• Journal of Korean Society for Atmospheric Environment
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• v.32 no.5
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• pp.526-535
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• 2016

Recently, fine dust in atmosphere have been considerably issued as a harmful element for human. Nitrogen oxide ($NO_x$) exhausted from diesel engines and power plants has been disclosed as a main source of secondary production of fine dust. In order to prevent exhausting these nitrogenous compounds into atmosphere, a treatment system with selective catalytic reduction (SCR) catalyst with ammonia as a reductant has been used in various industries. Urea solution has been widely studied to supply ammonia into a SCR catalytic reactor, safely. However, the conversion of urea solution to ammonia has several challenges, especially on a slow conversion velocity. In the present study, a fast urea conversion system including a plasma burner was suggested and designed to evaluate the performances of urea conversion and initial operation time. A designed lab-scale facility has a plasma burner, urea nozzle, mixer, and SCR catalyst which is for hydrolysis of isocyane. Flow rate of methane that is a fuel of the plasma burner was varied to control temperatures in the urea conversion facility. From experimental results, it is found that urea can be converted into ammonia using high temperature condition of above $400^{\circ}C$. In the designed test facility, it is found that ammonia can be produced within 1 min from urea injection and the result shows prospect commercialization of proposed technology in the SCR facilities.

• BMB Reports
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• v.33 no.3
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• pp.213-220
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• 2000

A fulminant hepatitis is associated with massive liver cell necrosis and a high mortality rate. But survivors regenerate a normal liver and do not have chronic liver disease. This clinical course suggests that the acutely injured livers release a factor that allows a recovery from chronic hepatitis or cirrhosis. The objective of this study was to isolate and characterize an anti-fibrotic factor from acutely damaged rat livers. The liver cell necrosis was prepared from rat by warm ischemical perfusion and the perfusates were assessed against the growth inhibition of fat-storing cells (FSC). A liver-derived growth inhibitory factor (LDGIF) was purified from ischemically damaged rat livers by chromatographies on Sephacryl S-300, CM Sepharose, hydroxyapatite, and Superose 12. The LDGIF was isolated with an overall purification of 194-fold and 40% recovery. Although LDGIF was identified as the rat liver arginase by Nterminal sequence analysis, LDGIF exists as a monomer and the purified native arginase has a trimer form. Furthermore, LDGIF has a lower enzyme activity on the hydrolysis of L-arginine and a higher inhibitory effect on proliferation of FSC than the normal rat liver arginase. The catalytic activity of LDGIF is ascribed to the monomeric characteristics of the LDGIF. Therefore, the inhibitory action of LDGIF might not be due to the arginine depletion by the catalytic activity of arginase. In conclusion, the presence of the LDGIF could interpret the clinical course that serious fibrosis is not found in the liver of patients recovering from severe hepatic necrosis due to fulminant hepatitis, suggesting that this LDGIF may provide a novel target for the prevention and treatment of hepatic fibrosis.

• Journal of Life Science
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• v.24 no.12
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• pp.1378-1382
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• 2014

Phospholipase D (PLD) catalyzes the hydrolysis of phospholipid to phosphatidic acid (PA), a lipid secondary messenger. Two forms of PLD isozymes, phosphatidylcholine-specific PLD1 and PLD2, have been identified. PLD has emerged as a critical regulator of cell proliferation and survival signaling, and dysregulation of PLD occurs in a various illnesses, including cancer. PLD activity is essential for cell survival and protection from apoptosis. Overexpression of PLD isozymes or PLD-generated PA attenuates the expression of apoptotic genes and confers resistance to apoptosis. The apoptosis-related molecular mechanisms of PLD remain largely unknown. Recently, the dynamics of PLD turnover during apoptosis have been reported. The cleavage of PLD isozymes as specific substrates of caspase differentially regulates apoptosis. PLD1 is cleaved at one internal site, and PLD2 is cleaved two sites at the front of the N-terminus. The cleavage of PLD1 reduces its enzymatic activity, probably via the dissociation of two catalytic motifs, whereas the cleavage of PLD2 does not affect the catalytic motifs and its activity. Thus, PLD2 maintains antiapoptotic capacity, despite its cleavage. Therefore, the differential cleavage pattern of PLD isozymes by caspase affects its enzymatic activity and antiapoptotic function. Thus, PLD is considered a potential target for cancer therapy. We summarize recent studies regarding the functional role of PLD in apoptosis.

• Applied Chemistry for Engineering
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• v.31 no.2
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• pp.125-137
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• 2020

In recent years, toxic organophosphorus compounds (OPs) have been used for civilians, becoming a great threat to the world. Alternative to the current treatment policy unpredictable for any prevention, researches on bioscavenger as an improved treatment have been actively conducted. Bioscavengers refer to proteins and enzymes that prevent intoxication by inactivating or binding toxic OPs before they reaches the target. In particular, extensive efforts have been made to develop catalytic bioscavengers that quickly detoxify OPs even with a small dose of the protein by performing multiple binding and hydrolysis processes with OPs. This review introduces the latest studies and results for developing catalytic bioscavengers using molecular evolution and protein engineering techniques. We will briefly present some of the remaining challenges on developing enzymes into clinically approved drugs.

• Korean Journal of Chemical Engineering
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• v.35 no.11
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• pp.2220-2231
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• 2018

Lipase from Candida rugosa was immobilized on $MgO{\cdot}SiO_2$ hybrid grafted with amine, thiol, cyano, phenyl, epoxy and carbonyl groups. The products were analyzed using Fourier transform infrared spectroscopy, nuclear magnetic resonance, low-temperature $N_2$ sorption and elemental analysis. Additionally, the degree of coverage of the oxide material surface with different functional groups and the number of surface functional groups were estimated. The Bradford method was used to determine the quantity of immobilized enzyme. The largest quantity of enzyme (25-28 mg/g) was immobilized on the hybrid functionalized with amine and carbonyl groups. On the basis of hydrolysis reaction of p-nitrophenyl palmitate to p-nitrophenol, it was determined how the catalytic activity of the obtained biocatalysts is affected by pH, temperature, storage time, and repeated reaction cycles. The best results for catalytic activity were obtained for the lipase immobilized on $MgO{\cdot}SiO_2$ hybrids with amine and carbonyl groups. The biocatalytic system demonstrated activity above 40% in the pH range 4-10 and in the temperature range $30-70^{\circ}C$. Lipase immobilized on the $MgO{\cdot}SiO_2$ systems with amine and epoxy groups retains, respectively, around 80% and 60% of its initial activity after 30 days of storage, and approximately 60-70% after 10 reaction cycles.

• Applied Chemistry for Engineering
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• v.8 no.5
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• pp.777-783
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• 1997

$TiO_2$ powders were synthesized via hydrolysis reaction of titanium n-propoxide in n-propanol solvent and the reaction rates were studied by use of UV-vis spectroscopic method. Concentration of water, reaction temperature, reaction time and acid-base effects of the solution were investigated to determine the optimum conditions for $TiO_2$ powder synthesis. The reaction were controlled to proceed to pseudo-first orders reaction in the presence of excess water in n-propanol solvent. The rate constants which varied with temperature and concentration of water were calculated by Guggenheim method. Reaction using $D_2O$ was also carried out to determine the catalytic character of water. $TiO_2$ powders were synthesized only in the neutral and basic solution and those were almost spheric forms having average particle size of $0.4-0.7{\mu}m$ diameter. Particle size decreased with increasing concentration of water and reaction temperature, however, increased with increasing reaction time. Associative $S_N2$ mechanism for the hydrolysis was proposed from the data of n-value in the transition state and thermodynamic parameter. $D_2O$ solvent isotope effect showed that $H_2O$ molecules reacted as nucleophilic catalysis.

• Journal of Microbiology and Biotechnology
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• v.18 no.2
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• pp.287-294
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• 2008

Three amino acid residues (His119, Glu164, and Glu338) in the active site of Thermus caldophilus GK24 ${\beta}$-glycosidase (Tca ${\beta}$-glycosidase), a family 1 glycosyl hydrolase, were mutated by site-directed mutagenesis. To verify the key catalytic residues, Glu164 and Glu338 were changed to Gly and Gln, respectively. The E164G mutation resulted in drastic reductions of both ${\beta}$-galactosidase and ${\beta}$-glucosidase activities, and the E338Q mutation caused complete loss of activity, confirming that the two residues are essential for the reaction process of glycosidic linkage hydrolysis. To investigate the role of His119 in substrate binding and enzyme activity, the residue was substituted with Gly. The H119G mutant showed 53-fold reduced activity on 5mM p-nitrophenyl ${\beta}$-D-galactopyranoside, when compared with the wild type; however, both the wild-type and mutant enzymes showed similar activity on 5mM p-nitrophenyl ${\beta}$-D-glucopyranoside at $75^{\circ}C$. Kinetic analysis with p-nitrophenyl ${\beta}$-D-galactopyranoside revealed that the $k_{cat}$ value of the H119G mutant was 76.3-fold lower than that of the wild type, but the $K_m$ of the mutant was 15.3-fold higher than that of the wild type owing to the much lower affinity of the mutant. Thus, the catalytic efficiency $(k_{cat}/K_m)$ of the mutant decreased to 0.08% to that of the wild type. The $k_{cat}$ value of the H119G mutant for p-nitrophenyl ${\beta}$-D-glucopyranoside was 5.l-fold higher than that of the wild type, but the catalytic efficiency of the mutant was 2.5% of that of the wild type. The H119G mutation gave rise to changes in optima pH (from 5.5-6.5 to 5.5) and temperature (from $90^{\circ}C\;to\;80-85^{\circ}C$). This difference of temperature optima originated in the decrease of H119G's thermostability. These results indicate that His119 is a crucial residue in ${\beta}$-galactosidase and ${\beta}$-glucosidase activities and also influences the enzyme's substrate binding affinity and thermostability.

• Animal Bioscience
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• v.34 no.5
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• pp.867-879
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• 2021

Objective: Fibronectin 3 (FN3) and immunoglobulin like modules (Ig) are usually collocated beside modular cellulase catalytic domains. However, very few researches have investigated the role of these modules. In a previous study, we have sequenced and analyzed bacterial metagenomic DNA in Vietnamese goats' rumen and found that cellulase-producing bacteria and cellulase families were dominant. In this study, the properties of modular cellulases and the role of a FN3 in unique endoglucanase belonging to glycosyl hydorlase (GH) family 5 were determined. Methods: Based on Pfam analysis, the cellulases sequences containing FN3, Ig modules were extracted from 297 complete open reading frames (ORFs). The alkaline, thermostability, tertiary structure of deduced enzymes were predicted by AcalPred, TBI software, Phyre2 and Swiss models. Then, whole and truncated forms of a selected gene were expressed in Escherichia coli and purified by His-tag affinity column for assessment of FN3 ability to enhance enzyme activity, solubility and conformation. Results: From 297 complete ORFs coding for cellulases, 148 sequences containing FN3, Ig were identified. Mostly FN3 appeared in 90.9% beta-glucosidases belonging to glycosyl hydrolase family 3 (GH3) and situated downstream of catalytic domains. The Ig was found upstream of 100% endoglucanase GH9. Rarely FN3 was seen to be situated downstream of X domain and upstream of catalytic domain endoglucanase GH5. Whole enzyme (called XFN3GH5 based on modular structure) and truncate forms FN3, XFN3, FN3GH5, GH5 were cloned in pET22b (+) and pET22SUMO to be expressed in single and fusion forms with a small ubiquitin-related modifier partner (S). The FN3, SFN3 increased GH5 solubility in FN3GH5, SFN3GH5. The SFN3 partly served for GH5 conformation in SFN3GH5, increased modules interaction and enzyme-soluble substrate affinity to enhance SXFN3GH5, SFN3GH5 activities in mixtures. Both SFN3 and SXFN3 did not anchor enzyme on filter paper but exfoliate and separate cellulose chains on filter paper for enzyme hydrolysis. Conclusion: Based on these findings, the presence of FN3 module in certain cellulases was confirmed and it assisted for enzyme conformation and activity in both soluble and insoluble substrate.

• Biotechnology and Bioprocess Engineering:BBE
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• v.1 no.1
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• pp.46-50
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• 1996

In order to design industrial scale reactors and proceises for multi-phase biocatalytic reactions, it is essential to understand the mechanisms by which such systems operate. To il-lustrate how such mechanisms can be modeled, the hydrolysis of the primary ester groups of triglycerides to produce fatty acids and monoglycerides by lipased (glycerol-ester hydrolase) catalysis has been selected as an example of multiphase biocatalysis. Lipase is specific in its behavior such that it can act only on the hydrolyzed (or emulsified) part of the substrate. This follows because the active center of the enzyme is catalytically active only when the substrate contacts it in its hydrolyzed form. In other words, lipase acts only when it can shuttleback and forth between the emulsion phase and the water phase, presumably within an interphase or boundary layer between these two phases. In industrial applications lipase is employed as a fat splitting enzyme to remove fat stains from fabrics, in making cheese, to flavor milk products, and to degrade fats in waste products. Effective use of lipase in these processes requires a fundamental understanding of its kinetic behavior and interactions with substrates under various environmental conditions. Therefore, this study focuses on modeling and simulating the enzymatic activity of the lipase as a step towards the basic understanding of multi-phase biocatalysis processes.

• Journal of the Korean Chemical Society
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• v.33 no.2
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• pp.263-270
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• 1989

Aluminum alkoxide, $Al(OC_3H_7\^i)_3\;and\;Al(OC_4H_9^s)_3$, were synthesized using aluminum sheet and corresponding alcohols to prepare various phase alumina in high purity. Aluminum hydroxides were prepared by hydrolysis of synthesized Al-alkoxides and from reagent $AlCl_3$. The catalytic properties of ${\gamma}$ and ${\eta}-Al_2O_3$ prepared at various temperatures were investigated and the reaction kinetics of ${\alpha}-Al_2O_3$ formation from $Al(OH)_3$ was considered.