• Applied Chemistry for Engineering
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• v.7 no.5
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• pp.1006-1014
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• 1996

A series of catalysts, $NiO-ZrO_2/WO_3$, for ethylene dimerization were prepared by coprecipitation from a solution of nickel chloride - zirconium oxychloride mixture followed by dry impregnation with an aqueous solution of ammonium metatungstate and calcination in air. On the basis of the results obtained from x-ray diffraction and DSC, the addition of NiO and $WO_3$ to $ZrO_2$ shifted the transition of $ZrO_2$ from amorphous to a tetragonal phase toward higher temperatures due to the interaction between NiO(or $WO_3$) and $ZrO_2$. $NiO-ZrO_2$ without $WO_3$ was inactive for the ethylene dimerization, but $NiO-ZrO_2/WO_3$ was found to be very active even at room temperature. The high catalytic activity of $NiO-ZrO_2/WO_3$ was closely correlated with the increase of acid strength by the inductive effect of $WO_3$.

• Korean Chemical Engineering Research
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• v.48 no.3
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• pp.382-390
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• 2010

In this research hydrogen sulfide, ammonia and toluene were designated as the representative source of malodor and VOC, respectively, frequently generated at the compost manufacturing factory and publicly owned facilities. The optimum operating condition to treat the waste air(2 L/min) containing malodor was constructed using photocatalytic reactor/biofilter process with humidifier composed of fluidized aerobic anf anoxic reactor. The ammonia(300 ppmv) of fed-waste air was removed by 22, 55 and 23% at the stage of photocatalytic reactor, humidifier and biofilter, respectively. The toluene(100 ppmv) of fed-waste air was removed by 20, 10 and 70% at the stage of photocatalytic reactor, humidifier and biofilter, respectively. Therefore the water-soluble ammonia and the water-insoluble toluene were treated mainly at the stage of humidifier and biofilter, respectively. In addition, hydrogen sulfide(10 ppmv) was almost treated at the stage of photocatalytic reactor and its negligible trace was absorbed in humidifier so that it was not detected before biofilter process. The nitrate concentration of the process water from anoxic reactor was found lower by 3 ppm than that from fluidized aerobic reactor. Besides, the dissolved ammonia-nitrogen concentration of the process water from humidifier remained at the high value of 1,500-2,000 ppm, which may be attributed to the existence of ammonium chloride and other source of ammonium nitrogen.

• Korean Journal of Microbiology
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• v.53 no.3
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• pp.200-207
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• 2017

A new approach to the solubilization of waste activated sludge (WAS) using alginate-quaternary ammonium complex beads was investigated under controlled mild alkaline conditions. The complex beads were prepared by the reaction of sodium alginate (SA) with 3-(trimethoxysilyl)propyl-octadecyldimethylammonium chloride (TSA) in acid solution, followed by crosslinking with $CaCl_2$. Treatment of WAS with SA-TSA complex beads was effective for enhancing the efficacy of WAS solubilization. The highest value of soluble chemical oxygen demand (SCOD) concentration (3,900 mg/L) was achieved after 10 days of treatment with 30% (v/v) SA-TSA complex beads. The WAS solubilization efficacy of the complex beads was also evaluated by estimating the concentrations of volatile fatty acids (VFAs). The maximum value of VFAs was 2,961 mg/L, and the overall proportions of VFAs were more than 75% of SCOD. The main components of VFAs were acetic, propionic, iso-butyric, and butyric acids. These results suggest that SA-TSA complex beads might be useful for enhancing the solubilization of WAS. The potential use of VFAs as the external carbon substrate for the production of polyhydroxyalkanoate (PHA) by a mixed microbial culture (MMC) was also examined. The enrichment of PHA-accumulating MMC could be achieved by periodic feeding of VFAs generated from WAS in a sequencing batch reactor. The composition of PHA synthesized from VFAs mainly consisted of 3-hydroxybutyrate. The maximum PHA content accounted for 25.9% of dry cell weight. PHA production by this process is considered to be promising since it has a doubly beneficial effect on the environment by reducing the amount of WAS and concomitantly producing an eco-friendly biopolymer.

• Korean Chemical Engineering Research
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• v.46 no.6
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• pp.1100-1106
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• 2008

In this study, we presented rapid and simple fabrication method of functionalized surface on various substrates as a universal platform for the selective immobilization of cells. The functionalized surface was achieved by using deposition of polyelectrolyte such as poly(allyamine hydrochloride) (PAH), poly(diallyldimethyl ammonium chloride) (PDAC), poly(4-ammonium styrene sulfonic acid) (PSS), poly(acrylic acid) (PAA) and fabrication of poly(ethylene glycol) (PEG) microstructure through micro-molding in capillaries (MIMIC) technique on each glass, poly(methyl methacrylate) (PMMA), polystyrene (PS) and poly(dimethyl siloxane) (PDMS) substrate. The polyelectrolyte multilayer provides adhesion force via strong electrostatic attraction between cell and surface. On the other hand, PEG microstructures also lead to prevent non-specific binding of cells because of physical and biological barrier. The characteristic of each modified surface was examined by using static contact angle measurement. The modified surface onto several substrates provides appropriate environment for cellular adhesion, which is essential technology for cell patterning with high yield and viability in the micropatterning technology. The proposed method is reproducible, convenient and rapid. In addition, the fabrication process is environmentally friendly process due to the no use of harsh solvent. It can be applied to the fabrication of biological sensor, biomolecules patterning, microelectronics devices, screening system, and study of cell-surface interaction.

• Korean Journal of Food Science and Technology
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• v.7 no.4
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• pp.243-249
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• 1975

This experiment were carried out to investigate the conditions of amylase produced by Candida muscorum in wheat bran cultures and the properties of its amylase (crude enzyme). The results obtained were as follows. 1. The optimum conditions for amylase production in wheat bran cultures were; water content 75 percent, temperature $25^{\circ}C$ and incubation time 4-7 days. 2. The production of amylase was increased about 20 percent in the medium added 0.5 percent of ammonium sulfate or ammonium chloride to wheat bran, but the production of those was decreased in the case of addition of nitrates. 3. No significant effect was found in the case of the addition of carbon source on the production of amylase. 4. The properties of liquefying amylase of the selected strain were; the optimum pH 4.2, the optimum temperature $60-65^{\circ}C$, the stable pH 3.2-6.8 and the stable heating (for 15 minutes heating) below $65^{\circ}C$. 5. The properties of saccharifying amylase of the selected strain were; the optimum pH 4.5, the optimum temperature $55^{\circ}C$, the stable pH 3.8-6.2 and the stable heating (for 15 minutes heating) below $45^{\circ}C$.

• Journal of the Korean Applied Science and Technology
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• v.36 no.2
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• pp.407-416
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• 2019

The criticical micelle concentration (CMC) was measured by using the UV-Vis method for the micellization of the ammonium type cationic surfactants (DTAB, TTAB, and CTAB) in the aqueous aniline solution. The enthalpy change (${\Delta}H^0$) and entropy change (${\Delta}S^0$) were calculated from the dependence of Gibbs free energy change (${\Delta}G^0$) on the temperature for micellization of the cationic surfactants between 290K and 314K. The effects of n-butanol and sodium chloride on the micellization of cationic surfactants were measured and compared with the other thermodynamic functions. All the free energy changes (${\Delta}G^0$) of the micellization were negative, all the enthalpy change (${\Delta}H^0$) were negative, and all the entropy change (${\Delta}S^0$) were positive values, respectively. The micelle formation of cationic surfactant in aniline solution is a spontaneous exothermic reaction, and the iso-structural temperature calculated from the thermodynamic values show that enthalpy and entropy contribution to the micellization are almost the same for the micellization of cationic surfactants

• Microbiology and Biotechnology Letters
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• v.7 no.3
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• pp.135-140
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• 1979

A Streptomyces sp. strain AS-727 which was capable of producing penicillinase, was isolated from soil. The enzyme production was affected by the carbon and nitrogen sources added. Among them so far tested, glucose (or maltose) and sodium nitrate increased the enzyme production. And the amount of enzyme prodced reached maximum in 4 days cultivation. The optimla pH and temperature of the penicillinase was between pH 6.0 to 8.0 and 4$0^{\circ}C$ respectively. The stabel pH range of the enzyme was stable at 4$0^{\circ}C$, but it lost about 30％ and 40％ of the the activity respectively when it was treated at 6$0^{\circ}C$ and 8$0^{\circ}C$ for 60 minutes. The activity of the enzyme was inhibited by Z $n^{++}$, but A $g^{+}$, $Co^{++}$, $_Mn^{++}$, $Ca^{++}$, P $b^{++}$ did not affected enzyme activity. Peculiarly, the enzyme protein precipitated by freezing or addition of ammonium sulfate, urea, sodium chloride and some organic solvents as etanol, methanol, acetone was not dissolved in deionized water or any buffer solution.n.n.ion.n.n.

• Journal of Nutrition and Health
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• v.19 no.6
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• pp.363-373
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• 1986

This study was devised to elucidate whether soused shrimp exhibits a digestive action on boiled pork meats. and the mechanism by which sousing with a high concentration of sodium chloride preserves nutrients in foods for a prolonged pe\ulcornerriod. Protease was isolated from soused shrimp using a combination of ammonium sulfate fractionation. DEAE - cellulose ion exchange chromatography and gel filtra\ulcornertion. The isolated protease had specific activity of 1.560 units. 210 purification fo\ulcornerld with an yield of 38%. Its optimum pH and temperature were 8.0 and $43^{\circ}C$ respectively. The molecular weight of the enzyme was 35.000. The Km value of the enzyme for casein was 1.6 x $10^{-6}$ M The e=yme required the presence of cu\ulcornerpric ion to exhibit its full activity. Eighty eight percent of the enzyme activity was in\ulcornerhibited by 3.5M NaCI showing a reversibly linear decrease of the enzyme activity as NaCI concentration increased. The nature of the inhibition by NaCl was rever\ulcornersible and noncompetitive. The protease activity in soused shrimp was well preser\ulcornerved with the elapse of time at least in part due to NaCI induced suppression of autodigestion. The enzyme was denatured by acid easily. i.e. 1% of the original activity remained after staying at pH 2 for 10 minutes. which is within the norm\ulcorneral range of pH of the human stomach. Soused shrimp was observed to be one of those containing the highest protease activity compared with the other soused foo\ulcornerds such as soused oyster. squid. clam. and Pollack intestine with respect to spec\ulcornerific activities of dialized 1:4 whole homogenates(w/v) in 5 mM sodium phospha\ulcornerte - 2.4 mM j3 - mercaptoethanol buffer. pH 8.0. Casein and boiled meats including pork, beef, and chicken appeared to be the good substrates for the protease. Casein was the best. Therefore. the ingestion of boiled meats including pork together with soused sh\ulcornerrimp would help digestion of boiled pork in human not only by increasing appe\ulcornertite also by the direct proteolytic digestion of boiled meats by soused shrimp to\ulcorner some extent. And a high concentration of sodium chloride inhibited the protease activity reversibly in a remarkable degree, which ensued in a significant retardat\ulcornerion of autodigestion of protein in foods by proteases, and hereby contributed to the preservation of foods for an extended period.

• The Korean Journal of Pharmacology
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• v.28 no.1
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• pp.91-102
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• 1992

In $Ca^{++}$ containing media, arachidonic acid markedly stimulated superoxide and $H_2O_2$ generation and activated NADPH oxidase. In $Ca^{++}$ free media, stimulatory action of arachidonic acid on NADPH oxidase was not detected. Arachidonic acid-stimulated respiratory burst was inhibited by EGTA, TMB-8, verapamil, diltiazem, nifedipine, dibucaine, lidocaine, CCCP, 2,4-dinitrophenol, sodium arsenate, chlorpromazine, theophylline, $HgCl_2$, PCMB and PCMBSA but not affected by tetrodotoxin, tetraethylammonium chloride and procaine. EGTA almost completely inhibited release of ${\beta}-glucuronidase$ by arachidonic acid and verapamil, CCCP and theophylline slightly inhibited it, whereas dibucaine did not show any significant effect. Arachidonic acid induced $Ca^{++}$ release from intact neutrophils and it was decreased by TMB-8. Arachidonic acid-induced elevation of intracellular free $Ca^{++}$ level was inhibited by EGTA and CCCP and slightly inhibited by TMB-8. Amount of intracellular free $Ca^{++}$ increased by either arachidonic acid plus verapamil or arachidonic acid plus dibucaine was greater than that by arachidonic acid alone. These results suggest that various changes of biochemical events may be implicated in the functional expression in neutrophils activated by arachidonic acid. Arachidonic acid appears to elevate cytosolic free $Ca^{++}$ level by stimulating $Ca^{++}$ release from intracellular $Ca^{++}$ storage sites. During activation of neutrophils, $Ca^{++}$ influx and efflux may be accomplished, simultaneously.

• Applied Biological Chemistry
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• v.41 no.1
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• pp.6-12
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• 1998

To extract insoluble proteins and to improve functional properties of abolished proteins, a protease producing Aspergillus sp. MS-18 was isolated from soil. The enzyme was purified and its enzymological characteristics were investigated. It was found that production of protease reached to the maximum when the wheat brae medium containing, 3% arabinose, 0.5% polypepton, 0.1% $(NH_4)_2SO_4$ and 0.2% magnesium chloride was cultured for 3 days. Protease was purified 16.9 folds after ion exchange chromatography and gel filtration and the specific activity was 340.4 unit/mg. Purified enzyme was confirmed as a single band by the polyacrylamide gel electrophoresis. The molecular weight of protease was estimated to be 30,000. Crystalization form of purified protease was a stick shape with rounding edges. The optimum pH and temperature for the protease activity were 9.0 and $60^{\circ}C$, respectively. The enzyme was stable in pH 7.0-12.0 at $50^{\circ}C$. The activity of purified enzyme was inhibited by $Hg^{2+}$, $Cu^{2+}$, $Zn^{2+}$ and $Pb^{2+}$, whereas it was activited by $Na^+$, $Mg^{2+}$ and $Mn^{2+}$. The activity of the protease was inhibited by the treatment with ethylenediaminetetraacetic acid and phenylmethane sulfonyl fluoride. The result suggests that the purified enzyme is a serine protease with metal ion at active site. Km and Vmax of purified protease were $29.33\;{\mu}mole/L$ and $5.13\;{\mu}g/min$, respectively.