• Korean Journal of Food Science and Technology
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• v.23 no.4
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• pp.400-404
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• 1991

Protease was purified from Aspergillus niger propagated on katsuobushi. The optimal pH and temperature of the enzyme were 7.2 and $45^{\circ}C$, respectively. The enzyme was stable at $pH\;5{\sim}8$ and at below $40^{\circ}C$. Enzyme activity was promoted by $K^{-}\;and\;Fe^{2+}$, whereas it was inhibited by $Hg^{2},\;Zn^{2},\;Mn^{2}\;and\;Cd^{2}$. The acidic, basic and neutral amino acid compositions were found to be 22.63, 13.57 and 63.80%, respectively. The content of nonpolar, poler and sulfur-containing amino acids were 39.72, 20.03 and 9.53% respectively, and aspartic and glutamic acids were abundant. The molecular weight was 42,000 and isoelectric point was estimated pH 5.6.

• Journal of the Korean Electrochemical Society
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• v.15 no.2
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• pp.83-89
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• 2012

We investigate the electrocatalytic activities for oxygen reduction at nanoporous gold (NPG) surfaces fabricated by selective dissolution of Ag from electrodeposited Ag-Au layers on electrode surfaces. The structure of NPG was controlled by changing the concentration ratios of precursor metal complexes during the electrodeposition of Ag-Au layers and the corresponding surface morphology and surface area was examined. NPG structures with Ag/Au ratio of 2.0 exhibited the highest electrocatalytic activity for oxygen reduction, where the nanoporous structure plays a key role, but the surface area does not affect on the electrocatalytic activity. The mechanism of electroreduction of oxygen was investigated by rotating disk electrode techniques. In acidic media, oxygen was first reduced to hydrogen peroxide followed by further reduction to water through 2-step 4-electron mechanism, whereas the oxygen was reduced directly to water by 4-electron mechanism in basic media.

• Membrane Journal
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• v.17 no.1
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• pp.67-79
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• 2007

Uniform microcapsules containing ionic model drugs were prepared by controlling various conditions of emulsification procedure using a lab-scale membrane emulsification system with a SPG (Shirasu porous glass) tubular membrane. We observed the effects of various emulsification parameters [concentration and molecular weight of polycaprolatone (PCL) polymer, transmembrane pressure and emulsifier concentration in disperse phase and continuous phase, stirring speed] on the mean size and size ditribution of microcapsules containing lidocaine hydrochloride (cationic drug), sodium salicylate (nonionic drug) and 4-acetaminophen (anionic drug) used as a model drugs. Also, release characteristics of a model drugs from PCL microcapsules were investigated. Controlling membrane emulsification parameters, uniform PCL microcapsules with about $5\;{\mu}m$ of the mean size were finally prepared. The release rate and the burst effect of microcapsules were decreased in condition of the acidic solution, but it was increased in condition of the base solution.

• Journal of Applied Biological Chemistry
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• v.53 no.3
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• pp.132-138
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• 2010

A gene encoding a putative alanine racemase in B. pseudomycoides was cloned and expressed in Escherichia coli BL21(DE3) using a pET-21 vector harbouring 6xHistidine tag. Affinity purification of the recombinant alanine racemase with a nickel resin resulted in one band by SDS-PAGE analysis. The purified enzyme showed a molecular weight of 46 kDa. The enzyme was the most active toward L-alanine and secondly D-alanine, implying that the enzyme is an alanine racemase. D-cysteine significantly inhibited the enzyme activity and also L-cysteine to a lesser extent. The enzyme was considerably activated by addition of pyridoxal-5'-phosphate (PLP), showing that 73% increase in activity was observed at 0.3 mM, compared to control. The enzyme was the most active at pH 9.0 and more stable at alkaline pHs than acidic pHs.

• Korean Journal of Microbiology
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• v.40 no.2
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• pp.139-146
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• 2004

A bacterium producing alkaline cellulase was isolated from soil, leaf mold and compost, and was identified as alkalophilic Bacillus sp. HSH-810 by morphological, cultural and biochemical determination. The optimum cul-ture condition of Bacillus sp. HSH-810 for the growth and alkaline cellulase production was $30^{\circ}C$ and pH 10.0. The maximum alkaline cellulase production was obtained when 1.0%(w/v) CMC, 0.5%(w/v) peptone, 0.02%(w/v) $CaCl_2$ and 0.02(w/v) $CoCl_2$ were used as carbon source, nitrogen source and mineral source, respectively. The optimum pH and temperature of the enzyme activity were pH 10.5 and $50^{\circ}C$, respectively. This enzyme was fairly stable in the pH range of 6.0-13.0 and at $50^{\circ}C$. For the effect of surfactants, the activity of alkaline cellulase was stable in the presence of sodium-$\alpha$-olefin sulfonate (AOS), sodium dodecyl sulfonate (SDS), Tween 20 and Tween 80, but inhibited by the presence of 0.1 linear alkyl-benzene sulfonate (LAS) sig-nificantly.

• Microbiology and Biotechnology Letters
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• v.28 no.2
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• pp.111-116
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• 2000

Cultural conditions for the production of water-soluble pigment from mycelial culture of Cordyceps scarabaeicola KEFC-C252 and antimutagenic activity of the pigment were investigated. To obtain the maximum productivity of the pigment from mycelial culture of C. scarabaeicola KEFC-C252, the optimized medium was made with 1.5% sucrose, 2.5% yeast extract and initial pH 5.5. C. scarabaeicola KEFC-C252 was cultivated to reach the maximum concentration of the pigment at $26^{\circ}C$ for 108 hrs. C. scarabaeicola KEFC-C252 produced about 1.2 g/liter pigment under the optimized condition. The pigment was isolated from the culture filtrate by ethylacetate extraction, acidic precipitation and crystallization. The isolated pigment was scarlet hexagonal column crystal, and the color of the pigment was changed according to pH of the solution. The pigment showed violet in the alkaline water but showed red color in the acidic water. The pigment showed inhibitory activity against mutagenic activity induced by 4-nitroquinoline N-oxide. Furthermore, the pigment showed inhibitory activity against spontaneous mutation on Salmonella typhimurium TA98 and TAlOO.

• Journal of the Korea Organic Resources Recycling Association
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• v.8 no.2
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• pp.71-76
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• 2000

The biological carbon dioxide fixation using microalgae has been known as an effective carbon dioxide reduction technology. With many environmental factors influencing microalgal productivity, the desirable cultivation factors were investigated using a green alga, Euglena gracilis. It has the high protein and vitamin E to be used as fodder. In batch culture with a photobioreactor, initial pH, temperature, carbon dioxide concentration and light intensity in the optimum cultivation condition were 3.5, $27^{\circ}C$,5-10% and $520{\mu}mol/m^2/s$, respectively. After that, the optimum hydraulic retention time (HRT for the continuous cultivation was 4 days at carbon dioxide concentration of 10%. In this condition, the final dry cell weight was 1.2g/l.

• Microbiology and Biotechnology Letters
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• v.14 no.6
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• pp.455-460
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• 1986

Dane particle was prepared from the plasma of chronic HBsAg carrier with high levels of HBsAg activity. DNA extracted front Dane particle core after a DNA polymerase reaction with $\alpha$-($^{32}$P) dNTP, was identified as HBV DNA by liquid scintillation counter and agarose gel electrophoresis-G.M. counting. To produce Hepatitis B surface antigen for use as a vaccine against Hepatitis B virus infection, yeast strains harboring recombinant plasmid with Apase promoter was used. Recombinant plasmid was construced from pHBV 130 and pAN 82, transformed into E coli, and then transferred into yeast strains. HBsAg was produced by derepression in Burkholder minimal medium with controlled inorganic phosphate concentration. The kinetics of HBsAg production was also investigated. Total HBsAg activity increased rapidly between 3 and 6 hours after transfer to phosphate-free medium and reached a maximum at around 9th hour. The transfer into phosphate-free medium after 6 hours in high phosphate cell growth medium gave maximum activity.

• Food Science and Preservation
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• v.12 no.5
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• pp.489-495
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• 2005

Polyphenol oxidase (PPO) from Burdock (Arctium lappa L.) was purified and characterized. Purification of polyphenol oxidase was achieved by ammonium sulfate precipitation, Phenyl-sepharose CL-4B hydrophobic chromatography and Sephadex G-100 gel filtration chromatography. The molecular mass of the purified PPO was estimated to be 30 kDa by SDS polyacrylamide gel electrophoresis. In a substrate specificity, maximum activity was achieved with chlorogenic acid, followed by catechol and catechin. Whereas, there was low activity with hydroquinic acid, resorcinol or tyrosine. The optimum pH and temperature for enzyme activity were 7.0 and 35$\circC$ with catechol, respectively. The enzyme was most stable at pH 7.0 while unstable at acidic and alkaline pH. The enzyme was stable when heated to 40$\circC$. But heating at 50$\circC$ for more than 30 min caused 50% loss of activity. Ascorbic acid, L-cystein and $Cu^{2+}$ inhibited the activity of pholyphenol oxidase.

• KSBB Journal
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• v.15 no.1
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• pp.66-71
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• 2000

The results for decolorization of various dyes by Geotrichum candidum (KCTC 6195) showed that optimal initial pH, temperature and glucose concentration were 6, $30^{\circ}C$, and 30g/L. Light had no effect on the cell growth and decolorization efficiency. All the dyes - dispersive dyes, acid dyes and reactive dyes - used on the solid medium were also decolorized in a liquid medium, although the decolorizing rates varies depending on the dye structure. An energy source was essential for cell growth or decolorization because textile dyes did not support growth. The percentage of decolorization of Acid orange 10 was shown to be 91% for initial conc. 100ppm and 84% for initial conc. 500ppm. The biomass could adsorb the dyes such as Acid red 1;19.8%, Acid red 88; 73%, Acid orange 10; 12.1% Reactive blue 19; 14.6%. The dye removal was due to the sorption of dye to the fungal biomass as well as some extracellular enzymes. Color removal was enhanced up to 97% within 3 days by the addition of glucose after 2 days incubation.