• Applied Biological Chemistry
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• v.24 no.3
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• pp.186-193
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• 1981

Three fractions of carboxymethyl-cellulase (F-I, F-II, and F-III) and ${\beta}-glucosidase$ form Aspergillus niger were partially purified by ammonium sulfate fractionation. Sephadex G-150 and DEAE-Sephadex column chromatography. The optimum conditions such as pH and temperature and thermal inactivation properties of the enzymes were investigated. Arrhenius plots of F-II and F-III appeared as straight lines, whereas that of F-I was biphasic. The Z-values of F-II and F-III were $8^{\circ}C$ and $10^{\circ}C$ respectively, while that of F-I was $4^{\circ}C$ over $60{\sim}70^{\circ}C$ and $383^{\circ}C$ over $70{\sim}98^{\circ}C$. Three fractions and the crude extract of carboxymethyl-cellulase exhibited a similar optimum pH 4.3 and temperature of $60^{\circ}C$, while Z-value of crude extract $(21.5^{\circ}C)$ was much higher than that of the purified enzyme. Maximum activity of both purified and crude extract of ${\beta}-glucosidase$ was shown at pH 4.7 and $60^{\circ}C$, and z-value of the enzyme was $7^{\circ}C$.

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.2
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• pp.228-233
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• 2001

This study was carried out to characterize the enzymatic properties and effectiveness on the firmness of pectinesterase(PE) and polygalacturonase(PG) which are present in carrot cell wall, and to determine the blanching condition of raw carrot. Crude enzyme was extracted from carrots and used as PE and PG. The optimum pH of PE and PG activity were 7.0 and 5.0, respectively. NaCl enhanced PE and PG activities, particularly at 0.15 M and 0.10 M, respectively. Although the optimum temperature of PG ($70^{\circ}C$) was higher than that of PE ($50^{\circ}C$), PE ($Z-value=8.76^{\circ}C$) was more heat-stable than PG($Z-value=6.67^{\circ}C$). Blanching condition was determined as at $55^{\circ}C$ for 60 min in 0.03 M $CaCl_2$, 0.1 M NaCl and pH 7.0 from measuring firmness after blanching at various temperature ($50~70^{\circ}C$) and time (5~60 min).

• Applied Chemistry for Engineering
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• v.23 no.6
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• pp.594-598
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• 2012

In the present study, biogas was produced from the anaerobic digestion of marine macroalgae (Laminaria japonica) biomass. The optimal anaerobic condition for producing the sludge was the freeze treatment at $-70^{\circ}C$ for 20 min. Total amounts of hydrogen and methane gas produced were 667.28 mL/L and 3420.24 mL/L, respectively, which were 2.7 and 3.4 times greater than that in the control group. Freeze treatment of sludge produced the maximum biogas under an initial optimum pH of 7.0 and the maximum biomass at an initial optimum pH of 8.0. We confirmed that biogas production was greatly reduced under acidic conditions compared to that under alkaline conditions. Sludge was freeze treated, and the biomass and sludge production was optimal the total amounts of hydrogen and methane gas produced were 643.73 mL/L and 4291.6 mL/L, respectively, which were 2.6 and 4.3 times greater than in the control group. Also the results showed that under optimal conditions in a 5-L bioreactor, a maximum of 1605.03 mL/L of hydrogen and 4593.71 mL/L of methane gas could be produced by the substrate contained in the marine macroalgae biomass.

• Applied Biological Chemistry
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• v.41 no.5
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• pp.337-341
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• 1998

The morphological and cultural characteristics of alkalophilic Coryneform bacteria TU-19 were investigated at various pHs. This bacterium showed normal growth pattern at $pH\;9.0{\sim}10.0$, but the cell growth was completely inhibited at extreme pH (12.0 or more). Interestingly, at pH 8.0 the morphology of the bacterial cells seems to form convoluted filaments during the exponential growth phase while at pH 10.0, the optimal pH for the growth of this organism, the bacteria grew with variable paired or single forms, and straight rods during growth stages. Growing in alkaline media $(pH\;9.0{\sim}11.0)$, it adjusted the pH of the culture media to around pH 8.5 by itself.

• KSBB Journal
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• v.23 no.1
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• pp.83-89
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• 2008

Food wastewater derived from the three-stage methane fermentation system developed in this lab contained high concentration organic substances. The organic wastewater should be treated through advanced wastewater treatment system to satisfy the "Permissible Pollutant Discharge Standard of Korea". In order to treat the organic wastewater efficiently, several optimum operation conditions of a modified $UV/TiO_{2}$ photocatalytic system have been investigated. In the first process, wastewater was pre-treated with $FeCl_{3}$. The optimum pH and coagulant concentration were 4.0 and 2000mg/L, respectively. Through this process, 52.6% of CODcr was removed. The second process was $UV-TiO_{2}$ photocatalytic reaction. The optimum operation conditions for the system were as follows: UV lamp wavelength, 254 nm; wastewater temperature, $40^{\circ}C$; pH 8.0; and air flow rate, 40L/min, respectively. Through the above two combined processes, 69.7% of T-N and 70.9% of CODcr contained in the wastewater were removed.

• Journal of Korean Society of Environmental Engineers
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• v.30 no.10
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• pp.1047-1053
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• 2008

This study was to evaluate the optimum conditions for chemical coagulation to remove color from the effluent of a piggery wastewater treatment process. The DOC concentration in the effluent was about 227.3 mg/L, color was 2,430 CU, turbidity was 22.1 NTU, and UV$_{254}$-absorbance was 3.7 cm$^{-1}$. The fractions of hydrophobic, transphilic, and hydrophilic substance of the effluent was about 55.3%, 17.4%, 27.3% respectively. Also, molecular weight cut-off(MWCO) of below 0.5 K, 0.5 K to 1 K, 1 K to 10 K, 10 K to 30 K, and over 30 K were 74.2%, 7.3%, 5.5%, 7.1%, and 5.9% respectively. SCD(streaming current Detector) was used to find out the optimum pH values and coagulant dosages. The optimum dosages and pH of Al$^{3+}$ were 5.84 mM and 5.3, while those of Fe$^{3+}$ were 9.25 mM and 5.0, respectively. At optimum conditions of coagulation, color removal efficiencies for aluminium sulfate and ferric chloride were as high as 91.9 and 98.7%, respectively. Chemical coagulation showed good performance to remove color from on biologically treated piggery wastewater.

• Korean Journal of Food Science and Technology
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• v.48 no.4
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• pp.341-346
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• 2016

The AMY2B gene, encoding human pancreatic ${\alpha}$-amylase isozyme (HPA II), was expressed in Pichia pastoris, and the effects of chloride ions on HPA II activity toward starch substrates were investigated. As seen with chloride ion-dependent ${\alpha}$-amylases-including HPA I, the isozyme of HPA II-chloride ions increased enzyme activity and shifted the optimal pH to an alkaline pH. The activity enhancement by chloride was more significant at pH 8 than that at pH 6, suggesting that the protonation state of the general acid/base catalyst of HPA II was important for the hydrolysis of starches at an alkaline pH because of the increase in its $pK_a$ by chloride ions. The turnover values for cereal starches as the substrates markedly increased in the presence of chloride by up to 7.2-fold, whereas that for soluble starch increased by only 1.7-fold. Chloride inhibited substrate hydrolysis at high substrate concentrations, with $K_i$ values ranging from 6 to 15 mg/mL.

• Microbiology and Biotechnology Letters
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• v.9 no.1
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• pp.35-44
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• 1981

Whole cell penicillin amidase of Escherichia coli was immobilized by entrapment in gelatin followed by extrusion and crosslinking with glutaraldehyde. The immobilized engyme preparation demonstrated the recovery yield of activity up to 70% and good stability during storage and operation. The half life of activity decay during the operation was estimated to be about 50 days. The optimum pH and temperature for both of immobilized and soluble enzyme are 8.5 and 5$0^{\circ}C$, respectively. No significant change was demonstrated in the effect of pH and temperature, but the increase in heat stability at high temperature was observed in the case of the immobilized enzyme. It was found that the plug flow reactor could be operated favorably since the pH drop along the column path due to tile reaction product was minimized by employing substrate solution with moderate buffer strength. The optimal condition of reactor operation was discussed with regard to the effect of substrate concentration and the residence time on the conversion efficiency and productivity.

• Microbiology and Biotechnology Letters
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• v.30 no.3
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• pp.210-215
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• 2002

A bacterium degrading soy protein was isolated from Korean traditional fermented foods. The isolated strain was identified as Bacillus subtilis, and named as B. subtilis EB464. The optimum pH and temperature of the protease produced by 5. subtilis EB464 were pH 9.0 and $50^{\circ}C$, respectively. The protease was stable in the range of pH 6~10 and below $40^{\circ}C$. The content of water-soluble protein and free amino acid of the medium were increased from 4.2% to 20.6% and ken 1.9% to 22.0%, respectively, by solid-state fermentation of soybean meal with B. subtilis EB464 for 72 h.

• Food Science and Preservation
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• v.21 no.3
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• pp.442-450
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• 2014

In this study, we isolated a cellulase-producing bacterium isolated from traditional Korean fermented soybean paste and investigated the effect of culture conditions on the production of cellulase. This bacterium, which was identified as Bacillus subtilis 4-1 through 16S rRNA gene sequence analysis, showed the highest cellulase activity when the cells were grown at $45^{\circ}C$ for 24 hours in the CMC medium supplemented with 1.0% of soluble starch and 0.1% yeast extract. The initial optimum pH of the medium was observed in the range of 5.0~9.0. The optimal pH and temperature for the production of cellulase from B. subtilis 4-1 were pH 9.0 and $60^{\circ}C$ respectively. In addition, the enzyme showed significant activity in the temperature range of $20{\sim}90^{\circ}C$, which indicates that B. subtilis 4-1 cellulase is an alkaline-resistance and thermo-stable enzyme. This enzyme showed higher activity with CMC as the substrate for endo-type cellulase than avicel or pNPG as the exo-type substrates for exo-type cellulase and ${\beta}$-glucosidase. These results suggest that the cellulase produced from B. subtilis 4-1 is a complex enzyme rather than a mono-enzyme.