• The Transactions of the Korean Institute of Electrical Engineers P
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• v.62 no.4
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• pp.223-226
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• 2013

In this study, we investigated the electro-optical(EO) characteristic of fringe-field switching(FFS) mode cell by the two kinds of ultraviolet(UV) alignment method on the organic thin film(polyimide: PI). The suitable organic layersfor FFS cell and the aligning capabilities of nematic liquid crystal(NLC) using the in-situ photoalignment method were studied Disclination is observed after conventional photoalignment method for 1h, and in-situ photoalignment method for 1h. Monodomain alignment of the NLC can be observed via in-situ photoalignment method for 2h and 3h. It is considered that NLC alignment is due to photo-depolymerization of the polymer with oblique non-polarized UV irradiation on PI surface. An unstable V-T curve of UV-aligned FFS-LCD with conventional photoalignment method can be achieved. However, a stable V-T curve of UV-aligned FFS-LCD with in-situ photoalignment method(1h), and V-T curve of UV-aligned FFS-LCD with in-situphotoalignment method was much stable comparing with that of other UV-aligned FFS-LCD's. As a result, more stable EO performanceof UV-aligned FFS-LCD with in-situphotoalignment method for 3h is obtained than that of the other UV-aligned FFS-LCD's.

• Korean Journal of Poultry Science
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• v.16 no.1
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• pp.17-22
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• 1989

In order to dull heat sensitivity of egg albumen, metal ions (aluminium, ferric, ferrous, copper) were added and functional properties or egg albumen were determined before and after heat treatment at $60^{\circ}C$ for 5 minutes. Effect of pH on heat sensitivity of aluminium salt added egg albumen was also determined. Addition of metal ions increased turbidity of egg albumen before and after the heat treatment. Changes of the turbidity were minimized by addition of aluminium salt. The foaming power was markedly increased by addition of ferric salt before the heat treatment and increased by addition of aluminium, ferric and copper salt after the heat treatment. Before the heat treatment the foam was stable by addition of ferric and ferrous salt but after the heat treatment it was stable by addition of aluminium and ferric salt. The turbidity and foaming property of the egg albumen with aluminium salt were not largely changed after the heat treatment at pH range 7 to 8.5. Over pH 9 the turbidity and foaming power were not decreased, but the foam stability was increased before and after the heat treatment. Salmonella typhimurium ATCC 14028 (10$^{6}$ cells/$m\ell$) inoculated in egg albumen at pH range 7 to 8.5 was destructed by the heat treatment.

• Microbiology and Biotechnology Letters
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• v.15 no.5
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• pp.306-311
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• 1987

After series of purification by means of ammonium sulfate fractionation, the 1st and 2nd DEAE-Cellulose, DEAE-Sephadex A-50, and Sephacryl S-200 superfine gel filtration, the activity of extracellular adenine deaminase from Streptomyces sp. J-350P increased 1764 fold and the yield was 0.3% of original activity. The enzyme was stable at the pH range 6.5 to 8.5 and at up to 5$0^{\circ}C$. The optimum pH and temperature of the enzyme were around 6.5 and 35$^{\circ}C$. The molecular weight ol the enzyme was estimated as 36, 000 by calibrated Sephacryl S-200 superfine column chromatography.

• Biotechnology and Bioprocess Engineering:BBE
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• v.3 no.2
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• pp.67-70
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• 1998

In order to understand the influence of ferroxidase center on the protein assembly and solubility of tadpole ferrin, three mutant plasmids, pTH58K, pTH61G, and pTHKG were constructed with the aid of site-directed mutagenesis and mutant proteins were produced in Eshcerichia coli. Mutant ferritin H-subunits produced by the cells carrying plasmids pTH58K and pTHKG were active soluble proteins, whereas the mutant obtained from the plasmid pTH61G was soluble only under osmotic stress in the presence obtained from the plasmid pTH61G was soluble only under osmotic stress in the presence of sorbitol and betaine. Especially, the cells carrying pTH61G together with the plasmid pGroESL harboring the molecular chaperone genes produced soluble ferritin. The mutant ferritin H-subunits were all assembled into ferritin-like holoproteins. These mutant ferritns were capable of forming stable iron cores, which means the mutants are able to accumulate iron with such modified ferroxidase sites. Further functional analysis was also made on the individual amino acid residues of ferroxidase center.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.19 no.6
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• pp.521-528
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• 1986

In this paper, proteolytic activity of the tissue extracts from the internal organs such as alimentary canal, pancreas, pyloric caeca, stomach, liver and spleen of mackerel, Scomber japonicus, and sardine, Sardinops melanosticta, was compared with each other under the optimum reaction condition. The proteinases distributed in alimentary canal, pancreas, pyloric caeca and spleen were active in alkaline pH range, but those in stomach were shown the activity in acid pH range, furthermore those in liver were exhibited the activity in acid, neutral and alkaline pH range. The proteinases distributed in the internal organs of both fish were stable at the heat treatment of $45^{\circ}C$ for 5 minutes. The proteinases from stomach and pyloric caeca of the two fish and those from pancreas of sardine were less stable than those from any other internal organs of both fish. Whereas the proteinases from spleen and neutral proteinases from liver were shown to be stable by the heat treatment at $55^{\circ}C$ for 5 minutes. The proteinases from pyloric caeca of both fish, and stomach, pancreas and spleen of mackerel were stable during the whole storage days at $5^{\circ}C$, but the other proteinases were slowly inactivated after 14 days of storage. The enzymes were seemed to be more stable in the storage at $-15^{\circ}C$ than at $5^{\circ}C$.

• Journal of Microbiology and Biotechnology
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• v.23 no.6
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• pp.864-871
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• 2013

The recombinant strain P. pastoris GS115-lccC was used to produce laccase with high activity. Factors influencing laccase expression, such as pH, methanol concentration, copper concentration, peptone concentration, shaker rotate speed, and medium volume were investigated. Under the optimal conditions, laccase activity reached 12,344 U/L on day 15. The recombinant enzyme was purified by precipitating and dialyzing to electrophoretic homogeneity, and was estimated to have a molecular mass of about 58 kDa. When guaiacol was the substrate, the laccase showed the highest activity at pH 5.0 and was stable when the pH was 4.5~6.0. The optimal temperature for the laccase to oxidize guaiacol was $60^{\circ}C$, but it was not stable at high temperature. The enzyme could remain stable at $30^{\circ}C$ for 5 days. The recombinant laccase was used to degrade chlorpyrifos in several laccase/mediator systems. Among three synthetic mediators (ABTS, HBT, VA) and three natural mediators (vanillin, 2,6-DMP, and guaiacol), vanillin showed the most enhancement on degradation of chlorpyrifos. Both laccase and vanillin were responsible for the degradation of chlorpyrifos. A higher dosage of vanillin may promote a higher level of degradation of chlorpyrifos, and the 2-step addition of vanillin led to 98% chlorpyrifos degradation. The degradation of chlorpyrifos was faster in the L/V system ($k_{obs}$ = 0.151) than that in the buffer solution ($k_{obs}$ = 0.028).

• KSBB Journal
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• v.20 no.5 s.94
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• pp.359-362
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• 2005

Bacillus licheniformis was an useful material for improvement of fecal microflora. The stability of Bacillus licheniformis in low pH (pH 2, 3, 4, 6, 7), artificial bile acid, high concentration of salt (0, 5, 10, 20, $30\%$), and ethanol (0, 4, 8, 16, $32\%$) was investigated in this study. The viability of Bacillus licheniformis was stable for pH 3, 4, 6, 7 Final viability of Bacillus licheniformis was confirmed below $25\%$, in the bile acid. In high concentration of salt, Bacillus licheniformis showed optimal viability in $10\%$ of salt. The viability of Bacillus licheniformis was over $95\%$ in condition of ethanol concentration $4\%,\;8\%,16\%,\;32\%$ contrast with uncontained ethanol at $37^{\circ}C$ for 4h. It was verified that Bacillus licheniformis was stable for pH 4, 6, 7, high concentration of salt and ethanol but was unstable in pH 2 and bile acid.

• The Korean Journal of Food And Nutrition
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• v.8 no.3
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• pp.253-261
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• 1995

A strain of alkalophilic Bacillus sp. C-21 has been Isolated from sold. The strain was capable of producing large amount of cyclodextrin glycosyltransferase (CGTase) in the high alkaline pH medium. The preferable medium composition was determined to be as follows : 1.0% soluble starch, 1.0% peptone, 0.5% yeast extract, 0.1% K2HP04, 0.02% MgSO4.7H2O and 1.0% Na2CO3(pH 10.0) The highest enzyme production was observed after 30hours of cultivation at 33$^{\circ}C$. The optimum temperature and pH for the activity of crude enzyme were 6$0^{\circ}C$ and 6.0, respectively. The enzyme was stable between pH 6.0 and 9.6, and up to 55$^{\circ}C$.

• Microbiology and Biotechnology Letters
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• v.27 no.6
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• pp.466-470
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• 1999

Protease production and its characteristics were investigated with Mucor racemosus f. racemosus PDA 103 which was isolated from Korean traditional meju. Optimum culture conditions of the strain for the production of the protease in basic medium[bean(Baektae):H2O=1:1(w/v)] were as follows: pH 6, 3$0^{\circ}C$ and 72hrs. Optimum pH and temperature for the enzyme activity of the protease produced by Mucor racemosus f. racemosus were pH 5 and 5$0^{\circ}C$, respectively. The enzyme was relatively stable a pH2.0~5.0 and at temperature below 4$0^{\circ}C$. Phenylmethane-sulfonyl fluoride and Ag+ inhibited the enzyme activity. This indicates that the enzyme is serine protease. Km value was 0.9$\times$10-4M and Vmax value was 5.93$\mu\textrm{g}$/min. This enzyme hydrolyzed casein more rapidly than bovine albumin.

• Journal of the Korean Ceramic Society
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• v.29 no.9
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• pp.739-749
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• 1992

The sols prepared by dialyzing solutions, in which the hydrolyzed precipitates of TEOT or directly Ti(OC3H7)4 were resolved, were the nanoparticulate sol with the average particle size less than 7 nm and the anatase crystal phase. In the pH range of 1.5 to 2.9, the particle size of the nanoparticulate TiO2 sols (0.09 mol/ι) increased gradually upto 15 nm~26nm with the increase of pH in the initial aging state but the sols were transparent all the time, and stable without growin any more after 30 days. When the slipcasted porous alumina tubes were coated by the sol-gel dipping method, the minimum particle size and the aging time for forming the coated gel layer at the given pH were optimized. For obtaining the very thin crack-free and reproducible membrane coating, the use of a nanoparticulate TiO2 sol (0.09 mol/ι) aged for about 30 dyas at pH=2.0 was found to be the best.