• Journal of the Korean Society of Food Culture
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• v.9 no.2
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• pp.137-142
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• 1994

Myrosinase in leaf mustard was purified and characterized to furnish a grounding information for utilizing the pungent taste and the potential antimicrobial capability of Dolsan leaf mustard to enhance the taste and storage life of kimchi. When myrosinase was purified from leaf mustard through a series of DEAE Sephadex, chromatofocusing and Con A Sepharose column chromatography, specific activity of the enzyme increased 7107-fold compared with that of crude enzyme preparation, and 18.8% yield was obtained. The purified myrosinase showed the optimum pH of 5.9, isoelectric point of 4.6, molecular weight of 129 kD, Km of 0.206 mM, and Vmax of $2.039\;{\mu}M{\cdot}min^{-1}{\cdot}mg\;protein^{-1}$, respectively. The optimum concentration of L-ascorbic for the maximum activity of the enzyme was 0.6 mM, and the enzyme activity decreased at a higher concentration of L-ascorbic acid than 0.6 mM, showing almost no enzyme activity at a L-ascorbic acid concentration of higher than 2.0 mM. Myrosinase activity in leaf mustard kimchi immediately after the kimchi was formulated was shown to be about 70 nmol/min/mg protein which decreased rapidly after 3 days of storage at $20^{\circ}C$, showing that less than half and almost none of the enzyme activity was retained in 4 and 10 days of storage, respectively.

• Journal of Life Science
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• v.14 no.4
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• pp.636-643
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• 2004

D-Xylose isomerase produced by Lactococcus sp. JK-8, isolated from kimchi, was purified 17-fold of homogeneity, and its physicochemical properties were determined. Although the N-terminal amino acid sequence of D-xylose isomerase was analysed to Ala-Tyr-Phe-Asn-Asp-Ile-Ala-Pro-Ile-Lys, it was not similar to that of Lactobacillus enzyme. The molecular weight of the purified enzyme was estimated to be 180 kDa by gel filtration, 45 kDa by SDS-PAGE and the enzyme was homotetramer. The optimum pH of the enzyme was around 7 and stable between pH 6 and 8. The optimum reaction temperature was 7$0^{\circ}C$ and stable up to 7$0^{\circ}C$ in the presence of 1 mM $Mn^{2+}$. Like other D-xylose isomerases, this enzyme required divalent cation, such as $Mg^{2+}$, $Co^{2+}$, or $Mn^{2+}$ for the activity and thermostability. $Mn^{2+}$was the best activator. Substrate specificity studies showed that this enzyme was highly active on D-xylose. The enzyme had an isoelectric point of 4.8, and fm values for D-xylose was 5.9 mM.

• Korean Journal of Food Science and Technology
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• v.21 no.4
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• pp.542-548
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• 1989

For the selective separation of proteins, the solubilization and desolubilization of proteins in sodium-di-2-ethylhexyl sulfosuccinate (AOT)-isooctane reverse micellar system were investigated. Protein solubilization increased with increasing the concentration of AOT to 200 mM and then decreased above that concentration. Protein was solubilized into reverse micelles in the pH range below the isoelectric Point of each protein, pH 4-10 for lysozyme and pH 5-6 for trypsin and ${\alpha}-chymotrypsin$, Lysozyme, trypsin and ${\alpha}-chymotrypsin$ were efficiently extracted in the precence of KCl and NaCl while larger molecular weight proteins such as pepsin and BSA had high solubilization with $CaCl_2$. At higher ionic strength all proteins exhibited murk less tendency to solubilize and the increase of ionic strength resulted in the decrease of micelle size. Lysozyme was successfully back transfered at pH 12.2 and 1.0M KCl; trypsin at pH 12.6 and 0.5M KCl; and ${\alpha}-chymotrypsin$ at pH 6.7 and 0.5M KCl. In a test group separation experiments, complete separation of lysozyme from BSA could be obtained.

• Journal of Animal Science and Technology
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• v.45 no.5
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• pp.731-738
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• 2003

The technique known as proteomics is useful for characterizing the protein expression pattern of a particular tissue or cell type as well as quantitatively identifying differences in the levels of individual proteins. In present study, we carried out the comparative expression patterns of white and red muscles. We used the two-dimensional electrophoresis(2-DE) for analyzing the protein expression. Proteins isolated from porcine white and red muscles were separated by 12% poly-acrylamide gel and then were detected by coomassie blue and silver staining. More than 600 protein spots were detected on each 2-DE gel. By visual analysis of the stained gel, five proteins were identified to be differentially expressed in the white vs red muscle. By database searching based on the molecular weights and pI(isoelectric point) of the five proteins, three of them were found to be most close to troponin I, T and myoglobin. However, further researche is needed for identification and functional analysis of the unidentified proteins. In conclusion, we found five proteins, which are differentially expressed in the white vs red muscle. The functional analysis of the differentially expressed proteins will provide valuable information on biochemical characteristics of the muscle type.

• KSBB Journal
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• v.9 no.5
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• pp.483-491
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• 1994

It is known that a key limiting factor to the use of ultrafiltration membranes is that of membrane fouling, which has been a major cause of permeate flux reduction. In this work, the effects of several factors (operating time, protein concentration, temperature and pH, etc.) influencing permeate flux during ultrafiltration of gelatin, casein and bovine serum albumin using a hollow fiber membrane(M. W. 10,000 cut off) reactor have been examined. The permeate flux of gelatin solution was maintained almost constant during the operation up to 6 hours, but those of casein and albumin solutions were decreased to 50% and 43% of initial value after an operation time of 60min. The permeate flux with increasing concentration and temperature of protein solutions increased, but the permeate flux showed a minimum value near the isoelectric point of proteins. The permeate fluxes of protein solution were enhanced by a temperature increase and pH control. Also, it is proposed that fouling can be decreased by the pretreatment of insoluble proteins with enzymes.

• Parasites, Hosts and Diseases
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• v.34 no.1
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• pp.49-58
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• 1996

Characterization of a purified proteinase from T4chomoncs uoginalis was carried out using bacitracin-sepharose affinity chromatography. Trichomonos uqginolis KT-9 isolate was used as a source of eye study Proteinase activity was determined using Bz-Pro- Phe-Arg-Nan as the substrate. Optimum pH for the purified proteinase activity was 7.0 and 6.0, 9.0 with DTT. Optimum temperature was 37℃ and isoelectric point was 7.2 Activity of this proteinase was inhibited by E-64, antipain, leupeptin, Hg2+ and Zn2+ and activated by DTT and cysteine. Activity of the purified proteinase was visualized by gelatin SDS- PAGE. The gelatinolytic activity of the purified proteinase was inhibited by E-64, antipain, leupeptin, and IAA, but not by PMSF and EDTA. On SDS-PAGE, the molecular weight of the purified proteinase was 60,000 daltons. Sera of rabbits infected with T. vaginalis reacted specifically in immunoblots with this proteinase. These results indicate that 60 kDa of purified proteinase was cysteine proteinase with antigenicity.

• Journal of the Korean Chemical Society
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• v.52 no.1
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• pp.57-65
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• 2008

are nanometer or micrometer scale vesicles that can be used as drug delivery carriers. However, plain liposomes are plagued by rapid opsonization, making their circulation time in bloodstream be shortened. In this study, model protein, bovine serum albumin (BSA)-coated liposomes were prepared by coating cationic liposomes with BSA molecules at higher pH than isoelectric point of BSA. The BSA molecules coated on the liposomal surface were denatured by thermal treatment at above 60oC. While both plain and cationic liposomes had about mean particle diameter of 1041 nm, BSA-coated cationic liposomes (BCL) had mean particle diameter of 1091 nm. Encapsulation of model drug, doxorubicin (DOX), in liposomes were carried out by using remote loading method and the loading efficiency of DOX to liposomes was about 90%. The mean particle diameter of BCL did not increase in blood plasma and adsorption of plasma protein was much less than plain or cationic liposomes. These results suggest that BCL can be used as a long-circulating liposomes in bloodstream.

• Journal of the Korean Chemical Society
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• v.7 no.2
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• pp.91-95
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• 1963

The basic studies of adsorption characteristics of collector on monazite were made by electrophoretic measurement and by determination of the adsorption of some typical flotation collectors. By above measurements made on monazite, it is concluded that $H^+\;and\;OH^-$ are identified to act as potential determining ions and thus the electrical properties of monazite is controlled by the pH of the solution. Therefore, anionic collectors are adsorbed on positively charged surfaces and cationic collectors on negatively charged surfaces, which in turn controls the effective flotation condition with respective collectors for this mineral. These results have been correlated with its flotation behavior obtained by Hallimond tube test.

• Korean journal of food and cookery science
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• v.9 no.1
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• pp.43-51
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• 1993

Buckwheat protein isolate was tested for the effects of pH, addition of sodium chloride and heat treatment on solubility, emulsion capacities, emulsion stability, surface hydrophobicity, foam capacities and foam stability. The solubility of buckwheat protein isolate was affected by pH and showed the lowest value at pH 4.5, the isoelectric point of buckwheat protein isolate. The solubility significantly as the pH value reached closer to either ends of the pH, i.e., pH 1.0 and 11.0. The effects of NaCl concentration on solubility were as follows; at pH 2.0, the solubility significantly decreased when NaCl was added; at pH 4.5, it increased above 0.6 M; at pH 7.0 it increased; and at pH 9.0 it decreased. The solubility increased above $80^{\circ}C$, at all pH ranges. The emulsion capacity was the lowest at pH 4.5. It significantly increased as the pH approached higher acidic or alkalic regions. At pH 2.0, when NaCl was added, the emulsion capacity decreased, but it increased at pH 4.5 and showed the maximum value at pH 7.0 and 9.0 with 0.6 M and 0.8 M NaCl concentrations. Upon heating, the emulsion capacity decreased at acidic pH's but was maximised at pH 7.0 and 9.0 on $60^{\circ}C$ heat treatment. The emulsion stability was the lowest at pH 4.5 but increased with heat treatment. At acidic pH, the emulsion stability increased with the increase in NaCl concentration but decreased at pH 7.0 and 9.0. Generally, at other pH ranges, the emulsion stability was decreased with increased heating temperature. The surface hydrophobicity showed the highest value at pH 2.0 and the lowest value at pH 11.0. As NaCl concentrationed, the surface hydrophobicity decreased at acidic pH. The NaCl concentration had no significant effects on surface hydrophobicity at pH 7.0, 9.0 except for the highest value observed at 0.8 M and 0.4 M. At all pH ranges, the surface hydrophobicity was increased, when the temperature increased. The foam capacity decreased, with increased in pH value. At acidic pH, the foam capacity was decreased with the increased in NaCl concentration. The highest value was observed upon adding 0.2 M or 0.4 M NaCl at pH 7.0 and 9.0. Heat treatments of $60^{\circ}C$ and $40^{\circ}C$ showed the highest foam capacity values at pH 2.0 and 4.5, respectively. At pH 7.0 and 9.0, the foam capacity decreased with the increased in temperature. The foam stability was not significantly related to different pH values. The addition of 0.4 M NaCl at pH 2.0, 7.0 and 9.0 showed the highest stability and the addition of 1.0 M at pH 4.5 showed the lowest. The higher the heating temperature, the lower the foam stability at pH 2.0 and 9.0. However, the foam stability increased at pH 4.5 and 7.0 before reaching $80^{\circ}C$.

• Journal of the Mineralogical Society of Korea
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• v.23 no.3
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• pp.235-242
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• 2010

Froth flotation using the residual water in the end of flotation process has been performed through controlling of pH. IEP (isoelectric point) of molybdenite and quartz in distilled water was below pH 3 and pH 2.7, respectively and the stabilized range was pH 5~10. In case of a suspension in reusing water, zeta potential of molybdenite decreased to below -10 mV or less at over pH 4 due to residual flocculants. As result of pH control, flotation efficiency in the alkaline conditions was deteriorated by flocculation, resulting from expanded polymer chain, ion bridge of the divalent metal cations ($Ca^{2+}$), and hydrophobic interactions between the nonpolar site of polymer/the hydrophobic areas of the particle surfaces. However, the weak acid conditions (pH 5.5~6) improved the efficiency of flotation as hydrogen ions neutralize polymer chains and then weakened its function. In cleans after rougher flotation, the Mo grade of 52.7% and recovery of 90.1% could be successfully obtained under the conditions of 20 g/t kerosene, 50 g/t AF65, 300 g/t $Na_2SiO_3$, pH 5.5 and 2 cleaning times. Hence, we developed a technique which can continuously supply waste water filtered from tailings into the grinding-rougher-cleaning processes.