• Korean Journal of Food Science and Technology
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• v.21 no.3
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• pp.419-424
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• 1989

The effects of browning Products (BP) from Kanjang(soy sauce) and charcoal on the degradation of aflatoxin $B_1(AFB_1)$ in Kanjang and its model system were studied. Approximately 60% of $AFB_1$ was degraded in the presence of 0.05% BP at pH 7 of phosphate buffer after 2 days of incubation at $30^{\circ}C$. The mutagenicity of the $AFB_1$ which reacted with the BP was decreased to about 50% and 70% in Salmonella typhimurium TA98 and TA100 strains, respectively (p<0.05). When a few pieces of charcoal were added to home made Kanjang, $AFB_1$ was quite stable for 5days at $30^{\circ}C$, however, about 80% of $AFB_1$ was removed when the charcoal was either in distilled water or in 20% of NaCl solution after 2 days of incubation. Activated carbon instead of the charcoal removed $AFB_1$ completely in the all samples under the same conditions.

• YAKHAK HOEJI
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• v.36 no.6
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• pp.538-547
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• 1992

Optimal synthetic condition of barium sulfate were investigated from the viewpoint of yield and bulkiness according to a randomized complete block design proposed by G.E.P. Box and K.B. Wilson. Barium chloride and magnesium sulfate were utilized as reactants in order to prepare barium sulfate in this study. It was found that optimum temperature range of reactant solutions was $60{\sim}100^{\circ}C$ and the optimum concentration range of the reactant solutions was $10{\sim}17.3%$ and $10{\sim}20%$ respectively, on the viewpoint of yield and bulkiness. The optimum mole ratio of $BaCI_2$ to $BaSO_4$ was in the range of $1.50{\sim}2.0$ and the optimum mole ratio of $BaCI_2$ to $BaSO_4$ was in the range of $1.50{\sim}2.0$ and the optimum reacting time range was $15{\sim}20$ minutes. The optimum drying temperature range was $110{\sim}130^{\circ}C$ from the viewpoint of yield, but it was $90{\sim}110^{\circ}C$ on the basis of bulkiness. Apparent viscosity of barium sulfate suspensions dispersed in various concentrations of Na. CMC was measured by using Brookfield synchrolectric viscometer model LVT, the relative equation, log ${\eta}_{sp}=A+B.{\phi}$ was examined and the equation was found to agree fairly well. 1 w/v% Na. CMC aqueous solution and 0.1 volume fraction of $BaSO_4$ powder were optimum in the preparation of $BaSO_4$ suspension showing highest viscosity at infinite shearing.

• KSBB Journal
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• v.11 no.2
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• pp.159-164
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• 1996

Transesterification of used frying oil was investigated to produce the bio-diesel oil. Experimental conditions included molar ratio of used frying oil to alcohol (1:3, 1:5 and 1:7), concentration of catalyst (0.5, 1.0 and 1.5 wt.%), ippe of catalyst(sodium melhoxide, NaOH and KOH), reaction temperature (30, 45 and $60^{\circ}C$), and types of alcohol(methanol, ethanol and butanol). The conversion of used frying oil increased with the alcohol mixing ratio and with the reaction temperature. The effect of the type of catalysts on conversion was not significant. The highest conversion was obtained when methanol was used as alcohol. Viscosity was a little higher with the ester product over grade #2 diesel oil. But the physical properties improved significantly with transesterification, resulting in similar fuel properties with those obtained for grade #2 diesel fuel.

• Journal of Chest Surgery
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• v.22 no.4
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• pp.548-561
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• 1989

In single atrial cells isolated from the rabbit the properties of inward current of Na-Ca exchange were investigated using the whole cell voltage clamp technique. The current was recorded during repolarization following brief 2 ms depolarizing pulse to +40 mV from a holding potential of * 70 mV. Followings are the results obtained: 1. When stimulated every 30 seconds, the inward currents were activated and reached peak values 6-12 ms after the beginning of depolarizing pulse. The mean current amplitude was 342 pA/cell. 2. The current decayed spontaneously from the peak activation and the time course of the relaxation showed two different phases fast and slow phase. The time constants were 10-18 ms and 60-140 ms, respectively. 3. The recovery of inward current was tested by paired pulse of various intervals. The peak current recovered exponentially with time constant of 140 ms and 1 p M isoprenaline accelerated the recovery process. 4. Relaxation time course was also affected by pulse interval and time constant of the fast phase was reduced almost linearly according to the decrease of pulse interval between 30 sec and 1 sec. 5. The peak activation was increased in magnitude by long prepulse stimulation, 5 p M Bay K, 1 p M isoprenaline or internal and external application of c-AMP. 6. The relaxation time constant of the fast phase was prolonged by 5 p M Bay K or c-AMP, and shortened by isoprenaline. However the time course of the slow relaxation phase was not so much changed. From the above results, it could be concluded that increase of the calcium current by Bay K or c-AMP results in the potentiation and prolongation of intracellular calcium transient, and the facilitation of Ca uptake by SR might be a mechanism of shortening the time constant of current relaxation by short interval stimulation or isoprenaline.

• Journal of Microbiology and Biotechnology
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• v.24 no.8
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• pp.1096-1104
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• 2014

$\small{L}$-Asparaginase from gram-positive bacteria has been poorly explored. We conducted recombinant overexpression and purification of $\small{L}$-asparaginase from Staphylococcus sp. OJ82 (SoAsn) isolated from Korean fermented seafood to evaluate its biotechnological potential as an antileukemic agent. SoAsn was expressed in Escherichia coli BL21 (DE3) with an estimated molecular mass of 37.5 kDa, determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Consistent with asparaginases in gram-negative bacteria, size-exclusion chromatography determined SoAsn as a homodimer. Interestingly, the optimal temperature of SoAsn was $37^{\circ}C$ and over 90% of activity was retained between $37^{\circ}C$ and $50^{\circ}C$, and its thermal stability range was narrower than that of commercial E. coli $\small{L}$-asparaginase (EcAsn). Both SoAsn and EcAsn were active between pH 9 and 10, although their overall pH-dependent enzyme activities were slightly different. The $K_m$ value of SoAsn was 2.2 mM, which is higher than that of EcAsn. Among eight metals tested for enzyme activity, cobalt and magnesium greatly enhanced the SoAsn and EcAsn activity, respectively. Interestingly, SoAsn retained more than 60% of its activity under 2 M NaCl condition, but the activity of EcAsn was reduced to 48%. Overall, the biochemical characteristics of SoAsn were similar to those of EcAsn, but its kinetics, cofactor requirements, and NaCl tolerance differed from those of EcAsn.

• The Korean Journal of Mycology
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• v.14 no.1
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• pp.79-84
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• 1986

A cellulose-degrading enzyme from Ganoderma lucidum was partially purified by ammonium sulfate precipitation and its enzymatic properties were studied. The enzyme had an optimum pH for activity at 4.0, and its stability range was pH $4.0{\sim}7.0$. The optimum temperature was $55^{circ}C$ and the enzyme retained 80% original activity after heated at $50^{\circ}C$ for 60 min. The activation energy of the enzyme for CMC degradation was caculated and found to be 6.2 Kcal/mole. The enzyme was activited by the addition of $Co^{++},\;Mn^{++}$, but slightly inactivated by $Hg^{++}$. Various enzyme inhibitors and chemical reagents did not affect the enzyme activity. The enzyme acted on native celluose as well as CMC. The Michaelis constant for CMC was calculated to be 2.4 mg glucose ep/ml.

• Korean journal of food and cookery science
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• v.7 no.3
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• pp.53-59
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• 1991

This study was carried out in order to investigate the change of protein functionalities such as foaming and emulsifying properties by succinylation of protein isolates. Succinylated and unsuccinylated munghean protein isolates were tested for finding out the effects of pH, heat treatment and sodium chloride concentration on the solubility, emulsion capacity, emulsion stability, foaming capacity, and foam stability. The results are summarized as follows: 1. Succinylation enhanced the solubility of MPI except at pH 4.5. When heated, succinylation greatly increased the solubility of succinylated MPI above $60^{\circ}C$. With the addition of NaCl, succinylation increased the solubility of MPI at acidic condition. 2. Emulsion capacity of succinylated MPI showed the lowest value at pH 7 and higher values at acidic and alkaine condition. when succinylated MPI was heated, emulsion capacity showed the highest at $80^{\circ}C$. With NaCl was added, emulsion capacity of succinylated MPI lincreased at pH 7, 9 or 11 decreased at pH 3 except addition of 1.0M NaCl. 3. Emulsion stability of MPI and succinylated MPI showed the highest at pH 4.5. Succinylation enhanced the emulsion stability of MPI at acidic condition. 4. The foaming capacity of MPI was increased at pH 3, 7 or 9 by succinylation. 5. When heated, foam stability of MPI and succinylated MPI showed the highest at pH 4.5 and at pH 11, respectively. When heated, both proteins showed the highest stability at $100^{\circ}C$.

• Fisheries and Aquatic Sciences
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• v.14 no.3
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• pp.186-191
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• 2011

An agar-degrading enzyme-producing strain was isolated from seawater. The isolate was identified as Microbulbifer sp. SD-1 by 16S rRNA sequencing analysis. The optimal pH and temperature for growth were 6.0 and $30^{\circ}C$, respectively, and growth was possible at pH 9.0 and $60^{\circ}C$. The isolate required 5% NaCl for optimal growth and showed 45% growth activity without NaCl. Agar concentrations of 0-0.4% in the medium did not affect growth. Thin-layer chromatography analysis revealed that this strain could degrade agar into a monosaccharide and oligosaccharide, which may have industrial applications.

• Korean Journal of Microbiology
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• v.13 no.3
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• pp.85-90
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• 1975

Crude cellulases freshly prepared from cultures of Aspergillus niger, Prnicillum motatum, Trichoderma vride 16273 and Trichoderma viride 16374 were assayed on 4 different substrates including Na-CMC, cellulose powder, starch and sucrose. Enzyme prepared from A. niger contained highly active hydrolytic enzymes of the 4 substrates assayed. P. notatum [yielded relatively lower amount of cellulase but the extracts were also highly reactive on starch and sucrose. Trichoderma viride 16274 yielded very little cellulase and invertase, but the extracts showed a high degree of amylase activity. Trichoderma viride 16374, however, yielded collulase comparable to that of Penicillium notatum, but lower activities of amylase and invertase were seen. Commercial cellulases prepared from Penicillium notatum (cellulase[K]) and Trichoderma viride(cellulase[J]) indicated enzyme activities closely parallel to the crude enzymes freshly prepared from fungus cultures. The optimum pH's of cellulolytic activities of cellulase[K] and cellulase[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase[K] and cellualse[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase [K] and cellulase [J] were $60{\circ}C$ and $50{\circ}C$ respectively. Assuming the average molecular weight of Na-CMC is about 115,000, the Km values of cellulase [K] and cellulase[J] were found to be $3.3{\times}10^{-5}/nM$ and $3.3{\times}10^{-4}/nM$ respectively.

• Journal of Korean Society on Water Environment
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• v.18 no.4
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• pp.421-433
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• 2002

This study was conducted to develope a simple, rapid and solvent-free solid-phase microextraction(SPME) procedure for extracting three organochlorine, one triazine and nine organophosphorus pesticides from water. The optimal conditions of SPME for analyses of organochlorine pesticides were obtained at $250^{\circ}C$ of desorption temperature, 45 minutes of equilibrium time, pH 6 and NaCl 0% addition using $100{\mu}m$ polydimethylsiloxane fiber and those of triazine and organophosphorus pesticides were obtained at $270^{\circ}C$ of desorption temperature, 60 minutes of equilibrium time, pH 6 and NaCl 0% addition using $100{\mu}m$ polydimethylsiloxane fiber. This method showed good lineality for organochlorine pesticides between 0.0001 and $10{\mu}g/L$ with regression coefficients ranging 0.9986~0.9992 and for triazine and organophosphorus pesticides between 0.01 and $10{\mu}g/L$ with regression coefficients ranging 0.9867~0.9998.