• Advances in Traditional Medicine
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• v.4 no.4
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• pp.227-234
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• 2004

An ${\alpha}-Amylase$ was purified to apparent homogeneity from germinating soybean seeds (Glycine max). Enzyme showed high specificity for starch. ${\alpha}-Amylase$ from soybean has optimum pH at 7.6 in the pH range 4.0-10.6. At this pH, the $K_m$ of starch was 2.63 mg/ml and the $V_{max}$ was equal to 52.6 mg/ml/min protein. Optimum temperature of the enzyme was found to be $55^{\circ}C,\;Q_{10}$ equal to 1.85 and energy of activation equal to 12 kcal/mol. Additives like, EDTA reduced the activity of ${\alpha}-amylase$ whereas PMSF enhanced the activity. ${\alpha}-Amylase$ was inhibited by several heavy metal ions.

• Journal of Ginseng Research
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• v.7 no.1
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• pp.88-93
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• 1983

Studies were carried out to elucidate the protein stabilizing effect of ginseng. Malate dehydrogenase (EC 1.1.1.37) was used as a protein and the rate constant of the enzyme inactivation was determined under the heat denaturation condition. There was an optimum pH for the enzyme stability, the rate constant of the enzyme inactivation was minimum at BH 8.8. The rate constant was increased at lower and higher pH regions than the optimum pH. The inactivation reaction followed the Arrehnius law and the activation energy was measured as 36.8kcal/mole. The reaction rate was not affected by the enzyme concentration and thus it was assumed to be unimolecular first order reaction. The water extract of red ginseng decreased the rate constant of Malate dehydrogenate under heat inactivation condition to stabilize the enzyme activity. Purified ginseng saponin also stabilized the enzyme against heat inactivation.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.33 no.5
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• pp.25-29
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• 2001

Dimethyldioxirane (DMD), which is a source of active oxygen, is effective agent that can be used in chemical pulp bleaching. In this study, delignification of kraft bagasse pulp has been carried out by using DMD. The effect of the applied charge of DMD (as active oxygen) and pH of the delignification medium were studied. The optimum conditions of the applied DMD charge and pH of the delignification reaction were achieved at pH range from 8~9, 2% of DMD (as active oxygen) and the rest of delignification reaction conditions were $25^{\circ}C$, 60 min, and 12% pulp consistency. The development of brightness per unit kappa number removal (ΔBrightness/ Δ Kappa number) has highest value at the optimum condition. The study showed that the reactivity of kraft bagasse pulp be enhanced to wards alkaline hydrogen peroxide bleaching by pulp treatment with DMD.

• The Korean Journal of Mycology
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• v.9 no.3
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• pp.129-132
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• 1981

Thle experiments were carried out to select the highest yield and good quality of the oyster mushroom (Pleurotus sp.) strain for brooding material sources. The strains used covered 6 from 4 countries, No. 2063, 2078 and 2093 were collected from Korea, No. 2068 introduced from Japan, No. 2091 from Germany and No. 2095 from Taiwan. Some characteristics of the strains are as follows. 1) The optimum temperature for strains, 2091, 2093 and 2063 of P. ostreatus was $30^{\circ}C$, it ranged from 25 to $30^{\circ}C$ for the others. 2) The optimum moisture content were 70% for strain 2068, 80% for strains 2093, 2095 and 2091, 75% for other strains. 3) The optimum pH of the mycelial growth were at pH 6.0 for strains 2093 and 2068, pH 6.0 and pH 8.0 for other strains. 4) The days from spawning to budding was the shortest in strain 2095 and the yield was the highest in 2091, $64.4kg/3.3m^2$on the rice straw cultivation.

• Korean Journal of Microbiology
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• v.30 no.4
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• pp.305-309
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• 1992

Cytosine deaminase (EC 3.5.4.1) from BaciNus stc~urorhermophilus was partially purified 7.2-fold with an overall yield of 52.7%. The partially purified enzyme deiiminated cytosine only.but not 5-methylcytosine and 5-fluorocytosine. The apparent Michaclis constant. Km valuefor cytosine was 5.9 mM. The enzyme was relatively stable in the range of pH 4.0 to 7.0.furthermore extremely thermo-stable : more than 75'X) of the activity was remained afterheating at 80$^{\circ}$C for I0 min at pH 6.5. The enzyme had a pH optimum at around pH7.0 to 7.5. and temperature optimum at 35 to 31$^{\circ}$C. And the activation energ (En value)determined from an Arrhenius plot was 26 Kcal/mol. The enzyme activity was stronglyinhibited by heavy metal ions such as Cd", Hg". Cut' at 1 mM, anJ by o-phenanthroline,and p-chloromcrcuribcnzoate at I mM. But the enrymc activity was activatetl increased byGMP, and CMP at 1 mM.ased by GMP, and CMP at 1 mM.

• Proceedings of the Korean Institute of Resources Recycling Conference
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• 2003.10a
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• pp.122-128
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• 2003

To develop a Mg-Zeolite for simultaneous recovery of the N and the P from sewage water, the natural zeolite was treated with 20% $MgCl_2$ solution by changing the pH the temperature and the treating time of the solution. And the contents of Ca Fe Na K Mg of Mg-Zeolite were analyzed by ICP. The optimum treatment condition for Mg-Zeolite was induced to pH 7.0 $50^{\circ}C$ in 20% $MgCl_2$ solution and for 80min treatment. And the Na and the K ions in natural zeolite are significant factors for Mg exchange in the zeolite.

• Journal of Industrial Technology
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• v.29 no.A
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• pp.169-176
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• 2009

The gene encoding endoxylanase (xylS) was isolated from a genomic library of Bacillus licheniformis NBL420. Two positive clones, which harbor 1.5 kb and 0.8 kb inserts respectively, were screened on RBB dyed-xylan plates and the recombinant plasmids were named as pBX3 and pBX5. The nucleotide sequencings of two inserts revealed the existence of common 639 bp of open reading frame which encode 232 amino acids. The xylS gene was successfully subcloned into pET22b(+) vector and overexpressed. Enzymatic properties including optimum pH, optimum temp, thermostability and pH stability were investigated. Activity staining of XylS was identical with that of original Bacillus licheniformis NBL420.

• The Research Journal of the Costume Culture
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• v.7 no.2
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• pp.315-322
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• 1999

The acquistion and dyeability of the Gardenia jasminoides were examined to establish the optimum condition for extraction and storage in the process of obtaining the natural dye, Gardenia jasminoides colorant. Also the dyeability and colorfastness of Gardenia jasminoides were investigated. The results of this study are as follows. The optimum part-removed seed. In all experiments, the part of fat-removed seed and pericarp was used. The optimum condition for extraction of Gardenia jasminoides colorant was at 40℃ and for 90 min. in methanol. As storage temperature was higher, the absorbance of colorant extract decreased rapidly. The Gardenia jasminoides colorant exhibited dyeability to cotton, silk, wool, and nylon. The dyeability was the greatest in wool, and then nylon, silk, and cotton. Both wool and nylon had the greatest K/S value at pH3, however, nylon and cotton at pH 6 and pH 8 respectively. In addition, the increase in K/S value corresponded to temperature in wool and nylon, but the silk and cotton had the greatest K/S value at 60℃. Also, the K/S value increased in concomitant with the increased number of dyeing repetition. In the most cases, colorfastness of light was weak but colorfastness of laundry, sweat was relatively excellent.

• Journal of Mushroom
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• v.2 no.4
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• pp.214-217
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• 2004

This study was carried out to investigate the physiological charateristics of F. pinicola in sawdust media. The optimum temperature in sawdust media was $30^{\circ}C$ in of F. pinicola. The optimum pH was 5 in F. pinicola. Mycelial growth and density of F. pinicola was quite good when birch tree and oak sawdust, respectively were used as cultural substrates. The best mycelial growth in F. pinicola was observed when beer waste was added as supplement on sawdust substrates. The optimum supplement ratios of beer waste and a magnecium sulfate were 20%, and 0.1% respectively. However, optimun supplement ratios of a calcium oxide and a LVD were different as 0.1% in F. pinicola.

• Journal of Life Science
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• v.8 no.4
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• pp.387-394
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• 1998

A thermophilic bacterium (strain DG0303) producing a thermostable $\alpha$-glucosidase was isolated from manure and identified as Bacillus sp. Strain DG0303 produced high level of $\alpha$-glucosidase compared with other thermophilic Bacillus strains. The cellular protein patterns were also compared with other Bacillus strains by sodium dodecyl sulfatepolyacrylamide gel electrophoresis(SDS-PAGE). On the basis of 16S rDNA analysis the Bacillus sp. DG0303 was found to be a member of Bacillus rDNA group 5. The optimum temperature for growth was 65$\circ$C and no growth was obtained at 40$\circ$C or 75$\circ$C. The optimum pH for growth was 5.5 to 8.5. $\alpha$-glucosidase activity was produced during growth and most activity was detected in the culture supernatant. The $\alpha$-glucosidase production was constitutive in the absence of carbohydrates. High level of enzyme activity was detected when the culture was grown on medium containing starch. Addition of glucose resulted in the repression of the $\alpha$-glucosidase production. The optimum pH and tempoerature for enzyme activity were pH 5.0 and 65$\circ$C, respectively. When analyzed by zymogram, the culture supernatant showed a single $\alpha$-glucosidase band with a molecular weight of approximately 60,000.