electro Magnetic Energy) developed in the U.S. is applied for indoor air purification and sterilization technology to counteract the outbreak of new airborne infections. In this study, an air sterilization performance experiment using REME was carried out. The results verified that air sterilization performance in the case of installing a REME system in a medical center was 31%, namely the number of floating bacteria decreased by 31% after only a five-day operation. In addition, the number of culture collections in the REME operating air conditioning systems using nonpathogenic Geobacillus stearothemophilus as a biological indicator decreased maximally to 67%. A field application of REME technology will be useful to prevent airborne infection-related diseases, especially in response to public health crises due to the advent of emerging diseases.

• 한국신재생에너지학회:학술대회논문집
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• 2008.10a
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• pp.383-386
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• 2008

The four-bed PSA process using a layered bed of activated carbon and zeolite 5A was studied to produce a high purity hydrogen product from SMR off-gas. At a desired product purity (99.999%+), the recovery increased with decreasing the linear velocity. However, the difference of the increasing of the recovery became smaller with the decreasing of the linear velocity and then was similar from below the linear velocity 3.9 cm/s. When the adsorbents, the feed gas composition, and the operating conditions are given, the residence time is mainly a function for design of the PSA bed size. The minimum residence time exists to obtain the maximum recovery at desired product purity.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.638-639
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• 2000

Quinone reductase was purified to electrophoretic homogeneity from bovine liver by using ammonium sulfate fractionation, ion-exchange chromatography, and gel filtration chromatography. The enzyme utilized either NADH or NADPH as the electron donor. The optimum pH of the enzyme was pH 8.5, and the activity of the enzyme was greatly inhibited by $Cu^{2+}$ and $Hg^{2+}$ ions, dicumarol and cibacron blue 3GA. The enzyme catalyzed the reduction of several quinones and other artificial electron acceptors. Furthermore, the enzyme catalyzed NAD(P)H-dependent reduction of azobenzene or 4-nitroso-N,N-dimethylaniline. The apparent $K_m$ for 1,4-benzoquinone, azobenzene, and 4-nitroso-N,N-dimethylaniline was 1.64mM, 0.524mM and 0.225mM, respectively. The reduction of azobenzene or 4-nitroso-N,N-dimethylaniline by quinone reductase was strongly inhibited by dicumarol or cibacron blue 3GA, potent inhibitors of quinone reductase.

• The Korean Journal of Zoology
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• v.29 no.4
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• pp.283-293
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• 1986

For the preliminary step to make and characterize the monoclonal antibodies of human alpha-fetoprotein (AFP) was purified from 534g of human fetal tissues through the procedures of tissue extraction, DEAE-cellulose, concanavalin A-Sepharose, Cibacron Blue F3GA-agarose and immunoadsorbent affinity chromatography. The isolated AFP preparation showed a single band on polyacrylamide gel electrophoresis and a single precipitin are against rabbit anti-human cord serum and anti-human AFP on immunoelectrophoresis. Our AFP also displayed a single band on SDS-polyacrylamide gel electrophoresis. The recovery of AFP was 8.76mg total.

• Membrane Journal
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• v.33 no.6
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• pp.369-376
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• 2023

In this study, the alternative to the energy-intensive conventional vacuum distillation process, an eco-friendly and energy-efficient pervaporation separation was employed in 1,2 hexane diol/water (HDO/water) mixture. The crosslinked PVA-glutaraldehyde was coated inside the alumina hollow fiber membrane (Al-HF). In the HDO/IPA pervaporation separation, optimization of the membrane concerning PVA/GA ratio, curing temperature, and pervaporation operating condition were performed. In the long-term stability test, the sustainable pervaporation separation performance giving flux in the range of 1.90~2.16 kg/m²h, and water content in permeate was higher than 99.5% (separation factor = 68) was obtained from the PVA/GA (molar ratio = 0.08, curing temperature = 80℃) coated Al-HF membrane from HDO/water (25/75, w/w, %) mixture at 40℃. Therefore, this work provides potential and inspiration for PVA-based membranes to mitigate excessive energy requirements in HDO/water separation by pervaporation.