• Journal of the Korean Applied Science and Technology
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• v.15 no.2
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• pp.77-81
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• 1998

Surface active properties of these aqueous Gemini surfactant solutions including surface tension, critical micelle concentration(cmc), foaming power, foam stability, emulsifying power and Krafft point were measured at given conditions. They showed excellent properties, being compared with conventional single-chain surfactants such as sodium dodecyl sulfonate(SDS). Their surface tensions in the aqueous solutions were decreased to $30{\sim}38$ mN/m, which is lower than 39 mN/m of SDS, and their cmc values evaluated by surface tension method were $2.8{\times}10^{-5}{\sim}3.3{\times}10^{-4}$ mol/L. These values were also much lower than that of SDS, $9.8{\times}10^{-3}$ mol/L. The foaming power and foam stability, especially decyl and dodecyl compounds, were good and the emulsifying power in benzene or soybean oil was also excellent. All of the synthesized Gemini surfactants possessed good water solubility and their Krafft points were all below $0^{\circ}C$. As results, DDED and DDOD, Gemini surfactants which were synthesized are expected to be applied as foamers, emulsifiers and so on.

• Journal of the Korea Furniture Society
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• v.22 no.3
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• pp.174-182
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• 2011

Over the last decade, Sick Building Syndrome has become a significant social issue in Korea and many methods have been considered to maintain comfortable indoor air quality. To reduce toxic substances emitted from wood composite products, the source control is an efficient method through the reduction of formaldehyde content by using natural material-based adhesives for composite wood products production. Among alternative materials, soybean protein is considered an appropriate natural material to replace formaldehyde-based resin and many efforts have been made to produce new products, such as soap, shampoo, ink, resin, adhesive and textile through changing the chemical or physical properties of soybean. To process soybeans into these useful products, the beans are dehulled and the oil is removed by crushing at very high pressure or by solvent extraction. For use soybean as an adhesive, it is processed at temperatures below $70^{\circ}C$ to preserve the alkaline solubility of the proteins. In addition, soybean-based adhesive is undergone treatment process to improve mechanical properties using urea, urease inhibitor N-(n-butyl) thiophosphoric triamide and sodium dodecyl sulfate. The modified soybean-based adhesive exhibited sufficient mechanical properties to use as an adhesive for composite wood products. This paper is a review article to discuss the possibilities of soybean-based adhesive for environment-friendly furniture materials.

• Food Science and Biotechnology
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• v.18 no.3
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• pp.782-787
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• 2009

In prion disease, spongiform neurodegeneration is preceded by earlier synaptic dysfunction. There is evidence that soluble N-ethylmaleimide sensitive factor attachment receptor (SNARE) complex formation is reduced in scrapie-infected in vivo models, which might explain this synaptic dysfunction because SNARE complex plays a crucial role in neuroexocytosis. In the present study, however, it is shown that prion protein (PrP) does not interfere with SNARE complex formation of 3 SNARE proteins: syntaxin 1a, SNAP-25, and synaptobrevin. Sodium dodecyl sulfate-resistant complex formation, SNAREdriven membrane fusion, and neuroexocytosis of PC12 cells were not altered by PrP. Thus, PrP does not alter synaptic function by directly interfering with SNARE complex formation.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.34 no.2
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• pp.120-126
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• 1989

This experiment was carried out to investigate the lectin of soybean (Glycine max L.) seed. Purification was done by 50-80% ammonium sulfate precipitation, CM-cellulose and Sephadex G-100 column. The purity was ascertained by electrophoresis. The molecular weight of purified lectin was estimated as 132,000. It was composed of three subunits which molecular weight was 45,000. The lectin was identified as glycoprotein by Schiff's reagent staining and Dubois method. The lectin agglutinated erythrocytes of rabbit and human. The amounts of the lectin to agglutinate human erythrocytes differed among the blood types: The blood type A required the least amount, the next was B, O, and AB in order. The agglutination was specifically inhibited by 5${\mu}$g/ml of N -acetyl.-D-galactoseamine and 200${\mu}$g/ml of D-galactose. Other tested sugars could not inhibit the agglutination of the erythrocytes by the lectin.

• Korean Chemical Engineering Research
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• v.50 no.5
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• pp.789-794
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• 2012

For the purpose of development of the latex suitable for polymer cement mortar, experiments on the preparation of carboxylated styrene butadiene latex by the method of the two-step emulsion polymerization were performed. Methyl methacrylate, methacrylic acid and acrylic acid were selected as carboxylic co-monomer, styrene and butadiene as monomer, sodium dodecylbenzene sulfonate and sodium salt of lauryl sulfonate as anionic emulsifiers, and nonylphenoxy poly (ethyleneoxy) ethanol (n=10, 20, 40) as latex stabilizer. Potassium persulfate and sodium bisulfite were also used as redox initiator, and sodium monohydrogen phosphate and potassium carbonate as electrolytes. The effects of categories and concentration of carboxylic co-monomer, molecular weight control agent, crosslinking agent, and styrene/butadiene monomer ratio on the characteristics of latex were investigated. Polymerization recipes for preparation of polymer cement mortar could be proposed. The prepared latexes were tested for the physical properties such as compressive and flexural strength when latexes were mixed with cement mortar. The results showed that the latex could be adapted to polymer cement mortar. Also, it was recognized that the compressive and flexural strength were exhibited 25.4% and 45.3% respectively higher improvement than the quality standards at 28 days curing time.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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• 2001.04a
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• pp.18-25
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• 2001

A new wood-degrading fungus Trichophyton rubrum LKY-7 secretes a high level of laccase in a glucose-peptone liquid medium. The production of laccase by the fungus was barely induced by 2,5-xylidine. The laccase has been purified to homogeneity through three chromatography steps in an overall yield of 40%. The molecular mass of the purified laccase was about 65 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified laccase had the distinct blue color and had basic spectroscopic features of a typical blue laccase: two absorption maxima at 278 and 610 nm and a shoulder at 338 nm. The N-terminus of the laccase has been sequenced, revealing high homology to laccases from wood-degrading white-rot fungi such as Ceriporiopsis subvermispora. The enzyme had a "low" redox potential (0.5 V vs normal hydrogen electrode), yet it was one of the most active laccases in oxidizing a series of representative substrates/mediators. Compared with other fungal laccases, the laccase has a very low Km value with ABTS [2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid] as a substrate and a very high Km value with violuric acid as a substrate. The laccase has the isoelectric point of 4.0. The laccase had very acidic optimal pH values (pH 3-4) while it was more stable at neutral pH than at acidic pH. The laccase oxidized hydroquinone faster than catechol and pyrogallol. The oxidation of tyrosine by the laccase was not detectable under the reaction conditions. The laccase was strongly inhibited by sodium azide and sodium fluoride. fluoride.

• Food Science of Animal Resources
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• v.34 no.5
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• pp.656-664
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• 2014

The purpose of this study was to analyze myosin heavy chain (MHC) isoforms in bovine longissimus thoracis (LT) muscle by liquid chromatography (LC) and mass spectrometry (MS). LT muscles taken from Hanwoo (Korean native cattle) steer (n=3) used to separate myosin bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The peptide queries were obtained from the myosin bands by LC-MS/MS analysis following in-gel digestion with trypsin. A total of 33 and 43 queries were identified as common and unique peptides, respectively, of MHC isoforms (individual ions scores >43 indicate identity or extensive homology, p<0.05). MHC-1 (IIx), -2 (IIa), -4 (IIb), and -7 (slow/I) were identified based on the Mowse score (5118, 3951, 2526, and 2541 for MHC-1, -2, -4, and -7, respectively). However, more analysis is needed to confirm the expression of MHC-4 in bovine LT muscle because any query identified as a unique peptide of MHC-4 was not found. The queries that were identified as unique peptides could be used as peptide markers to confirm MHC-1 (14 queries), -2 (8 queries), and -7 (21 queries) in bovine LT muscle; no query identified as a unique peptide of MHC-4 was found. LC-MS/MS analysis is a useful approach to study MHC isoforms at the protein level.

• Food Science of Animal Resources
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• v.38 no.5
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• pp.1101-1108
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• 2018

The aim of this study was to investigate the effects of dry-aging (DA) and the cooking process on the myofibril protein functionalities and in vitro digestibility of proteins in beef loin. Six sirloins from beef were dry-aged for 28 d, and the control group (n=6) was analyzed 2 d postmortem for this study. Dimensional changes (reduction of thickness and surface shrinkage) after cooking were significantly greater in the control group than the DA group, whereas the shear force of the DA group was significantly lower than that of the control. Effect of cooking on aggregation, hydrophobicity, and in vitro digestibility were significantly higher in the DA group than in the control. After cooking, the protein in DA sirloins was more oxidized than in the control samples. According to the sodium dodecyl sulfate-polyacrylamide gel electrophoresis result, the low molecular weight bands (below 17 kDa) increased in the DA group, finding that the protein characteristics of dry-aged beef was affected by cooking.

• Journal of Microbiology and Biotechnology
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• v.4 no.1
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• pp.41-48
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• 1994

The xylanase from alkali-tolerant Bacillus sp. YA-14 was purified to homogeneity by CM-cellulose, Sephadex G-50, and hydroxyapatite column chromatographies. The molecular weight of the purified enzyme was estimated to be 20, 000 Da by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified enzyme slightly hydrolyzed carboxymethyl cellulose and Avicel, but did not hydrolyze soluble starch, dextran, pullulan, and ${\rho}-nitrophenyl-{\beta}$-D-xylopyranoside. The maximum degree of hydrolysis by enzyme for birchwood xylan and oat spelts xylan were 47 and 40%, respectively. The Michaelis constants for birchwood xylan and oat spelts xylan were calculated to be 3.03 mg/ml and 5.0 mg/ml, respectively. The activity of the xylanase was inhibited reversibly by $HgCl_2$, and showed competitive inhibition by N-bromosuccinimide, which probably indicates the involvement of tryptophan residue in the active center of the enzyme. The Xylanase was identified to be xylose-producing endo-type xylanase and did not show the enzymatic activities which cleave the branch point of the xylan structure.

• Journal of Plant Biology
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• v.38 no.3
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• pp.251-258
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• 1995

The soluble acid invertase ($\beta$-D-fructofuranoside fructohydrolase, EC 3.2.1.26) was isolated and characterized from the hypocotyls of mung bean (Phaseolus radiatus L.). The enzyme was purified to apparent homogeneity by consecutive step using diethylaminoethyl (DEAE)-cellulose anion exchange, Concanavalin (Con) A affinity and Sephacryl S-300 chromatography. The overall purification was about 148-fold with a yield of about 15%. The finally purified enzyme exhibited a specific activity of about 139 $\mu$mol of glucose produced mg-1 protein min-1 at pH 5.0 and appeared to be a single protein by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and nondenaturing PAGE. The enzyme had the native molecular weight of 70 kD and subunit molecular weight of 70 kD as estimated by Sephadex G-200 chromatography and SDS-PAGE, respectively, suggesting that the enzyme was composed of a monomeric protein. On the other hand, the enzyme appeared to be a glycoprotein containing N-linked high mannose oligosaccharide chain on the basis of its ability to bind to the immobilized C on A. The enzyme had a Km for sucrose of 1.8 mM at pH 5.0 and maximum activity around pH 5.0. The enzyme showed highest enzyme activity with sucrose as substrate, but the activity was slightly measured with raffinose and cellobise. No activity was measured with maltose and lactose. These results indicate the soluble acid invertase is a $\beta$-fructofuranosidase.