• Journal of the East Asian Society of Dietary Life
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• v.15 no.1
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• pp.78-90
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• 2005

The purpose of this study was to make ramyon from Korean cultured wheat by adding with hot water extract powder from safflower seed in order to add the value of it. The cooking quality, instrumental texture and sensory characteristics of ramyon were analyzed. The ramyons with 0.1%, 0.3%, 0.5%, and 0.7% of hot water extract powder(HEP) from safflower seed, control, and those with 3% and 5% of dried powder(DP) from safflower seed were compared. The yield of HEP was 7.8%. Lightness, redness, Max. weight, strength, hardness, adhesiveness, cohesiveness and springiness were measured. As the amounts of HEP and DP was increasing, ramyons smelled stronger and was getting harder and chewier, while became less transparent and had no difference in elasticity and adhesiveness. In overall acceptability, both control and ramyon with HEP had similar points. From three important factors, appearance, color and smell to make ramyon more acceptable, addition of 0.3～0.5% of hot water extract powder from safflower seed was found to be the best. However, further studies on smells are needed to make processed foodstuffs with safflower seed.

• BMB Reports
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• v.28 no.4
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• pp.348-352
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• 1995

A thermophilic Bacillus sp. strain KK-1 isolated from soil produced an extracellular xylanase. From the culture supernatant of Bacillus sp., the xylanase was purified to homogeneity by ammonium sulfate precipitation and DEAE-Sephadex A-50 chromatography. The molecular weight of the purified xylanase was estimated to be 45 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel permeation chromatography. The apparent $K_m$ values for xylanase, using oat spelt xylan and birchwood xylan as substrates, were 7.1 mg/ml and 3.2 mg/ml, and $V_{max}$ values were $27.0\;{\mu}mol{\cdot}min^{-1}{\cdot}mg^{-1}$ and $29.0\;{\mu}mol{\cdot}min^{-1}{\cdot}mg^{-1}$, respectively. The xylanase hydrolyzed oat spelt xylan to mostly xylobiose, xylotriose, and xylose. The amino acid composition indicated that the xylanase contained high amounts of amino add residues of glutamic acid and glutamine (Glx) and aspartic acid and asparagine (Asx).

• BMB Reports
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• v.30 no.3
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• pp.205-210
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• 1997

p53 tumor suppressor plays an important role in the regulation of cellular proliferation. To identify proteins regulating the expression of p53 in rat liver, we analyzed p53 promoter by electrophoretic mobility shift assay (EMSA) and DNase I footprinting assay. We found that a protein binds the sequence CACGTG, bHLH consensus sequence in rat p53 promoter. Southwestern blotting analysis with oligonucleotides containing this sequence shows that the molecular weight of the protein is 100 kDa. This size is not compatible with the bHLH family such as USF or c-Myc/Max which is known to regulate the expression of the human and mouse p53 gene. Therefore this 100 kDa protein may be a new protein regulating basal transcription of rat p53. We purified this 100 kDa protein through sequence-specific DNA affinity chromatogaphy.

• BMB Reports
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• v.28 no.2
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• pp.149-154
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• 1995

Protein methylase II (S-adenosyl-L-methionine : protein O-methyl-transferase, EC 2.1.1.24; PM II) was purified approximately 1250-fold from porcine testis by fractional precipitation and DEAE-cellulose chromatography, followed by gel filtration on a Sephadex G-75 column and HPLC on a Protein Pak 125 column. The molecular weight of the enzyme was estimated to be 33,000 daltons by SDS-PAGE, which agreed with the value determined by gel filtration. Isoelectric focusing of purified PM II showed a single protein species with an isoelectric point of 6.2. The optimum pH for the reaction was 6.0. The $K_m$ value of the enzyme was $1{\times}10^{-5}M$ with a $V_{max}$ value of 769 pmol/min/mg of enzyme. S-adenosyl-L-homocysteine is a competitive inhibitor of PM II with a $K_i$ value of $1.38{\times}10^{-6}M$.

• Microbiology and Biotechnology Letters
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• v.20 no.1
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• pp.25-33
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• 1992

One acetolactate synthase isozyme which has Rf value of 0.83 on polyacrylamide gel electrophoresis was purified from Sewatia marcescens ATCC 25419 by ammonium sulfate fractionation, DEAE-Sephacel chromatography, Phenyl-Sepharose chromatography, Sephacryt S-400 gel filtration followed by native gel elution. The native molecular weight of the enzyme was determined to be 531,400 by gel filtration method, and SDS-polyacrylamide gel electrophoresis separated the native enzyme into two polypeptides having molecular sizes of 55,000 and 38,900 respectively. In kinetic parameters, $K_m$ value for pyruvate was 2.54 mM, and $V_{max}$ was 21.75 nmoie/min/mg. The enzyme showed maximal activity around pH 8.0 and optimal temperature of the acetolactate formation was $37^{\circ}C$. Feedback inhibition studies indicate that the purified enzyme is rather resistant to branched chain amino acids when compared with acetolactate synthase isozymes of plants or other enterobacteria.

• Journal of the Korean Society of Manufacturing Process Engineers
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• v.10 no.3
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• pp.28-32
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• 2011

The safety of transporting equipment in a cryogenic condition is one of important problems under the circumstances that the application weight of natural gas is gradually increasing. As a larger disaster may be generated by leakage of oil or gas from valves in case of fire occurrence of a ship, the present research applied a numerical analysis method on thermal stress distribution and deformation, etc. to the design of ball valves satisfying fire safety test's specification(API607) to prevent this. In addition, the present research progressed fire safety tests and compared the test result with numerical analysis results. The Max stress by parts was confirmed through thermal analysis of major parts to evaluate safety. The fire safety test was progressed according to the regulation of API607.

• Journal of The Korean Society of Grassland and Forage Science
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• v.16 no.3
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• pp.245-252
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• 1996

This experiment was carried out to investigate the effect of feeding order bay-concentrate-silage, concentratehay- silage, silage-concentrate-hay, silage-concentrate-hay, concentrate-silage-hay) on ruminal characteristics change with 3 fistulated dry Holstein cows in a Latin square design. The main results obtained were as follows : DM intake in forage hayconcentrate-silage feeding order was 1.65% of body weight, which is the highest of all treatments, but that in concentrate-hay-silage 1.4%, which is the lowest. The difference between max and min rumen pH in hayconcentrate-silage feeding order was lowest as 0.55, but there is no significant. The mean rumen $NH_3N$ content in silage-concentrate-hay feeding order was highest as 6.12mg/100ml, but that in silageconcentrate-hay feeding order lowest as 4.82mg/100ml. Acetic acid and propionic acid content was highest in forage hay-concentrate-silage feeding order. but there is no significant. The ratio of acetic acid to propionic acid averaged 3.47~3.69(NS). In conclusion, the best feeding order fitted in ruminal physiology was forage hay-concentrate-silage.

• Journal of Microbiology and Biotechnology
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• v.16 no.7
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• pp.1047-1052
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• 2006

A bile salt hydrolase (BSH) was purified from Lactobacillus plantarum CK 102 and its enzymatic properties were characterized. This enzyme was successfully purified using ion-exchange chromatography with Q-Excellose and hydrophobic interaction chromatography with Butyl-Excellose. The purified enzyme showed a single protein band of 37 kDa by SDS-polyacrylamide gel electrophoresis, which was similar to the molecular weight of known BSHs. The amino acid sequence of GLGLPGDLSSMSR, determined by MALDI-TOF, was identical to that of BSH of L. plantarum WCFS1. Although this BSH hydrolyzed all of the six major human bile salts, glycine-conjugated bile acid was the best substrate, based on its specificity and $K_{m}$ value. Among the various substrates, the purified enzyme maximally hydrolyzed glycocholate with apparent $K_{m}$ and $V_{max}$ values of 0.5 mM and 94 nmol/min/mg, respectively. The optimal pH of the enzyme ranged from 5.8 to 6.3. This enzyme was strongly inhibited by thiol enzyme inhibitors such as iodoacetate and periodic acid.

• Journal of Microbiology and Biotechnology
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• v.25 no.11
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• pp.1928-1935
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• 2015

Microbial growth kinetics is often used to optimize environmental processes owing to its relation to the breakdown of substrate (contaminants). However, the quantification of bacterial populations in the environment is difficult owing to the challenges of monitoring a specific bacterial population within a diverse microbial community. Conventional methods are unable to detect and quantify the growth of individual strains separately in the mixed culture reactor. This work describes a novel quantitative PCR (qPCR)-based genomic approach to quantify each species in mixed culture and interpret its growth kinetics in the mixed system. Batch experiments were performed for both single and dual cultures of Pseudomonas putida and Escherichia coli K12 to obtain Monod kinetic parameters (μ_max and K_s). The growth curves and kinetics obtained by conventional methods (i.e., dry weight measurement and absorbance reading) were compared with that obtained by qPCR assay. We anticipate that the adoption of this qPCR-based genomic assay can contribute significantly to traditional microbial kinetics, modeling practice, and the operation of bioreactors, where handling of complex mixed cultures is required.

• Journal of Applied Biological Chemistry
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• v.48 no.1
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• pp.7-10
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• 2005

Trichoderma sp. SY most effectively produces an extracellular ${\gamma}$-L-arabinofuranosidase (AF) using arabinose as a carbon source. AF grown on cellulose as a carbon source was purified 28-fold with 4.4% yield by DEAE exchange and HQ/20 cation exchange chromatographies The purified enzyme was found to be homogeneous on SDS-PAGE with molecular weight of 89 kDa. It exhibited a high level of activity with p-nitrophenyl ${\alpha}$-L-arabinofuranoside, showing $K_m$ and $V_{max}$ values of $0.15\;{\mu}M$ and $239.85U{\cdot}mg^{-1}$, respectively and did not require any metal ion for activity. It also released p-nitrophenol from p-nitrophenol conjugated ${\beta}$-D-xylopyranoside, and ${\beta}$-D-galactopyranoside not from ${\beta}$-D-glucopyranoside.